{"id":"F2015L00452","name":"Australia New Zealand Food Standards Code – Schedule 18 – Processing aids","slug":"australia-new-zealand-food-standards-code-schedule-18-processing-aids","collection":"legislative_instrument","jurisdiction":"commonwealth","status":"in_force","isInForce":true,"actNumber":null,"makingDate":null,"administeringDepartment":null,"currentVersion":{"id":93062,"registerId":"commonwealth-F2015L00452-current","compilationNumber":null,"startDate":"2026-04-02","status":"InForce","reasons":null,"registeredAt":null},"sections":[{"sectionNumber":"1","sectionType":"section","heading":"Australia New Zealand Food Standards Code – Schedule 18 – Processing aids","content":"Schedule 18 Processing aids\n\nNote 1 This instrument is a standard under the Food Standards Australia New Zealand Act 1991 (Cth). The standards together make up the Australia New Zealand Food Standards Code. See also section 1.1.1—3.\n\nSubstances used as processing aids are regulated by Standard 1.1.1 and Standard 1.3.3. This standard lists substances that may be used as processing aids for paragraph 1.1.2—13(3)(a) and contains permissions to use substances as processing aids for Standard 1.3.3.\n\nNote 2 The provisions of the Code that apply in New Zealand are incorporated in, or adopted under, the Food Act 2014 (NZ). See also section 1.1.1—3.\n\nS18—1 Name\n\nThis Standard is Australia New Zealand Food Standards Code – Schedule 18 – Processing aids.\n\nNote Commencement: \nThis Standard commences on 1 March 2016, being the date specified as the commencement date in notices in the Gazette and the New Zealand Gazette under section 92 of the Food Standards Australia New Zealand Act 1991 (Cth). See also section 93 of that Act.\n\nS18—2 Generally permitted processing aids—substances for section 1.3.3—4\n\n(1) For paragraph 1.3.3—4(2)(b), the substances are:\n\nGenerally permitted processing aids\n\n| activated carbon |\n| ------------------------------------------------------ |\n| ammonia |\n| ammonium hydroxide |\n| argon |\n| bone phosphate |\n| carbon monoxide |\n| diatomaceous earth |\n| ethoxylated fatty alcohols |\n| ethyl alcohol |\n| fatty acid polyalkylene glycol ester |\n| furcellaran |\n| hydrogenated glucose syrups |\n| isopropyl alcohol |\n| magnesium hydroxide |\n| oleic acid |\n| oleyl oleate |\n| oxygen |\n| perlite |\n| phospholipids |\n| phosphoric acid |\n| polyethylene glycols |\n| polyglycerol esters of fatty acids |\n| polyglycerol esters of interesterified ricinoleic acid |\n| polyoxyethylene 40 stearate |\n| potassium hydroxide |\n| propylene glycol alginate |\n| silica or silicates |\n| sodium hydroxide |\n| sodium lauryl sulphate |\n| sulphuric acid |\n| tannic acid |\n\n(2) In this section:\n\nsilica or silicates includes:\n\n(a) sodium calcium polyphosphate silicate; and\n\n(b) sodium hexafluorosilicate; and\n\n(c) sodium metasilicate; and\n\n(d) sodium silicate; and\n\n(e) silica; and\n\n(f) modified silica;\n\nthat complies with a specification in section S3—2 or S3—3.\n\n \n\nNote Silicates that are additives permitted at GMP (see section S16—2) may also be used as processing aids, in accordance with paragraph 1.3.3—4(2)(a).\n\nS18—3 Permitted processing aids for certain purposes\n\nFor section 1.3.3—5, the substances, foods and maximum permitted levels are:\n\nPermitted processing aids for certain purposes (section 1.3.3—5)\n\n```html\n

Substance

Maximum permitted level (mg/kg)

Technological purpose—Antifoam agent

Butanol

10

Oxystearin

GMP

Polydimethylsiloxane

10

Polyethylene glycol dioleate

GMP

Polyethylene/ polypropylene glycol copolymers

GMP

Soap

GMP

Sorbitan monolaurate

1

Sorbitan monooleate

1

Technological purpose—Catalyst

Chromium (excluding chromium VI)

0.1

Copper

0.1

Molybdenum

0.1

Nickel

1.0

Peracetic acid

0.7

Potassium ethoxide

1.0

Potassium (metal)

GMP

Sodium (metal)

GMP

Sodium ethoxide

1.0

Sodium methoxide

1.0

Technological purpose—decolourants, clarifying, filtration and adsorbent agents

Acid clays of montmorillonite

GMP

Chloromethylated aminated styrene‑divinylbenzene resin

GMP

Co-extruded polystyrene and polyvinyl polypyrrolidone

GMP

Copper sulphate

GMP

Dimethylamine-epichlorohydrin copolymer

150

Dimethyldialkylammonium chloride

GMP

Divinylbenzene copolymer

GMP

High density polyethylene co‑extruded with kaolin

GMP

Iron oxide

GMP

Fish collagen, including isinglass

GMP

Magnesium oxide

GMP

Modified polyacrylamide resins

GMP

Nylon

GMP

Phytates (including phytic acid, magnesium phytate & calcium phytate)

GMP

Polyester resins, cross-linked

GMP

Polyethylene

GMP

Polypropylene

GMP

Polyvinyl polypyrrolidone

GMP

Potassium ferrocyanide

0.1

Technological purpose—desiccating preparation

Aluminium sulphate

GMP

Ethyl esters of fatty acids

GMP

Short chain triglycerides

GMP

Technological purpose—ion exchange resin

Completely hydrolysed copolymers of methyl acrylate and divinylbenzene

GMP

Completely hydrolysed terpolymers of methyl acrylate, divinylbenzene and acrylonitrile

GMP

Cross-linked phenol-formaldehyde activated with one or both of the following: triethylene tetramine and tetraethylenepentamine

GMP

Cross-linked polystyrene, chloromethylated, then aminated with trimethylamine, dimethylamine, diethylenetriamine, or dimethylethanolamine

GMP

Diethylenetriamine, triethylene-tetramine, or tetraethylenepentamine cross-linked with epichlorohydrin

GMP

Divinylbenzene copolymer

GMP

Epichlorohydrin cross-linked with ammonia

GMP

Epichlorohydrin cross-linked with ammonia and then quaternised with methyl chloride to contain not more than 18% strong base capacity by weight of total exchange capacity

GMP

Hydrolysed copolymer of methyl acrylate and divinylbenzene

GMP

Methacrylic acid-divinylbenzene copolymer

GMP

Methyl acrylate-divinylbenzene copolymer containing not less than 2% by weight of divinylbenzene, aminolysed with dimethylaminopropylamine

GMP

Methyl acrylate-divinylbenzene copolymer containing not less than 3.5% by weight of divinylbenzene, aminolysed with dimethylaminopropylamine

GMP

Methyl acrylate-divinylbenzene-diethylene glycol divinyl ether terpolymer containing not less than 3.5% by weight divinylbenzene and not more than 0.6% by weight of diethylene glycol divinyl ether, aminolysed with dimethaminopropylamine

GMP

Methyl acrylate-divinylbenzene-diethylene glycol divinyl ether terpolymer containing not less than 7% by weight divinylbenzene and not more than 2.3% by weight of diethylene glycol divinyl ether, aminolysed with dimethaminopropylamine and quaternised with methyl chloride

GMP

Reaction resin of formaldehyde, acetone, and tetraethylenepentamine

GMP

Regenerated cellulose, cross-linked and alkylated with epichlorohydrin and propylene oxide, then derivatised with carboxymethyl groups whereby the amount of epichlorohydrin plus propylene oxide is no more than 70% of the starting amount of cellulose

GMP

Regenerated cellulose, cross-linked and alkylated with epichlorohydrin, then derivatised with tertiary amine groups whereby the amount of epichlorohydrin is no more than 10% of the starting amount of cellulose

GMP

Regenerated cellulose, cross-linked and alkylated with epichlorohydrin and propylene oxide, then derivatised with quaternary amine groups whereby the amount of epichlorohydrin plus propylene oxide is no more than 250% of the starting amount of cellulose

GMP

Regenerated cellulose, cross-linked and alkylated with epichlorohydrin and propylene oxide, then sulphonated, whereby the amount of epichlorohydrin plus propylene oxide employed is no more than 250% of the starting amount of cellulose

GMP

Styrene-divinylbenzene cross-linked copolymer, chloromethylated then aminated with dimethylamine and oxidised with hydrogen peroxide whereby the resin contains not more than 15% of vinyl N,N-dimethylbenzylamine-N-oxide and not more than 6.5% of nitrogen

GMP

Sulphite-modified cross-linked phenol-formaldehyde, with modification resulting in sulphonic acid groups on side chains

GMP

Sulphonated anthracite coal

GMP

Sulphonated copolymer of styrene and divinylbenzene

GMP

Sulphonated terpolymers of styrene, divinylbenzene, and acrylonitrile or methyl acrylate

GMP

Sulphonated tetrapolymer of styrene, divinylbenzene, acrylonitrile, and methyl acrylate derived from a mixture of monomers containing not more than a total of 2% by weight of acrylonitrile and methyl acrylate

GMP

Technological purpose—lubricant, release and anti-stick agent

Acetylated mono- and diglycerides

100

Mineral oil based greases

GMP

Thermally oxidised soya-bean oil

320

White mineral oil

GMP

Technological purpose—carrier, solvent, diluent

Benzyl alcohol

500

Croscarmellose sodium

GMP

Ethyl acetate

GMP

Glycerol diacetate

GMP

Glyceryl monoacetate

GMP

Glycine

GMP

Isopropyl alcohol

1000

L-Leucine

GMP

Triethyl citrate

GMP

\n```\n\nS18—4 Permitted enzymes\n\n(1) For section 1.3.3—6, the enzymes and sources are set out in:\n\n(a) subsection (3) (permitted enzymes of animal origin); and\n\n(b) subsection (4) (permitted enzymes of plant origin); and\n\n(c) subsection (5) (permitted enzymes of microbial origin).\n\n(2) The sources listed in relation to enzymes of microbial origin may contain additional copies of genes from the same organism.\n\nNote 1 EC, followed by a number, means the number the Enzyme Commission uses to classify the principal enzyme activity, which is known as the Enzyme Commission number.\n\nNote 2 ATCC, followed by a number, means the number which the American Type Culture Collection uses to identify a prokaryote.\n\n(3) The permitted enzymes of animal origin are:\n\nPermitted enzymes (section 1.3.3—6)—Enzymes of animal origin\n\n| Enzyme | Source |\n| ------------------------------------ | ----------------------------------------------------------------------------------------------- |\n| Lipase, triacylglycerol (EC 3.1.1.3) | Bovine stomach; salivary glands or forestomach of calf, kid or lamb; porcine or bovine pancreas |\n| Pepsin (EC 3.4.23.1) | Bovine or porcine stomach |\n| Phospholipase A2 (EC 3.1.1.4) | Porcine pancreas |\n| Thrombin (EC 3.4.21.5) | Bovine or porcine blood |\n| Trypsin (EC 3.4.21.4) | Porcine or bovine pancreas |\n\n(4) The permitted enzymes of plant origin are:\n\nPermitted enzymes (section 1.3.3—6)—Enzymes of plant origin\n\n| Enzyme | Source |\n| ------------------------------ | -------------------------------------------- |\n| α-Amylase (EC 3.2.1.1) | Malted cereals |\n| β-Amylase (EC 3.2.1.2) | Sweet potato (Ipomoea batatas)Malted cereals |\n| Actinidin (EC 3.4.22.14) | Kiwifruit (Actinidia deliciosa) |\n| Ficin (EC 3.4.22.3) | Ficus spp. |\n| Fruit bromelain (EC 3.4.22.33) | Pineapple fruit (Ananas comosus) |\n| Papain (EC 3.4.22.2) | Carica papaya |\n| Stem bromelain (EC 3.4.22.32) | Pineapple stem (Ananas comosus) |\n\n(5) The permitted enzymes of microbial origin are:\n\nPermitted enzymes (section 1.3.3—6)—Enzymes of microbial origin\n\n| Enzyme | Source |\n| ------------------------------------------------------------------ | ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- |\n| α-Acetolactate decarboxylase (EC 4.1.1.5) | Bacillus amyloliquefaciensBacillus subtilisBacillus subtilis, containing the gene for α-Acetolactate decarboxylase isolated from Bacillus brevis |\n| Aminopeptidase (EC 3.4.11.1) | Aspergillus oryzaeLactococcus lactis |\n| α-Amylase (EC 3.2.1.1) | Aspergillus nigerAspergillus oryzaeBacillus amyloliquefaciensBacillus licheniformisBacillus licheniformis, containing the gene for α-Amylase isolated from Geobacillus stearothermophilusBacillus subtilisBacillus subtilis, containing the gene for α-Amylase isolated from Geobacillus stearothermophilusGeobacillus stearothermophilus |\n| β-Amylase (EC 3.2.1.2) | Bacillus amyloliquefaciensBacillus subtilis |\n| Amylomaltase (EC 2.4.1.25) | Bacillus amyloliquefaciens, containing the gene for amylomaltase derived from Thermus thermophilus |\n| α-Arabinofuranosidase (EC 3.2.1.55) | Aspergillus niger |\n| Asparaginase (EC 3.5.1.1) | Aspergillus nigerAspergillus oryzaeBacillus subtilis, containing the gene for asparaginase isolated from Pyrococcus furiosus |\n| Aspergillopepsin I (EC 3.4.23.18) | Aspergillus nigerAspergillus oryzae |\n| Aspergillopepsin II (EC 3.4.23.19) | Aspergillus niger |\n| Carboxylesterase (EC 3.1.1.1) | Rhizomucor miehei |\n| Catalase (EC 1.11.1.6) | Aspergillus nigerMicrococcus luteus |\n| Cellulase (EC 3.2.1.4) | Aspergillus nigerPenicillium funiculosumTrichoderma reeseiTrichoderma viride |\n| Chymosin (EC 3.4.23.4) | Aspergillus nigerEscherichia coli K-12 strain GE81Kluyveromyces lactis |\n| Chymotrypsin (EC 3.4.21.1) | Bacillus licheniformis, containing the gene for chymotrypsin isolated from Nocardiopsis prasina |\n| Cyclodextrin glucanotransferase (EC 2.4.1.19) | Paenibacillus macerans |\n| Dextranase (EC 3.2.1.11) | Chaetomium gracilePenicillium lilacinum |\n| Endo-1,4-beta-xylanase (EC 3.2.1.8) | Aspergillus nigerAspergillus oryzaeAspergillus oryzae, containing the gene for Endo-1,4-beta-xylanase isolated from Aspergillus aculeatusAspergillus oryzae, containing the gene for Endo-1,4-beta-xylanase isolated from Thermomyces lanuginosusBacillus amyloliquefaciensBacillus subtilisHumicola insolensTrichoderma reesei |\n| Endo-1,4-beta-xylanase (EC 3.2.1.8) | Bacillus licheniformis, containing the gene for Endo-1,4-beta-xylanase isolated from Bacillus licheniformis |\n| Endo-arabinase (EC 3.2.1.99) | Aspergillus niger |\n| Endo-protease (EC 3.4.21.26) | Aspergillus niger |\n| β-Fructofuranosidase (EC 3.2.1.26) | Aspergillus fijiensis ATCC 20611Aspergillus nigerSaccharomyces cerevisiae |\n| α-Galactosidase (EC 3.2.1.22) | Aspergillus niger |\n| β-Galactosidase (EC 3.2.1.23) | Aspergillus nigerAspergillus oryzaeBacillus circulans ATCC 31382Bacillus licheniformis, containing the gene for β-Galactosidase isolated from Bifidobacterium bifidumKluyveromyces marxianusKluyveromyces lactis |\n| Glucan 1,3-β-glucosidase (EC 3.2.1.58) | Trichoderma harzianum |\n| β-Glucanase (EC 3.2.1.6) | Aspergillus nigerAspergillus oryzaeBacillus amyloliquefaciensBacillus subtilisDisporotrichum dimorphosporumHumicola insolensTalaromyces emersoniiTrichoderma reesei |\n| Glucoamylase (EC 3.2.1.3) | Aspergillus nigerAspergillus oryzaeRhizopus delemarRhizopus oryzaeRhizopus niveus |\n| Glucose oxidase (EC 1.1.3.4) | Aspergillus nigerAspergillus oryzae, containing the gene for glucose oxidase isolated from Aspergillus niger |\n| α-Glucosidase (EC 3.2.1.20) | Aspergillus oryzaeAspergillus niger |\n| β-Glucosidase (EC 3.2.1.21) | Aspergillus niger |\n| Glutaminase (EC 3.5.1.2) | Bacillus amyloliquefaciens |\n| Glycerophospholipid cholesterol acyltransferase (EC 2.3.1.43) | Bacillus licheniformis, containing the gene for glycerophospholipid cholesterol acyltransferase isolated from Aeromonas salmonicida subsp. salmonicida |\n| Hemicellulase endo-1,3-β-xylanase (EC 3.2.1.32) | Humicola insolens |\n| Hemicellulase multicomponent enzyme (EC 3.2.1.78) | Aspergillus nigerBacillus amyloliquefaciensBacillus subtilisTrichoderma reesei |\n| Hexose oxidase (EC 1.1.3.5) | Hansenula polymorpha, containing the gene for Hexose oxidase isolated from Chondrus crispus |\n| Inulinase (EC 3.2.1.7) | Aspergillus niger |\n| Lipase, monoacylglycerol (EC 3.1.1.23) | Penicillium camembertii |\n| Lipase, triacylglycerol (EC 3.1.1.3) | Aspergillus nigerAspergillus oryzaeAspergillus oryzae, containing the gene for Lipase, triacylglycerol isolated from Fusarium oxysporumAspergillus oryzae, containing the gene for Lipase, triacylglycerol isolated from Humicola lanuginosaAspergillus oryzae, containing the gene for Lipase, triacylglycerol isolated from Rhizomucor mieheiCandida rugosaHansenula polymorpha, containing the gene for Lipase, triacylglycerol isolated from Fusarium heterosporumMucor javanicusPenicillium roquefortiiRhizopus arrhizusRhizomucor mieheiRhizopus niveusRhizopus oryzae |\n| Lipase, triacylglycerol (EC 3.1.1.3) | Aspergillus niger, containing the gene for lipase, triacylglycerol isolated from Fusarium culmorum |\n| Lysophospholipase (EC 3.1.1.5) | Aspergillus niger |\n| Maltogenic α-amylase (EC 3.2.1.133) | Bacillus subtilis containing the gene for maltogenic α-amylase isolated from Geobacillus stearothermophilus |\n| Maltotetraohydrolase (EC 3.2.1.60) | Bacillus licheniformis, containing the gene for maltotetraohydrolase isolated from Pseudomonas stutzeri |\n| Metalloproteinase | Aspergillus oryzaeBacillus amyloliquefaciensBacillus coagulansBacillus subtilis |\n| Mucorpepsin (EC 3.4.23.23) | Aspergillus oryzaeAspergillus oryzae, containing the gene for Aspartic proteinase isolated from Rhizomucor meiheiRhizomucor meiheiCryphonectria parasitica |\n| Oryzin (EC 3.4.21.63) | Aspergillus melleus |\n| Pectin lyase (EC 4.2.2.10) | Aspergillus niger |\n| Pectinesterase (EC 3.1.1.11) | Aspergillus nigerAspergillus oryzae, containing the gene for pectinesterase isolated from Aspergillus aculeatus |\n| Phospholipase A1 (EC 3.1.1.32) | Aspergillus oryzae, containing the gene for phospholipase A1 isolated from Fusarium venenatum |\n| Phospholipase A2 (EC 3.1.1.4) | Aspergillus niger, containing the gene isolated from porcine pancreasStreptomyces violaceoruber |\n| 3-Phytase (EC 3.1.3.8) | Aspergillus niger |\n| 4-Phytase (EC 3.1.3.26) | Aspergillus oryzae, containing the gene for 4-phytase isolated from Peniophora lycii |\n| Polygalacturonase or Pectinase multicomponent enzyme (EC 3.2.1.15) | Aspergillus nigerAspergillus oryzaeTrichoderma reesei |\n| Pullulanase (EC 3.2.1.41) | Bacillus acidopullulyticusBacillus amyloliquefaciensBacillus licheniformisBacillus subtilisBacillus subtilis, containing the gene for pullulanase isolated from Bacillus acidopullulyticusKlebsiella pneumoniae |\n| Serine proteinase (EC 3.4.21.14) | Aspergillus oryzaeBacillus amyloliquefaciensBacillus haloduransBacillus licheniformisBacillus subtilis |\n| Transglucosidase (EC 2.4.1.24) | Aspergillus niger |\n| Transglutaminase (EC 2.3.2.13) | Streptomyces mobaraensis |\n| Trypsin (EC 3.4.21.4) | Fusarium venenatum, containing the gene for trypsin isolated from Fusarium oxysporum |\n| Urease (EC 3.5.1.5) | Lactobacillus fermentum |\n| Xylose isomerase (EC 5.3.1.5) | Actinoplanes missouriensisBacillus coagulansMicrobacterium arborescensStreptomyces olivaceusStreptomyces olivochromogenesStreptomyces murinusStreptomyces rubiginosus |\n\nS18—5 Permitted microbial nutrients and microbial nutrient adjuncts\n\nFor section 1.3.3—7, the substances are:\n\nPermitted microbial nutrients and microbial nutrient adjuncts\n\n| adenine |\n| -------------------------- |\n| adonitol |\n| ammonium sulphate |\n| ammonium sulphite |\n| arginine |\n| asparagine |\n| aspartic acid |\n| benzoic acid |\n| biotin |\n| calcium pantothenate |\n| calcium propionate |\n| copper sulphate |\n| cystine |\n| cysteine monohydrochloride |\n| dextran |\n| ferrous sulphate |\n| glutamic acid |\n| glycine |\n| guanine |\n| histidine |\n| hydroxyethyl starch |\n| inosine |\n| inositol |\n| manganese chloride |\n| manganese sulphate |\n| niacin |\n| nitric acid |\n| pantothenic acid |\n| peptone |\n| phytates |\n| polyvinylpyrrolidone |\n| pyridoxine hydrochloride |\n| riboflavin |\n| sodium formate |\n| sodium molybdate |\n| sodium tetraborate |\n| thiamin |\n| threonine |\n| uracil |\n| xanthine |\n| zinc chloride |\n| zinc sulphate |\n\nS18—6 Permitted processing aids for water\n\nFor section 1.3.3—8, the substances and maximum permitted levels are:\n\nPermitted processing aids for water (section 1.3.3—8)\n\n| Substance | Maximum permitted level (mg/kg) |\n| ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- | ------------------------------- |\n| Aluminium sulphate | GMP |\n| Ammonium sulphate | GMP |\n| Calcium hypochlorite | 5 (available chlorine) |\n| Calcium sodium polyphosphate | GMP |\n| Chlorine | 5 (available chlorine) |\n| Chlorine dioxide | 1 (available chlorine) |\n| Cobalt sulphate | 2 |\n| Copper sulphate | 2 |\n| Cross-linked phenol-formaldehyde activated with one or both of triethylenetetramine or tetraethylenepentamine | GMP |\n| Cross-linked polystyrene, first chloromethylated then aminated with trimethylamine, dimethylamine, diethylenetriamine or dimethylethanolamine | GMP |\n| Diethylenetriamine, triethylenetetramine or tetraethylenepentamine cross-linked with epichlorohydrin | GMP |\n| Ferric chloride | GMP |\n| Ferric sulphate | GMP |\n| Ferrous sulphate | GMP |\n| Hydrofluorosilicic acid (fluorosilicic acid) (only in water used as an ingredient in other foods) | 1.5 (as fluoride) |\n| Hydrolysed copolymers of methyl acrylate and divinylbenzene | GMP |\n| Hydrolysed terpolymers of methyl acrylate, divinylbenzene and acrylonitrile | GMP |\n| Hydrogen peroxide | 5 |\n| 1-Hydroxyethylidene-1,1-diphosphonic acid | GMP |\n| Lignosulphonic acid | GMP |\n| Magnetite | GMP |\n| Maleic acid polymers | GMP |\n| Methyl acrylate-divinylbenzene copolymer containing not less than 2% divinylbenzene aminolysed with dimethylaminopropylamine | GMP |\n| Methacrylic acid-divinylbenzene copolymer | GMP |\n| Methyl acrylate-divinylbenzene-diethylene glycol divinyl ether terpolymer containing not less than 3.5% divinylbenzene and not more than 0.6% diethylene glycol divinyl ether, aminolysed with dimethylaminopropylamine | GMP |\n| Modified polyacrylamide resins | GMP |\n| Monobutyl ethers of polyethylene-polypropylene glycol | GMP |\n| Ozone | GMP |\n| Phosphorous acid | GMP |\n| Polyacrylamide (polyelectrolytes) (as acrylamide monomer) | 0.0002 |\n| Polyaluminium chloride | GMP |\n| Polydimethyldiallyl ammonium chloride | GMP |\n| Polyoxypropylene glycol | GMP |\n| Potassium permanganate | GMP |\n| Reaction resin of formaldehyde, acetone and tetraethylenepentamine | GMP |\n| Regenerated cellulose, cross-linked and alkylated with epichlorohydrin and propylene oxide, then sulphonated whereby the amount of epichlorohydrin plus propylene oxide employed is no more than 250% of the starting amount of cellulose | GMP |\n| Silver ions | 0.01 |\n| Sodium aluminate | GMP |\n| Sodium fluoride (only in water used as an ingredient in other foods) | 1.5 (as fluoride) |\n| Sodium fluorosilicate (Sodium silicofluoride) (only in water used as an ingredient in other foods) | 1.5 (as fluoride) |\n| Sodium glucoheptonate | 0.08 (measured as cyanide) |\n| Sodium gluconate | GMP |\n| Sodium humate | GMP |\n| Sodium hypochlorite | 5 (available chlorine) |\n| Sodium lignosulphonate | GMP |\n| Sodium metabisulphite | GMP |\n| Sodium nitrate | 50 (as nitrate) |\n| Sodium polymethacrylate | 2.5 |\n| Sodium sulphite (neutral or alkaline) | GMP |\n| Styrene-divinylbenzene cross-linked copolymer | 0.02 (as styrene) |\n| Sulphonated copolymer of styrene and divinylbenzene | GMP |\n| Sulphonated terpolymers of styrene, divinylbenzene acrylonitrile and methyl acrylate | GMP |\n| Sulphite modified cross-linked phenol-formaldehyde | GMP |\n| Tannin powder extract | GMP |\n| Tetrasodium ethylene diamine tetraacetate | GMP |\n| Zinc sulphate | GMP |\n\nS18—7 Permitted bleaching, washing and peeling agents—various foods\n\nFor section 1.3.3—9, the substances, foods and maximum permitted levels are:\n\nPermitted bleaching, washing and peeling agents (section 1.3.3—9)\n\n| Substance | Food | Maximum permitted level (mg/kg) |\n| ---------------------------------- | --------------------------- | ---------------------------------------------------------------------- |\n| Benzoyl peroxide | All foods | 40 (measured as benzoic acid) |\n| Bromo-chloro-dimethylhydantoin | All foods | 1.0 (available chlorine)1.0 (inorganic bromide)2.0 (dimethylhydantoin) |\n| Calcium hypochlorite | All foods | 1.0 (available chlorine) |\n| Chlorine | All foods | 1.0 (available chlorine) |\n| Chlorine dioxide | All foods | 1.0 (available chlorine) |\n| Diammonium hydrogen orthophosphate | All foods | GMP |\n| Dibromo-dimethylhydantoin | All foods | 2.0 (inorganic bromide)2.0 (dimethylhydantoin) |\n| 2-Ethylhexyl sodium sulphate | All foods | 0.7 |\n| Hydrogen peroxide | All foods | 5 |\n| Iodine | Fruits, vegetables and eggs | GMP |\n| Oxides of nitrogen | All foods | GMP |\n| Ozone | All foods | GMP |\n| Peracetic acid | All foods | GMP |\n| Sodium chlorite | All foods | 1.0 (available chlorine) |\n| Sodium dodecylbenzene sulphonate | All foods | 0.7 |\n| Sodium hypochlorite | All foods | 1.0 (available chlorine) |\n| Sodium laurate | All foods | GMP |\n| Sodium metabisulphite | Root and tuber vegetables | 25 |\n| Sodium peroxide | All foods | 5 |\n| Sodium persulphate | All foods | GMP |\n| Triethanolamine | Dried vine fruit | GMP |\n\nS18—8 Permitted extraction solvents—various foods\n\nFor section 1.3.3—10, the substances, foods and maximum permitted levels are:\n\nPermitted extraction solvents (section 1.3.3—10)\n\n| Substance | Food | Maximum permitted level (mg/kg) |\n| ------------------- | ------------------------------------------------- | ------------------------------- |\n| Acetone | Flavouring substances | 2 |\n| | Other foods | 0.1 |\n| Benzyl alcohol | All foods | GMP |\n| Butane | Flavouring substances | 1 |\n| | Other foods | 0.1 |\n| Butanol | All foods | 10 |\n| Cyclohexane | All foods | 1 |\n| Dibutyl ether | All foods | 2 |\n| Diethyl ether | All foods | 2 |\n| Dimethyl ether | All foods | 2 |\n| Ethyl acetate | All foods | 10 |\n| Glyceryl triacetate | All foods | GMP |\n| Hexanes | All foods | 20 |\n| Isobutane | Flavouring substances | 1 |\n| | Other foods | 0.1 |\n| Methanol | All foods | 5 |\n| Methylene chloride | Decaffeinated coffee | 2 |\n| | Decaffeinated tea | 2 |\n| | Flavouring substances | 2 |\n| Methylethyl ketone | All foods | 2 |\n| 2-Methyloxolane | Infant formula products | 3 |\n| | Foods for infants | 5 |\n| | Formulated supplementary foods for young children | 5 |\n| | All other foods | 20 |\n| Propane | All foods | 1 |\n| Toluene | All foods | 1 |\n\nS18—9 Permitted processing aids—various technological purposes\n\n(1) For section 1.3.3—11, the substances, foods, technological purposes and maximum permitted levels are set out in the table to subsection (3).\n\n(2) In this section:\n\namine agarose ion exchange resin means agarose cross-linked and alkylated with epichlorohydrin and propylene oxide, then derivatised with tertiary amine groups whereby the amount of epichlorohydrin plus propylene oxide does not exceed 250% by weight of the starting amount of agarose.\n\napproved food for use of phage means food that:\n\n(a) is ordinarily consumed in the same state in which it is sold; and\n\n(b) is solid; and\n\n(c) is one of the following:\n\n (i) meat or meat product;\n (ii) fish or fish product;\n (iii) fruit or fruit product;\n (iv) vegetable or vegetable product;\n (v) cheese; and\n\n(d) is not one of the following:\n\n (i) whole nuts in the shell;\n (ii) raw fruits and vegetables that are intended for hulling, peeling or washing by the consumer.\n\nsulphonate agarose ion exchange resin means agarose cross-linked with epichlorohydrin and reacted with allyl glycidyl ether or propylene oxide, then derivatised with sulphonate groups whereby the amount of epichlorohydrin plus allyl glycidyl ether or propylene oxide does not exceed 250% by weight of the starting quantity of agarose.\n\n(3) The table is:\n\nPermitted processing aids—various purposes (section 1.3.3—11)\n\n| Substance | Technological purpose and food | Maximum permitted level (mg/kg) |\n| -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- | ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- | -------------------------------------------------------------------------------- |\n| Amine agarose ion exchange resin | Removal of specific proteins and polyphenols from beer | GMP |\n| Aminopeptidase Y (EC 3.4.11.15) sourced from Trichoderma reesei containing the aminopeptidase Y gene from Aspergillus clavatus | For use in protein processing, yeast processing,and flavour production | GMP |\n| Ammonium bisulphite | For use in the manufacture of wine, sparkling wine and fortified wine as a microbial nutrient and microbial nutrient adjunct. | GMP |\n| Ammonium persulphate | Yeast washing agent | GMP |\n| Ammonium sulphate | Decalcification agent for edible casings | GMP |\n| α-Amylase (EC 3.2.1.1) sourced from Aspergillus niger containing the α-Amylase gene from Rhizomucor pusillus | For use in starch processing and the production of potable alcohol | GMP |\n| α-Amylase (EC 3.2.1.1) sourced from Bacillus licheniformis containing the α-amylase gene from Cytophaga species | For use in:(a) brewing;(b) the production of potable alcohol; and(c) starch processing. | GMP |\n| α-Amylase (EC 3.2.1.1) sourced from Bacillus subtilis containing the α-amylase gene from Thermoactinomyces vulgaris | For use in the manufacture of bakery products | GMP |\n| α-Amylase (EC 3.2.1.1) sourced from Trichoderma reesei containing the α-Amylase gene from Aspergillus kawachii | For use in brewing and the production of potable alcohol. | GMP |\n| β-Amylase (EC 3.2.1.2) sourced from soybean (Glycine max) | For use in starch processing to manufacture maltose syrup | GMP |\n| β-Amylase (EC 3.2.1.2) sourced from Bacillus licheniformis containing the β-amylase gene from Priestia flexa (basionym Bacillus flexus) | For use in starch processing to manufacture maltose syrup | GMP |\n| α-Arabinofuranosidase (EC 3.2.1.55) sourced from Trichoderma reesei containing the α-arabinofuranosidase gene from Talaromyces pinophilus | For use in:grain processing; andthe production of potable alcohol. | GMP |\n| Aqualysin 1 (EC 3.4.21.111) sourced from Bacillus subtilis containing the aqualysin 1 gene from Thermus aquaticus | For use in the manufacture of bakery products | GMP |\n| Aspergillopepsin I (EC 3.4.23.18) sourced from Trichoderma reesei containing the gene for aspergillopepsin I isolated from Trichoderma reesei | For use in the manufacture of potable alcohol and of animal and vegetable protein products. | GMP |\n| Butanol | Suspension agent for sugar crystals | 10 |\n| Carbonic acid | Bleached tripe washing agent | GMP |\n| Carboxypeptidase (EC 3.4.16.6) sourced from Aspergillus oryzae containing the carboxypeptidase gene from Aspergillus oryzae | For use inbrewing; andthe manufacture of bakery products; andthe manufacture and/or processing of the following types of food:flavourings; andproteins; andyeast. | GMP |\n| Cellulase (EC 3.2.1.4) sourced from Aspergillus niger containing the cellulase gene from Trichoderma reesei | For use in brewing and the production of potable alcohol | GMP |\n| Cetyl alcohol | Coating agent on meat carcasses and primal cuts to prevent desiccation | 1.0 |\n| Chitin-glucan | For use in the manufacture of wine, sparkling wine and fortified wine as a decolourant, clarifying, filtration and absorbent agent. | GMP |\n| Chitosan sourced from Aspergillus niger | Manufacture of wine, beer, cider, spirits and food grade ethanol | GMP |\n| Chymosin (EC 3.4.23.4) sourced from Trichoderma reesei containing the chymosin gene from Bos taurus | For use in the manufacture of cheese, cheese products, fermented milk products and rennetted milk products. | GMP |\n| A colouring that is an additive permitted at GMP, a colouring permitted at GMP, or a colouring permitted to a maximum level | Applied to the outer surface of meat as a brand for the purposes of inspection or identification | GMP |\n| Cupric citrate | Removal of sulphide compounds from wine | GMP |\n| β-Cyclodextrin | Used to extract cholesterol from eggs | GMP |\n| β-Galactosidase (EC 3.2.1.23) from Papiliotrema terrestris strain AE‑BLC | For use in the production of *galacto‑oligosaccharides from lactose. | GMP |\n| β-Galactosidase (EC 3.2.1.23) sourced from Bacillus subtilis containing the gene for β-galactosidase isolated from Bifidobacterium bifidum. | For use in the production of lactose reduced dairy foods and for the production of galacto-oligosaccharides. | GMP |\n| β-Galactosidase (EC 3.2.1.23) sourced from Bacillus subtilis containing the β-galactosidase gene from Lactobacillus delbrueckii subsp. bulgaricus | For use in the production of lactose reduced dairy foods. | GMP |\n| L-Cysteine (or HCl salt) | Dough conditioner | 75 |\n| Endo-1,4-beta-xylanase (EC 3.2.1.8) from Bacillus subtilis, containing the gene for Endo-1,4-beta-xylanase isolated from Pseudoalteromonas haloplanktis. | For use in the manufacture of bakery and other cereal-based products. | GMP |\n| Endo-1,4-ß-xylanase (EC 3.2.1.8) from Trichoderma reesei, containing the gene for endo-1,4-ß-xylanase isolated from Thermopolyspora flexuosa | For depolymerisation of arabinoxylans during the manufacture and/or processing of the following types of food:(a) bakery products;(b) cereal products;(c) grain;(d) cereal based beverages (including beer); and(e) potable alcohol | GMP |\n| Endo-1,4-beta-xylanase (EC 3.2.1.8) sourced from Trichoderma reesei containing the endo-1,4-beta-xylanase gene from Aspergillus niger. | For use in the manufacture of bakery and other cereal-based products, including cereal-based beverages | GMP |\n| Endo-1,4-β-xylanase (EC 3.2.1.8) sourced from Trichoderma reesei, containing the endo-1,4-ß-xylanase gene from Fusarium verticillioides | For use in starch processing and the production of potable alcohol | GMP |\n| Endo-1,4-beta-xylanase (EC 3.2.1.8) sourced from Trichoderma reesei containing the endo-1,4-beta-xylanase gene from Talaromyces leycettanus | For use in:brewing; andfats and oils processing; andgrain processing; andthe production of potable alcohol. | GMP |\n| Enzyme that:(a) contains both of the following components -(i) UDP‑glucosyltransferase; and(ii) sucrose synthase (EC 2.4.1.13); and(b) is sourced from Pichia pastoris strain UGT-A. | For the conversion of purified stevia leaf extract to produce rebaudioside E. | GMP |\n| Enzyme that: contains both UDP‑glucosyltransferase and sucrose synthase (EC 2.4.1.13) components; and is sourced from Pichia pastoris strain UGT-A. | For the conversion of purified stevia leaf extract to produce rebaudioside D. | GMP |\n| Enzymes that: contain both UDP-glucosyltransferase and sucrose synthase (EC 2.4.1.13) components; and are sourced from both of the following; a Pichia pastoris strain expressing UGT-A, and a Pichia pastoris strain expressing both UGT-B1 and UGT-B2. | For the conversion of purified stevia leaf extract to produce rebaudioside M | GMP |\n| Ethyl acetate | Cell disruption of yeast | GMP |\n| Ethylene diamine tetraacetic acid | Metal sequestrant for edible fats and oils and related products | GMP |\n| Fructan β-fructosidase (EC 3.2.1.80) sourced from Trichoderma reesei containing the fructan β-fructosidase gene from Lactobacillus crispatus | For use in the manufacture of bakery products | GMP |\n| β-Fructofuranosidase (EC 3.2.1.26) sourced from Trichoderma reesei containing the β-fructofuranosidase gene from Aspergillus niger | For use in the production of short-chain fructooligosaccharides; and to produce a reduction in sugar levels in treated fruit and vegetable products | GMP |\n| Fructosyltransferase, immobilised, (EC 2.4.1.9) derived from Aspergillus oryzae | For use in the manufacture of short-chain fructooligosaccharides from sucrose | GMP |\n| Gibberellic acid | Barley germination | GMP |\n| Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Gloeophyllum sepiarium | For use in:baking;brewing;the production of distilled alcohol; and(d) starch processing for the production of glucose syrups and other starch hydrolysates. | GMP |\n| Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Penicillium oxalicum | For use in:(a) the manufacture of bakery products;(b) brewing; and(c) starch processing for the production of starch hydrolysates, including glucose syrups. | GMP |\n| Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the gene for glucoamylase isolated from Talaromyces emersonii | To hydrolyse starch in the manufacture of syrups, beverages, cereal-based products, fruit products and vegetable products | GMP |\n| Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Trametes cingulata | For use in starch processing and the production of potable alcohol | GMP |\n| Glucoamylase (EC 3.2.1.3) sourced from Trichoderma reesei containing the glucoamylase gene from Trichoderma reesei | For use in:(a) brewing;(b) the manufacture of bakery products;(c) the production of potable alcohol; and(d) starch processing. | GMP |\n| Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Gloeophyllum trabeum | For use in starch processing and the production of potable alcohol | GMP |\n| α-Glucosidase (EC 3.2.1.20) sourced from Trichoderma reesei containing the α‑glucosidase gene from Aspergillus niger | For use in the manufacture and/or processing of the following types of food:potable alcohol;lysine;organic acids;monosodium glutamate and other biochemicals; andisomalto-oligosaccharides and other sweeteners andbeer. | GMP |\n| Glucose oxidase (EC 1.1.3.4) sourced from Trichoderma reesei containing the glucose oxidase gene from Penicillium amagasakiense | For use in:the manufacture of bakery and other cereal-based products; andegg processing. | GMP |\n| Glucose oxidase (EC 1.1.3.4) sourced from Penicillium rubens | For use in the manufacture of:(a) cooked products made from a dough including bread;(b) pasta;(c) noodles; and(d) dried egg powder. | GMP |\n| Gluteral | Manufacture of edible collagen casings | GMP |\n| Hydrogen peroxide | Control of lactic acid producing microorganisms to stabilise the pH during the manufacture of:(a) fermented milk;(b) fermented milk products;(c) cheese made using lactic acid producing microorganisms; or(d) cheese products made using lactic acid producing microorganisms | 5 |\n| | Inhibiting agent for dried vine fruits, fruit and vegetable juices, sugar, vinegar and yeast autolysate | 5 |\n| | Removal of glucose from egg | 5 |\n| | Removal of sulphur dioxide | 5 |\n| 1-Hydroxyethylidene-1, 1-diphosphonic acid | Metal sequestrant for use with antimicrobial agents for meat, fruit and vegetables | GMP |\n| Ice Structuring Protein type III HPLC 12 | Manufacture of ice cream and edible ices | 100 |\n| Indole acetic acid | Barley germination | GMP |\n| Inulinase (EC 3.2.1.7) sourced from Aspergillus oryzae containing the inulinase gene from Aspergillus ficuum | Hydrolysing inulin to produce fructo‑oligosaccharides | GMP |\n| Lactoperoxidase from bovine milk EC 1.11.1.7 | Reduce the bacterial population or inhibit bacterial growth on meat surfaces | GMP |\n| Lipase, triacylglycerol (EC 3.1.1.3) sourced from Candida cylindracea | For use in the manufacture of bakery products and dairy products and in the processing of fats and oils. | GMP |\n| Lipase, triacylglycerol (EC 3.1.1.3) sourced from Komagataella phaffii containing the lipase, triacylglycerol gene from Fusarium oxysporum | For use in the manufacture of bread and bakery products. | GMP |\n| Lipase, triacylglycerol (EC 3.1.1.3) sourced from Trichoderma reesei containing the gene for lipase, triacylglycerol isolated from Aspergillus tubingensis | For use in the production of bakery products, and cereal-based beverages and foods. | GMP |\n| Lipase, triacylglycerol (EC 3.1.1.3) sourced from Trichoderma reesei containing the gene for lipase, triacylglycerol isolated from Fusarium oxysporum | For use in the manufacture of bakery and other cereal-based products | GMP |\n| Listeria phage P100 | Listericidal treatment for use on approved food for use of phage | GMP |\n| Lysophospholipase (EC 3.1.1.5) sourced from Trichoderma reesei containing the gene for lysophospholipase isolated from Aspergillus nishimurae | For use in starch processing, including the production of syrups | GMP |\n| Maltogenic α-Amylase (EC 3.2.1.133) sourced from Escherichia coli containing the maltogenic α-Amylase gene from Geobacillus stearothermophilus | For use in baking, brewing and starch processing | GMP |\n| Lipase, triacylglycerol (EC 3.1.1.3) sourced from Trichoderma reesei containing the lipase, triacylglycerol gene from Thermomyces lanuginosus | For use in the manufacture of bakery and other cereal-based products | GMP |\n| Maltogenic α-amylase (EC 3.2.1.133) sourced from Saccharomyces cerevisiae containing the gene for maltogenic α-amylase from Geobacillus stearothermophilus | For use in the manufacture of bakery products | GMP |\n| Maltogenic α-amylase (EC 3.2.1.133) sourced from Bacillus licheniformis containing the gene for maltogenic α-amylase from Geobacillus stearothermophilus. | For use in:brewing;the manufacture of bakery products;the production of potable alcohol; and;starch processing. | GMP |\n| Morpholine | Solubilising agent for coating mixtures on fruits | GMP |\n| Oak | For use in the manufacture of wine | GMP |\n| Octanoic acid | Antimicrobial agent for meat, fruit and vegetables | GMP |\n| Paraffin | Coatings for cheese and cheese products | GMP |\n| Pectinesterase (EC 3.1.1.11) sourced from Aspergillus oryzae containing the pectinesterase gene from Aspergillus tubingensis | For use during the manufacture and/or processing of the following types of food:coffee;fruit and vegetable juices;fruit and vegetable products;wine; andflavouring substances. | GMP |\n| Phosphoinositide phospholipase C (EC 3.1.4.11) sourced from Bacillus licheniformis containing the phosphoinositide phospholipase C gene from Pseudomonas sp. 62186 | For use in degumming vegetable fats and oils | GMP |\n| Phospholipase A1 (EC 3.1.1.32) sourced from Aspergillus oryzae containing the phospholipase A1 gene from Valsaria rubricosa | For use in the manufacture of bakery products | GMP |\n| Phospholipase A1 (EC 3.1.1.32) sourced from Aspergillus niger containing the phospholipase A1 gene from Evansstolkia leycettana (basionym Talaromyces leycettanus) | For use in the degumming of vegetable oils | GMP |\n| Phospholipase C (EC 3.1.4.3) sourced from Bacillus licheniformis containing the gene for phospholipase C from Bacillus thuringiensis | For use in degumming vegetable fats and oils | GMP |\n| Polygalacturonase (EC 3.2.1.15) sourced from Aspergillus oryzae containing the polygalacturonase gene from Aspergillus tubingensi | For use during the manufacture and/or processing of the following types of food:(a) coffee;(b) fruit and vegetable juices;(c) fruit and vegetable products;(d) wine; and(e) flavouring substances. | GMP |\n| Polyvinyl acetate | Preparation of waxes for use in cheese and cheese products | GMP |\n| Polyvinylimidazole-polyvinylpyrrolidone co-polymers | For use in the manufacture of wine, sparkling wine and fortified wine as a decolourant, clarifying, filtration and absorbent agent. | GMP |\n| Potassium bromate | Germination control in malting | Limit of determination of bromate |\n| Prolyl oligopeptidase (EC 3.4.21.26) sourced from Trichoderma reesei containing the prolyl oligopeptidase gene from Aspergillus niger | For use in brewing | GMP |\n| Protein glutaminase (EC 3.5.1.44) sourced from Chryseobacterium proteolyticum strain AE-PG | To deamidate proteins during the manufacture and/or processing of the following types of food:baked products;pasta;noodles;milk;other dairy products;meat;fish;grains;yeast; andegg based products. | GMP |\n| D-psicose 3-epimerase (EC 5.1.3.30) from Microbacterium foliorum | For use in the manufacture of D-allulose | GMP |\n| Pullulanase (EC 3.2.1.41) sourced from Bacillus licheniformis containing the pullulanase gene from Bacillus deramificans. | For use in brewing and in starch processing. | GMP |\n| Pullulanase (EC 3.2.1.41) sourced from Bacillus subtilis containing the pullulanase gene from Bacillus deramificans | For use in starch processing for production of glucose syrups and other starch hydrolysates | GMP |\n| Salmonella phage preparation (S16 and FO1a) | Reduce population of Salmonella species on the surface of raw meat and raw poultry meat during processing. | GMP |\n| Silver chloride | For use in the manufacture of wine, sparkling wine and fortified wine to remove fermentation and storage-related odours. | GMP |\n| Sodium bromate | Germination control in malting | Limit of determination of bromate |\n| Sodium chlorite | Antimicrobial agent for meat, fish, fruit and vegetables | Limit of determination of chlorite, chlorate, chlorous acid and chlorine dioxide |\n| Sodium gluconate | Denuding, bleaching & neutralising tripe | GMP |\n| Sodium glycerophosphate | Cryoprotectant for starter culture | GMP |\n| Sodium metabisulphite | Dough conditioner | 60 |\n| | Removal of excess chlorine | 60 |\n| | Softening of corn kernels for starch manufacture | 60 (in the starch) |\n| | Treatment of hides for use in gelatine and collagen manufacture | GMP |\n| Sodium sulphide | Treatment of hides for use in gelatine and collagen manufacture | GMP |\n| Sodium sulphite | Dough conditioner | 60 |\n| Sodium thiocyanate | Reduce and/or inhibit bacterial population on meat surfaces | GMP |\n| Stearyl alcohol | Coating agent on meat carcasses and primal cuts to prevent desiccation | GMP |\n| Subtilisin (EC 3.4.21.62) sourced from Bacillus licheniformis containing the gene for subtilisin from Pyrococcus furiosus | For use in the production of potable alcohol. | GMP |\n| Subtilisin (EC 3.4.21.62) sourced from Bacillus subtilis containing the gene for subtilisin from Bacillus clausii | For use in hydrolysing proteins in foods containing proteins. | GMP |\n| Sucrose synthase (EC 2.4.1.13) sourced from Escherichia coli BL21 containing the gene for sucrose synthase from Arabidopsis thaliana | For the conversion of purified stevia leaf extract to produce rebaudioside M | GMP |\n| Sucrose synthase (EC 2.4.1.13) sourced from Escherichia coli K-12 containing the gene for sucrose synthase from Arabidopsis thaliana | For the conversion of purified stevia leaf extract to produce one or more of the following: rebaudioside D, rebaudioside M; and rebaudioside AM | GMP |\n| Sucrose synthase (EC 2.4.1.13) sourced from Escherichia coli K-12 containing the gene for sucrose synthase from Glycine max | For the conversion of purified stevia leaf extract to produce one or more of the following: rebaudioside I and rebaudioside M | GMP |\n| Sulphonate agarose ion exchange resin | Production of lactoferrin from bovine milk and milk-related products | GMP |\n| Sulphur dioxide | Control of nitrosodimethylamine in malting | 750 |\n| | Treatment of hides for use in gelatine and collagen manufacture | 750 |\n| Sulphurous acid | Softening of corn kernels | GMP |\n| | Treatment of hides for use in gelatine and collagen manufacture | GMP |\n| Thermolysin (EC 3.4.24.27) sourced from Anoxybacillus caldiproteolyticus Rokko | For protein hydrolysis during:(a) beer brewing; and(b) the manufacture and/or processing of the following types of food:(i) dairy;(ii) eggs;(iii) meat;(iv) fish;(v) protein concentrates and isolates; and(vi) yeast. | GMP |\n| Thermolysin (EC 3.4.24.27) sourced from Anoxybacillus caldiproteolyticus strain TP-7 | To catalyse the hydrolysis of peptide bonds during the manufacture and/or processing of the following types of food:dairy;egg;meat;fish;protein;yeast; andflavouring | GMP |\n| Thermomycolin (EC 3.4.21.65) sourced from Trichoderma reesei containing the thermomycolin gene from Malbranchea cinnamomea | To catalyse the hydrolysis of peptide bonds during the manufacture and/or processing of the following types of food:meat products;vegetable products; andseafood products. | GMP |\n| Transglutaminase (EC 2.3.2.13) sourced from Bacillus licheniformis containing the transglutaminase gene from Streptomyces mobaraensis | For use inbrewing; andin the manufacture and/or processing of the following types of food:bakery and other cereal-based products, including pasta and noodles;cheese;meat products;fish products;fermented dairy products;egg substitutes;dairy analogues;meat analogues; andfish analogues | GMP |\n| Triethanolamine | Solubilising agent for coating mixtures for fruits | GMP |\n| Urea | Manufacture of concentrated gelatine solutions | 1.5 times the mass of the gelatine present |\n| | Microbial nutrient and microbial nutrient adjunct for the manufacture of all foods, except alcoholic beverages | GMP |\n| Uridine diphosphate (UDP) glucosyltransferases sourced from Escherichia coli BL21 containing the UDP glucosyltransferase gene from Stevia rebaudiana | For the conversion of purified stevia leaf extract to produce rebaudioside M | GMP |\n| Uridine diphosphate (UDP)- glucosyltransferase sourced from Escherichia coli K-12 containing the UDP-glucosyltransferase gene from Oryza sativa | For the conversion of purified stevia leaf extract to produce rebaudioside M | GMP |\n| Uridine diphosphate (UDP) glucosyltransferase sourced from Escherichia coli K-12 containing the UDP glucosyltransferase gene from Solanum lycopersicum | For the conversion of purified stevia leaf extract to produce one or more of the following: rebaudioside D, rebaudioside M; and rebaudioside AM | GMP |\n| Uridine diphosphate (UDP) glucosyltransferase sourced from Escherichia coli K-12 containing the UDP glucosyltransferase gene from Stevia rebaudiana | For the conversion of purified stevia leaf extract to produce one or more of the following: rebaudioside D, rebaudioside M; and rebaudioside AM | GMP |\n| Uridine triphosphate (UTP)-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) sourced from Escherichia coli K-12, containing the gene for UTP-glucose-1-phosphate uridylyltransferase from Bifidobacterium bifidum | For the conversion of purified stevia leaf extract to produce one or more of the following: rebaudioside I and rebaudioside M | GMP |\n| Woodflour from untreated Pinus radiata | Gripping agent used in the treatment of hides | GMP |\n\nS18—10 Permission to use dimethyl dicarbonate as microbial control agent\n\nFor section 1.3.3—12, the foods and maximum permitted addition levels are:\n\nPermission to use dimethyl dicarbonate as microbial control agent (section 1.3.3—12)\n\n| Food | Maximum permitted addition level |\n| ------------------------------------------- | -------------------------------- |\n| Any of the following: | 250 mg/kg |\n| (a) fruit juice; | |\n| (b) vegetable juice; | |\n| (c) fruit juice product; | |\n| (d) vegetable juice product. | |\n| Water based flavoured drinks | 250 mg/kg |\n| Formulated beverages | 250 mg/kg |\n| Any of the following: | 200 mg/kg |\n| (a) wine | |\n| (b) sparkling wine; | |\n| (c) fortified wine; | |\n| (d) fruit wine (including cider and perry); | |\n| (e) vegetable wine; | |\n| (f) mead | |\n\nS18—11 Permission to use cetylpyridinium chloride as an antimicrobial agent\n\n1. For section 1.3.3—13, the food, maximum permitted levels and conditions are set out in the table to subsection (3).\n2. In this section:\n\nPoultry meat means the whole or any part of a poultry carcass which:\n\n1. has skin attached; and\n2. is intended for human consumption; and\n3. is not, or does not include, offal.\n\nNote Subsection 1.1.2—3(2) defines ‘offal’.\n\n1. The table is:\n\nPermission to use cetylpyridinium chloride as an antimicrobial agent (section 1.3.3—13)\n\n| Food | Maximum permitted level (mg/kg) | Conditions of use |\n| ---------------- | ------------------------------- | ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- |\n| Raw poultry meat | 13.4 (in the skin) | (1) The concentration of cetylpyridinium chloride in the aqueous wash solution that is applied to the raw poultry meat must not exceed 1% w/v.(2) The raw poultry meat, after being treated with cetylpyridinium chloride, must be rinsed in potable water. |\n\n\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\\_\n\n \n\nAmendment History\n\nThe Amendment History provides information about each amendment to the Schedule. The information includes commencement or cessation information for relevant amendments.\n\nThese amendments are made under section 92 of the Food Standards Australia New Zealand Act 1991 unless otherwise indicated. Amendments do not have a specific date for cessation unless indicated as such.\n\nAbout this compilation\n\nThis is compilation No. 52 of Schedule 18 as in force on 26 February 2026 (up to Amendment No. 246). It includes any commenced amendment affecting the compilation to that date.\n\nPrepared by Food Standards Australia New Zealand on 26 February 2026.\n\nUncommenced amendments or provisions ceasing to have effect\n\nTo assist stakeholders, the effect of any uncommenced amendments or provisions which will cease to have effect, may be reflected in the Schedule as shaded boxed text with the relevant commencement or cessation date. These amendments will be reflected in a compilation registered on the Federal Register of Legislation including or omitting those amendments and provided in the Amendment History once the date is passed.\n\nThe following abbreviations may be used in the table below:\n\nad = added or inserted am = amended\n\nexp = expired or ceased to have effect rep = repealed\n\nrs = repealed and substituted\n\nSchedule 18 was published in the Food Standards Gazette No. FSC96 on 10 April 2015 as part of Amendment 154 (F2015L00452 –- 1 April 2015) and has since been amended as follows:\n\n```html\n

Section affected

A’ment No.

FRL registration

Gazette

Commencement

(Cessation)

How affected

Description of amendment

S18—3

161

F2016L00120

18 Feb 2016

FSC103

22 Feb 2016

1 March 2016

am

Correction of spelling of tetraethylenepentamine.

S18—3

168

F2017L00414

11 April 2017

FSC110

13 April 2017

13 April 2017

rs

Omission of an inadvertent duplication of the entry for ion exchange resin regenerated cellulose, cross-linked and alkylated with epichlorohydrin and propylene oxide and replacement with correct text.

S18—4(5)

156

F2015L01227

6 Aug 2015

FSC98

6 Aug 2015

1 March 2016

ad

Entry for chymotrypsin.

S18—4(5)

156

F2015L01228

6 Aug 2015

FSC98

6 Aug 2015

1 March 2016

ad

Entry for trypsin.

S18—4(5)

157

F2015L01374

1 Sept 2015

FSC99

3 Sept 2015

1 March 2016

am

Entry for aspergillopepsin I previously included in the Code as part of A1091.

S18—4(5)

157

F2015L01374

1 Sept 2015

FSC99

3 Sept 2015

1 March 2016

ad

Entries for endo-1,4-beta-xylanase (EC 3.2.1.8) and endo-1,4-beta-xylanase, protein engineered variant (EC 3.2.1.8) previously included in the Code as part of A1096.

S18—4(5)

157

F2015L01374

1 Sept 2015

FSC99

3 Sept 2015

1 March 2016

rep

Entry for hemicellulase endo-1,4-β-xylanase previously included in the Code as part of A1096.

S18—4(5)

159

F2015L01919

2 Dec 2015

FSC101

7 Dec 2015

1 March 2016

rs

Entry for asparaginase.

S18—4(5)

164

F2016L01199

20 July 2016

FSC106

21 July 2016

21 July 2016

ad

Entry for glutaminase.

S18—4(5)

170

F2017L00583

23 May 2017

FSC112

25 May 2017

25 May 2017

ad

Entry for oryzin.

S18—4(5)

172

F2017L01136

5 Sept 2017

FSC114

7 Sept 2017

7 Sept 2017

am

Entry for β-Galactosidase (EC 3.2.1.23).

S18—9(2)

164

F2016L01204

20 July 2016

FSC106

21 July 2016

21 July 2016

rs

Replace definition of ‘agarose ion exchange resin’ with definitions of ‘amine agarose ion exchange resin’ and sulphonate agarose ion exchange resin’.

S18—9(3)

163

F2016L00787

12 May 2016

FSC105

19 May 2016

19 May 2016

ad

Entry for Salmonella phage preparation (S16 and FO1a).

S18—9(3)

164

F2016L01204

20 July 2016

FSC106

21 July 2016

21 July 2016

rs

Reference to agarose ion exchange resin replaced with amine agarose ion exchange resin.

S18—9(3)

164

F2016L01204

20 July 2016

FSC106

21 July 2016

21 July 2016

ad

Entry for sulphonate agarose ion exchange resin.

S18—9(3)

168

F2017L00414

11 April 2017

FSC110

13 April 2017

13 April 2017

am

Correction of formatting errors for potassium bromate and sodium bromate.

S18—9(3)

172

F2017L01138

6 Sept 2017

FSC114

7 Sept 2017

7 September 2017

ad

Entry for Endo-1,4-beta-xylanase (EC 3.2.1.8) from Bacillus subtilis, containing the gene for Endo-1,4-beta-xylanase isolated from Pseudoalteromonas haloplanktis

S18—9(3)

174

F2017L01389

24 Oct 2017

FSC115

26 Oct 2017

26 October 2017

ad

Entry for ammonium bisulphite, chitin-glucan, polyvinylimidazole-polyvinylpyrrolidone co-polymers and silver chloride

S18—9(3)

176

F2018L00033

10 Jan 2018

FSC117

11 Jan 2018

11 January 2018

ad

Entry for Lipase, triacylglycerol (EC 3.1.1.3) sourced from Candida cylindracea

S18—9(3)

176

F2018L00035

10 Jan 2018

FSC117

11 Jan 2018

11 January 2018

ad

Entry for Aqualysin 1 (EC 3.4.21.111) sourced from Bacillus subtilis containing the aqualysin 1 gene from Thermus aquaticus

S18—9(3)

178

F2018L00578

3 May 2018

FSC119

3 May 2018

3 May 2018

ad

Entry for Protein glutaminase (EC 3.5.1.44) sourced from Chryseobacterium proteolyticum strain AE-PG

S18—9(3)

180

F2018L01148

21 Aug 2018

FSC 121

23 Aug 2018

23 August 2018

ad

Entry for β-Galactosidase (EC 3.2.1.23) from Papiliotrema terrestris strain AE‑BLC.

S18—9(3)

180

F2018L01147

21 Aug 2018

FSC 121

23 Aug 2018

23 August 2018

ad

Entry for Endo-1,4-ß-xylanase, protein engineered variant, (EC 3.2.1.8) from Trichoderma reesei, containing the gene for endo-1,4-ß-xylanase isolated from Thermopolyspora flexuosa

S18—9(3)

181

F2018L01445

18 Oct 2018

FSC 122

23 Oct 2018

23 October 2018

ad

Entry for Thermolysin (EC 3.4.24.27) sourced from Anoxybacillus caldiproteolyticus strain TP-7

S18—9(3)

182

F2018L01594

23 Nov 2018

FSC123

29 Nov 2018

29 Nov 2018

am

Corrections typographical errors, Dimethyldialkylammonium chloride, Technological purpose and Maximum permitted and food level (mg/kg) headings

S18—9(3)

183

F2019L00039

11 Jan 2019

FSC124

23 Jan 2019

23 January 2019

ad

Entry for Protein engineered enzymes that: contain both UDP-glucosyltransferase (EC 2.4.1.17) and sucrose synthase (EC 2.4.1.13) components; and are sourced from both of the following; a Pichia pastoris strain expressing UGT-A, and a Pichia pastoris strain expressing both UGT-B1 and UGT-B2.

S18—9(3)

185

F2019L00704

30 May 2019

FSC126

6 June 2019

6 June 2019

ad

Entry for Lipase, triacylglycerol (EC 3.1.1.3) sourced from Trichoderma reesei containing the gene for lipase, triacylglycerol isolated from Fusarium oxysporum

S18—9(3)

185

F2019L00709

30 May 2019

FSC126

6 June 2019

6 June 2019

ad

Entry for Lysophospholipase (EC 3.1.1.5) sourced from Trichoderma reesei containing the gene for lysophospholipase isolated from Aspergillus nishimurae

S18—9(3)

185

F2019L00712

30 May 2019

FSC126

6 June 2019

6 June 2019

ad

Entry for β-Galactosidase (EC 3.2.1.23) sourced from Bacillus subtilis containing the gene for β-galactosidase isolated from Bifidobacterium bifidum.

S18—9(3)

186

F2019L00995

17 July 2019

FSC127

25 July 2019

25 July 2019

ad

Entry for Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the gene for glucoamylase isolated from Talaromyces emersonii

S18—9(3)

187

F2019L01137

12 May 2020

FSC133

14 May 2020

F2019L01137

28 Aug 2019

FSC128

5 Sep 2019

Note: This variation was not correctly published in Gazette FSC128

14 May 2020

ad

Entry for Lipase, triacylglycerol (EC 3.1.1.3) sourced from Trichoderma reesei containing the lipase 3 gene from Aspergillus tubingensis

S18—9(3)

187

F2019L01137

28 Aug 2019

FSC128

5 Sep 2019

5 September 2019

ad

Entry for Aspergillopepsin I (EC 3.4.23.18) sourced from Trichoderma reesei containing the gene for aspergillopepsin I isolated from Trichoderma reesei

S18—9(3)

187

F2019L01137

28 Aug 2019

FSC128

5 Sep 2019

5 September 2019

ad

Entry for Protein engineered enzyme that: contains both UDP‑glucosyltransferase (EC 2.4.1.17) and sucrose synthase (EC 2.4.1.13) components; and is sourced from Pichia pastoris strain UGT-A.

S18—9(3)

188

F2019L01569

4 Dec 2019

FSC129

5 Dec 2019

5 December 2019

ad

Entry for Pullulanase (EC 3.2.1.41) sourced from Bacillus licheniformis containing the pullulanase gene from Bacillus deramificans.

S18—9(3)

190

F2020L00025

15 Jan 2020

FSC131

17 Jan 2020

17 January 2020

ad

Entry for α-Glucosidase (EC 3.2.1.20) sourced from Trichoderma reesei containing the α‑glucosidase gene from Aspergillus niger.

S18—9(3)

191

F2020L00153

20 Feb 2020

FSC 132

26 Feb 2020

26 February 2020

ad

Entry for Sucrose synthase (EC 2.4.1.13) sourced from Escherichia coli K-12 containing the gene for sucrose synthase from Arabidopsis thaliana.

S18—9(3)

191

F2020L00153

20 Feb 2020

FSC 132

26 Feb 2020

26 February 2020

ad

Uridine diphosphate (UDP) glucosyltransferase sourced from Escherichia coli K-12 containing the UDP glucosyltransferase gene from Solanum lycopersicum

S18—9(3)

191

F2020L00153

20 Feb 2020

FSC 132

26 Feb 2020

26 February 2020

ad

Uridine diphosphate (UDP) glucosyltransferase sourced from Escherichia coli K-12 containing the UDP glucosyltransferase gene from Stevia rebaudiana

S18—9(3)

191

F2020L00151 Feb 2020

FSC 132

26 Feb 2020

26 February 2020

ad

Inulinase (EC 3.2.1.7) sourced from Aspergillus oryzae containing the inulinase gene from Aspergillus ficuum

S18—9(3)

192

F2020L00568

12 May 2020

FSC133

14 May 2020

14 May 2020

ad

Entry for Endo-1,4-beta-xylanase (EC 3.2.1.8) sourced from Trichoderma reesei containing the endo-1,4-beta-xylanase gene from Aspergillus niger

S18—9(3)

192

F2020L00570

12 May 2020

FSC133

14 May 2020

14 May 2020

ad

Entry for Glucose oxidase (EC 1.1.3.4) sourced from Trichoderma reesei containing the glucose oxidase gene from Penicillium amagasakiense

S18—9(3)

193

F2020L00937

23 July 2020

FSC134

28 July 2020

28 July 2020

ad

Entry for Protein engineered enzyme that: contains both UDP‑glucosyltransferase and sucrose synthase (EC 2.4.1.13) components; and is sourced from Pichia pastoris strain UGT-A.

S18—9(3)

195

F2020L01111

31 August 2020

FSC136

3 Sept 2020

3 September 2020

ad

Entry for Glucoamylase (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Trametes cingulata

S18—9(3)

195

F2020L01113

31 August 2020

FSC136

3 Sept 2020

3 September 2020

ad

α-Amylase (EC 3.2.1.1) sourced from Aspergillus niger containing the α-Amylase gene from Rhizomucor pusillus

S18—9(3)

196

F2020L01516

1 Dec 2020

FSC137

3 Dec 2020

3 December 2020

ad

Glucoamylase (EC 3.2.1.3) sourced from Trichoderma reesei containing the glucoamylase gene from Trichoderma reesei

S18—9(3)

196

F2020L01522

1 Dec 2020

FSC137

3 Dec 2020

3 December 2020

ad

α-Amylase (EC 3.2.1.1) sourced from Trichoderma reesei containing the α-Amylase gene from Aspergillus kawachii

S18—9(3)

200

F2021L00671

1 June 2021

FSC141

3 June 2021

3 June 2021

ad

β-Amylase (EC 3.2.1.2) sourced from soybean (Glycine max)

S18—9(3)

200

F2021L00684

2 June 2021

FSC141

3 June 2021

3 June 2021

rep

Omit (EC 2.4.1.17) whenever occuring

S18—9(3)

201

F2021L00984

14 July 2021

FSC142

22 July 2021

22 July 2021

ad

Subtilisin (EC 3.4.21.62) sourced from Bacillus licheniformis containing the gene for subtilisin from Pyrococcus furiosus

S18—9(3)

202

F2021L01181

24 August 2021

FSC143

26 August 2021

26 August 2021

ad

Maltogenic α-amylase, protein engineered variant, (EC 3.2.1.133) sourced from Saccharomyces cerevisiae containing the gene from Geobacillus stearothermophilus.

S18—9(3)

202

F2021L01181

24 August 2021

FSC143

26 August 2021

26 August 2021

ad

Note included on enzyme sources and related standards.

S18—9(3)

203

F2021L01436

14 October 2021

FSC 144

21 October 2021

21 October 2021

ad

β-Galactosidase (EC 3.2.1.23) sourced from Bacillus subtilis containing the β-galactosidase gene from Lactobacillus delbrueckii subsp. bulgaricus

S18—9(3)

205

F2022L00039

18 January 2022

FSC 146

20 January 2022

20 January 2022

ad

Maltogenic α-amylase (EC 3.2.1.133) sourced from Bacillus licheniformis containing the gene for maltogenic α-amylase from Geobacillus stearothermophilus.

S18—4(5)

208

F2022L00722

27 May 2022

FSC 148

20 June 2022

1 June 2022

rep

β-Fructofuranosidase (EC 3.2.1.26)

S18—9(3)

208

F2022L00723

27 May 2022

FSC 148

1 June 2022

1June 2022

ad

Maltogenic α-Amylase (EC 3.2.1.133) sourced from Escherichia coli containing the maltogenic α-Amylase gene from Geobacillus stearothermophilus

S18—11

211

F2022L01125

26 August 2022

FSC151

1 Sept 2022

1 September 2022

ad

Cetylpyridinium chloride as an anti-microbial agent

S18—9(3)

213

F2022L01385

24 October 2022

FSC153

27 October 2022

27 October 2022

ad

Thermomycolin (EC 3.4.21.65) sourced from Trichoderma reesei containing the thermomycolin gene from Malbranchea cinnamomea

S18—9(3)

213

F2022L01400

26 October 2022

FSC153

27 October 2022

27 October 2022

ad

Chymosin (EC 3.4.23.4) sourced from Trichoderma reesei containing the chymosin gene from Bos taurus

S18—9(3)

214

F2022L01590

8 Dec 2022

FSC154

8 Dec 2022

8 December 2022

ad

Polygalacturonase (EC 3.2.1.15) sourced from Aspergillus oryzae containing the polygalacturonase gene from Aspergillus tubingensis

S18—9(3)

214

F2022L01593

8 Dec 2022

FSC154

8 Dec 2022

8 December 2022

ad

Pectinesterase (EC 3.1.1.11) sourced from Aspergillus oryzae containing the pectinesterase gene from Aspergillus tubingensis

S18—9(3)

214

F2022L01592

8 Dec 2022

FSC154

8 Dec 2022

8 December 2022

ad

Phospholipase A1 (EC 3.1.1.32) sourced from Aspergillus oryzae containing the phospholipase A1 gene from Valsaria rubricosa

S18—9(3)

214

F2022L01588

8 Dec 2022

FSC154

8 Dec 2022

8 December 2022

ad

Glucoamylase, protein engineered variant, (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Gloeophyllum trabeum

S18—9(3)

214

F2022L01588

8 Dec 2022

FSC154

8 Dec 2022

8 December 2022

ad

Insert, Glucoamylase, protein engineered variant; to note after table.

S18—9(3)

215

F2023L00031

11 January 2023

FSC155

16 January 2023

16 January 2023

ad

α-Amylase (EC 3.2.1.1) sourced from Bacillus licheniformis containing the α-amylase gene from Cytophaga species

S18—9(3)

216

F2023L00186

2 March 2023

FSC156

2 March 2023

2 March 2023

ad

β-Amylase (EC 3.2.1.2) sourced from Bacillus licheniformis containing the β-amylase gene from Priestia flexa (basionym Bacillus flexus)

S18—9(3)

216

F2023L00143

24 Feb 2023

FSC156

2 March 2023

2 March 2023

ad

Phospholipase A1 (EC 3.1.1.32) sourced from Aspergillus niger containing the phospholipase A1 gene from Evansstolkia leycettana (basionym Talaromyces leycettanus)

S18—9(3)

216

F2023L00147

24 Feb 2023

FSC156

2 March 2023

2 March 2023

ad

Glucose oxidase (EC 1.1.3.4) sourced from Penicillium rubens

S18—9(3)

217

F2023L00449

18 April 2023

FSC157

21 April 2023

21 April 2023

ad

Glucoamylase, protein engineered variant, (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Penicillium oxalicum

S18—9(3)

219

F2023L00565

23 May 2023

FSC159

26 May 2023

26 May 2023

ad

α-Amylase (EC 3.2.1.1) sourced from Bacillus subtilis containing the α-amylase gene from Thermoactinomyces vulgaris

S18—9(4)2

220

F2023L01004

11 July 2023

FSC160

19 July 2023

19 July 2023

rs

Repeal and substitute note 3

S18—9(3)

220

F2023L01004

11 July 2023

FSC160

19 July 2023

19 July 2023

rs

Repeal and substitute column 2 in Table

S18—9(3

221

F2023L01124

29 Aug 2023

FSC161

1 Sept 2023

1 September 2023

ad

α-Arabinofuranosidase (EC

3.2.1.55) sourced from Trichoderma

reesei containing the αarabinofuranosidase gene from Talaromyces pinophilus

S18—9(3)

221

F2023L01120

28 Aug 2023

FSC161

1 Sept 2023

1 September 2023

ad

Endo-1,4-beta-xylanase (EC

3.2.1.8) sourced from Trichoderma

reesei containing the endo-1,4-beta-xylanase gene from Talaromyces

leycettanus

S18—9(3)

221

F2023L01121

28 Aug 2023

FSC161

1 Sept 2023

1 September 2023

ad

Carboxypeptidase (EC 3.4.16.6)

sourced from Aspergillus oryzae

containing the carboxypeptidase

gene from Aspergillus oryzae

S18—9(3)

222

F2023L01402

20 October 2023

FSC162

30 October 2023

30 October 2023

rs

Repeal and substitute S18-9(3) entry for α-Glucosidase (EC 3.2.1.20) sourced from Trichoderma reesei containing the α glucosidase gene from Aspergillus niger

S18—9(3)

223

F2023L01554

27 Nov 2023

FSC163

30 Nov 2023

30 November 2023

ad

Endo-1,4-β-xylanase, protein engineered variant, (EC 3.2.1.8) sourced from Trichoderma reesei, containing the endo-1,4-ß-xylanase gene from Fusarium verticillioides

S18—9(3)

225

F2024L00079

17 January 2024

FSC165

19 January 2024

19 January 2024

ad

Entries for the following new enzymes, each with a technological purposes and maximum permitted level;

Sucrose synthase, protein engineered variant, (EC 2.4.1.13) sourced from Escherichia coli K-12 containing the gene for sucrose synthase from Glycine max

Uridine diphosphate (UDP)- glucosyltransferase, protein engineered variant, sourced from Escherichia coli K-12 containing the UDP-glucosyltransferase gene from Oryza sativa

Uridine triphosphate (UTP)-glucose-1-phosphate uridylyltransferase, protein engineered variant, (EC 2.7.7.9) sourced from Escherichia coli K-12, containing the gene for UTP-glucose-1-phosphate uridylyltransferase from Bifidobacterium bifidum

S18—9(3)

225

F2024L00078

17 January 2024

FSC165

19 January 2024

19 January 2024

ad

Insert new entry Fructan β-fructosidase

S18—9(3)

225

F2024L00078

17 January 2024

FSC165

19 January 2024

19 January 2024

rs

Omit and substitute note after table to protein engineered variants of enzymes listed in the note.

S18—9(3)

225

F2024L00077

17 January 2024

FSC165

19 January 2024

19 January 2024

ad

Pullulanase (EC 3.2.1.41) sourced from Bacillus subtilis containing the pullulanase gene from Bacillus deramificans.

S18—9(3)

227

F2024L00465

17 April 2024

FSC167

29 April 2024

29 April 2024

ad

Cellulase, protein engineered variant, (EC 3.2.1.4) sourced from Aspergillus niger containing the cellulase gene from Trichoderma reesei

S18—9(3)

227

F2024L00468

18 April 2024

FSC167

29 April 2024

29 April 2024

ad

β-Fructofuranosidase (EC 3.2.1.26) sourced from Trichoderma reesei containing the β-fructofuranosidase gene from Aspergillus niger

S18—9(3)

228

F2024L00579

28 May 2024

FSC168

31 May 2024

31 May 2024

ad

Transglutaminase (EC 2.3.2.13) sourced from Bacillus licheniformis containing the transglutaminase gene from Streptomyces mobaraensis

S18-9(3)

230

F2024L00988

13 August 2024

FSC 170

15 August 2024

15 August 2024

ad

Subtilisin, protein engineered variant, (EC 3.4.21.62) sourced from Bacillus subtilis containing the gene for subtilisin from Bacillus clausii

S18-9(3)

230

F2024L00988

13 August 2024

FSC 170

15 August 2024

15 August 2024

rs

Substitute note after table to Protein engineered enzymes used in the manufacture of various steviol glycosides;

Subtilisin, protein engineered variant.

S18—9(3)

233

F2024L01377

28 October 2024

FSC173

29 October 2024

29 October 2024

ad

Insert D-psicose 3-epimerase (EC 5.1.3.30) from Microbacterium foliorum into S18—9(3) table.

S18—9(3)

233

F2024L01378

28 October 2024

FSC173

29 October 2024

29 October 2024

ad

Insert in table Lipase, triacylglycerol, protein engineered variant, (EC 3.1.1.3) sourced from Trichoderma reesei containing the lipase, triacylglycerol gene from Thermomyces lanuginosus

S18—9(3)

233

F2024L01378

28 October 2024

FSC173

29 October 2024

29 October 2024

rs

Omit dot point list after table identifying protein engineered enzymes and substitute.

S18—8

234

F2025L00012

8 January 2025

FSC 174

13 January 2025

13 January 2025

ad

Insert 2-Methyloxolane into table

S18—9(3)

234

F2025L00014

8 January 2025

FSC 174

13 January 2025

13 January 2025

ad

Insert Glucoamylase, protein engineered variant, (EC 3.2.1.3) sourced from Aspergillus niger containing the glucoamylase gene from Gloeophyllum sepiarium

S18—9(3)

236

F2025L00521

24 April 2025

FSC 176

29 April 2025

29 April 2025

ad

Insert fructosyltransferase, immobilised, (EC 2.4.1.9) derived from Aspergillus oryzae

S18—9(3)

236

F2025L00522

24 April 2025

FSC 176

29 April 2025

29 April 2025

ad

Insert lipase, triacylglycerol (EC 3.1.1.3) sourced from Komagataella phaffii containing the lipase, triacylglycerol gene from Fusarium oxysporum

S18—9(3)

240

F2025L00860

22 July 2025

FSC 180

22 July 2025

22 July 2025

ad

Insert Prolyl oligopeptidase (EC 3.4.21.26) sourced from Trichoderma reesei containing the prolyl oligopeptidase gene from Aspergillus niger

S18—4(2) (Note 3)

243

F2025L00988

26 August 2025

FSC183

2 Sept 2025

2 September 2025

rep

Repeal note 3

S18—4(5)

243

F2025L00988

26 August 2025

FSC183

2 Sept 2025

2 September 2025

rep

Repeal protein engineered variant (wherever occurring)

S18—9(3)

243

F2025L00988

26 August 2025

FSC183

2 Sept 2025

2 September 2025

rep

Repeal protein engineered variant (wherever occurring)

S18—9(3)

243

F2025L00988

26 August 2025

FSC183

2 Sept 2025

2 September 2025

rs

Replace Protein engineered enzyme with Enzyme

S18—9(3)

243

F2025L00988

26 August 2025

FSC183

2 Sept 2025

2 September 2025

rs

Replace Protein engineered enzymes with Enzymes

S18—9(3) (Note)

243

F2025L00988

26 August 2025

FSC183

2 Sept 2025

2 September 2025

rep

Repeal the note

S18—9(3)

245

F2025L01258

21 October 2025

FSC185

28 October 2025

28 October 2025

ad

New entry for Sucrose synthase (EC 2.4.1.13)

S18—9(3)

245

F2025L01258

21 October 2025

FSC185

28 October 2025

28 October 2025

ad

New entry for Uridine diphosphate (UDP) glucosyltransferases

S18—9(3)

246

F2025L01468

2 December 2025

FSC186

4 December 2025

4 December 2025

ad

New entry for Thermolysin (EC 3.4.24.27)

S18—9(3)

248

F2026L00128

20 February 2026

FSC188

26 February 2026

26 February 2026

ad

New entry for Aminopeptidase Y (EC 3.4.11.15)

S18—9(3)

248

F2026L00130

23 February 2026

FSC188

26 February 2026

26 February 2026

ad

New entry for Phospholipase C (EC 3.1.4.3)

S18—9(3)

248

F2026L00132

23 February 2026

FSC188

26 February 2026

26 February 2026

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New entry for Phosphoinositide phospholipase C (EC 3.1.4.11)

\n```","sortOrder":0}],"analysis":{"flash_summary_failed":{"failed":true,"reason":"A positive credit balance is required for all requests, including BYOK, so fallback providers remain available. Add credits at https://vercel.com/d?to=%2F%5Bteam%5D%2F%7E%2Fai%3Fmodal%3Dtop-up to continue.","source":"analysis-cron"},"flash_summary":{"complexity_score":9,"scope_assessment":{"changed":true,"description":"The Schedule has broadened substantially beyond a short list of traditional processing aids. Over successive amendments it has progressively added many highly specific entries—particularly recombinant and protein‑engineered enzymes, microbial phage preparations, and novel solvents—so the Schedule now functions both as a conventional list of incidental technical aids and as a managed approvals list for modern biotechnologies used in processing (see S18—4(5) and S18—9(3) entries and the amendment history entries adding recombinant enzyme sources and engineered variants). That expansion changes the practical scope from merely recording accepted ancillary materials to acting as the gate where new technological processing methods must be individually authorised and specified, increasing regulatory granularity and commercial gating for entrants who want to use new enzymes or engineered production strains."},"complexity_factors":["Extensive tabular material covering many substance types (chemicals, enzymes, resins, solvents, antimicrobials, water aids) across multiple purposes (decolourant, filtration, catalyst, antifoam, carrier, etc.)","Large number of defined entries for enzymes with specific EC numbers and explicit source organisms, including recombinant or protein‑engineered variants (S18—4(5) and S18—9(3))","Multiple numerical limits and measurement bases (mg/kg, 'available chlorine', 'as fluoride', 'as styrene', 'measured as benzoic acid', 'limit of determination') requiring different testing methods","Numerous conditional permissions with operational rules (e.g. rinse requirement and max wash concentration for cetylpyridinium chloride in S18—11)","Cross‑references to other Code standards (notably Standard 1.3.3 and 1.1.1) and to specifications in other sections (S3—2, S3—3, S16—2) creating interpretive dependencies","Many entries allowed under 'GMP' which requires case‑by‑case judgement about 'minimum needed' and places interpretive burden on both industry and regulators","Long amendment history with repeated additions, substitutions and repeals (dozens of amendments recorded), increasing the risk of inconsistencies and interpretive ambiguity","Specific carve‑outs for particular foods or processing contexts (e.g. infant formula vs other foods for 2‑Methyloxolane in S18—8) requiring contextual application","Use of both conventional chemical aids and modern biotechnological permissions (phage preparations, recombinant enzymes) increases technical variety and regulatory assessment complexity"],"plain_english_summary":"**What this instrument does (mechanically)\n\n- This Schedule (Schedule 18) to the Australia New Zealand Food Standards Code lists which substances may be used as \"processing aids\" in food manufacture, and the conditions or maximum residue levels that apply when they are used. It works by cross‑referencing to the Code’s operative clauses (notably Standard 1.3.3 and 1.1.1) and giving detailed tables of allowed chemicals, enzymes, solvents, filtration media, antimicrobials, water treatment agents and similar materials. (See S18—2 to S18—11.)\n\n- Where the table shows \"GMP\" the substance is permitted where used in accordance with Good Manufacturing Practice (i.e. used at the lowest level needed to achieve the technological purpose and under appropriate controls). Numeric entries are maximum permitted residual amounts (mg/kg) or other specified measurement limits. (See S18—3, S18—6, S18—7, S18—8, S18—9, S18—10, S18—11.)\n\n- The Schedule separately identifies permitted enzymes by origin (animal, plant, microbial) and, for many microbial or recombinant enzymes, the specific source organism or engineered strain that is permitted. (See S18—4(3)–(5).)\n\n- The Schedule also contains narrow permissions with use conditions: for example, maximum addition levels for dimethyl dicarbonate as a microbial control agent in juices and some beverages (S18—10), and a conditional permission for cetylpyridinium chloride to be used as an antimicrobial wash on raw poultry with rinsing and concentration limits (S18—11).\n\n**Who is affected\n\n- Food manufacturers and processors who use processing aids (including dairies, bakeries, breweries, starch and syrup producers, wine and fruit processors, meat processors, edible casing and gelatin manufacturers, and ingredient suppliers). (Tables throughout S18—3 to S18—9.)\n\n- Suppliers of enzymes, solvents, filtration media, water treatment chemicals, antimicrobials and other technical inputs: they must supply products and documentation that meet the listed specifications and permitted uses.\n\n- Regulatory agencies and food inspectors responsible for enforcement of the Code (they interpret the tables, test residues and check conditions of use).\n\n- Consumers are indirectly affected because the Schedule determines which processing chemicals may be used and at what residual levels are acceptable in food.\n\n**Why it matters (claimed purpose, and practical implications)\n\n- Stated purpose: to control the safety and technological use of substances that assist food processing but are not intended to remain as functional ingredients (see S18 preface and cross‑references to Standard 1.3.3). The Schedule sets permitted lists and limits so that processors can achieve technological outcomes (e.g. clarification, decolourising, enzyme‑catalysed reactions, antimicrobial control) while managing safety through residue limits and use conditions.\n\n- Practical effects and trade‑offs:\n - Predictability for business: processors get legal certainty about which aids they may use and under what conditions (specific substances, maximum residues or GMP). This reduces legal ambiguity when sourcing technical inputs (see S18—3, S18—4).\n - Compliance costs: businesses bear costs for recordkeeping, supplier verification, process controls, and residue testing where numeric limits apply (e.g. solvents S18—8, antimicrobials S18—7, water treatment S18—6). Where the Schedule lists source organisms for enzymes, suppliers may need to provide traceability and certificates of origin. Enforcement and testing also impose administrative load on regulators.\n - Innovation and market access: listing of specific engineered or recombinant enzymes and protein‑engineered variants (through numerous entries in S18—9 and S18—4(5)) permits use of modern biotechnological production methods, which can lower processing costs or enable new food products. At the same time, an approvals‑by‑listing approach means new technologies must be individually added to the Schedule to be lawful, creating a commercialization checkpoint and potential delay.\n - Concentrated benefits vs diffuse costs: suppliers of newly permitted specialised enzymes or processing aids get a clear commercial advantage once listed. Costs of expanded monitoring and any public concern about residues are spread across many consumers and small producers.\n - Implementation risk: several permissions impose operational conditions (e.g. maximum concentration in wash solutions, requirement to rinse treated poultry—S18—11). Effective risk control depends on firms’ process controls and regulators’ testing capacity; weak oversight risks non‑compliance or higher than intended residues.\n\n**How it affects decisions and behaviour\n\n- Who decides: FSANZ (and ultimately food regulators acting under the Code) decides which substances are listed and under what terms; business operators decide whether to adopt them in production and must comply with the listed conditions (see S18—1 and cross references).\n\n- What changes for business: manufacturers may change formulations, adopt enzyme or chemical aids to improve yield or reduce costs, or substitute permitted alternatives where the Schedule allows broader options (e.g. many filtration resins and ion‑exchange media in S18—3 and S18—6). They must also implement verification and testing protocols to demonstrate compliance with numerical limits and GMP obligations.\n\n**Operational notes and common terms\n\n- \"GMP\" in the tables means permitted at Good Manufacturing Practice — i.e. used at the minimum level necessary and with appropriate process controls.\n- Many entries are qualified by the food type and technological purpose (e.g. extraction solvent limits differ for flavourings vs \"other foods\" in S18—8).\n- The Schedule is highly specific about enzyme source organisms and, for many microbial sources, allows genetically modified production strains by naming the host plus the gene donor (see S18—4(5)).\n\n**Selected section pointers (examples)\n\n- General permitted processing aids list: S18—2.\n- Permitted enzymes and permitted sources: S18—4 (animal, plant, microbial).\n- Specific technological purposes and maximum permitted levels: S18—3 and S18—9 (large tabulation of purposes and limits).\n- Water treatment aids and maximums: S18—6.\n- Extraction solvents and residue limits: S18—8.\n- Special permissions with conditions: dimethyl dicarbonate (S18—10), cetylpyridinium chloride on raw poultry with rinsing and concentration limits (S18—11).\n\n(References are to the Schedule’s section headings: S18—2 through S18—11.)"},"kimi_summary":{"_metrics":{"completionTokens":825},"content_quality":"ok","complexity_score":8,"scope_assessment":{"changed":true,"description":"The Schedule has expanded significantly from its original 2016 commencement. Originally focused on traditional processing aids, it now encompasses advanced biotechnologies including: numerous genetically modified enzymes with specified gene sources; bacteriophage preparations for pathogen control; protein-engineered enzyme variants; and complex steviol glycoside production systems involving multiple engineered enzymes. The scope has shifted from simple chemical processing aids to sophisticated biological processing technologies."},"complexity_factors":["Extensive cross-referencing to Standards 1.1.1, 1.1.2, 1.3.3 and other Code provisions","Multiple tables with conditional permissions based on food type, technological purpose, and maximum permitted levels","Highly technical chemical nomenclature including IUPAC names, polymer specifications, and enzyme EC numbers","Genetically modified enzyme entries require parsing of source organism + gene origin organism combinations","Nested definitions in section S18-9(2) for specialised resin types with complex chemical specifications","Dual jurisdiction application (Australia and New Zealand) with different enabling legislation","Frequent amendments (52 compilations, 246 amendments) creating version control complexity","GMP (Good Manufacturing Practice) as a limit creates subjective compliance boundaries","Specific exclusions and conditions (e.g., 'approved food for use of phage' definition with 5 criteria)"],"plain_english_summary":"This Schedule sets rules for processing aids—substances used in food manufacture that are not intended to remain in the final product—covering hundreds of permitted chemicals, enzymes, solvents and microbial nutrients for use in Australia and New Zealand. It binds manufacturers and importers to Good Manufacturing Practice or specified maximum levels, ensuring food‑safety oversight while allowing modern processing technologies."}},"importantCases":[],"_links":{"self":"/api/acts/australia-new-zealand-food-standards-code-schedule-18-processing-aids","history":"/api/acts/australia-new-zealand-food-standards-code-schedule-18-processing-aids/history","analysis":"/api/acts/australia-new-zealand-food-standards-code-schedule-18-processing-aids/analysis","conflicts":"/api/acts/australia-new-zealand-food-standards-code-schedule-18-processing-aids/conflicts","importantCases":"/api/acts/australia-new-zealand-food-standards-code-schedule-18-processing-aids/important-cases","documents":"/api/acts/australia-new-zealand-food-standards-code-schedule-18-processing-aids/documents"}}