Trypsin
9002-07-7 · TrypsinCAS 9002-07-7
Listed as an enzyme by the US.
Listed as enzymes (US)
- United States: Enzyme — FDA, Substances Added to Food: TRYPSIN FROM ANIMAL TISSUE
- United States: Enzymes — 21 CFR 184.1914, citing 21 CFR 170.3(o)(9)
Trypsin is a protein-digesting enzyme used to make protein hydrolysates and to modify proteins in food processing. It is obtained from animal pancreas.
Where it is and isn’t permitted
| Jurisdiction | Status | Scope and limits | Citation |
|---|---|---|---|
| Australia and New Zealand | No listed food uses foundThis site has not matched this substance to any food use on this jurisdiction’s list of authorised food additives. A food additive may be used only in foods that list names. Flavourings, enzymes, processing aids and added nutrients are regulated separately and do not appear on it. | ||
| Canada | No listing matchedHealth Canada’s lists name additives without E or INS numbers, so this site matches them by exact name. A substance listed there under a name this site does not recognise has no row here. | ||
| European Union | No listed food uses foundThis site has not matched this substance to any food use on this jurisdiction’s list of authorised food additives. A food additive may be used only in foods that list names. Flavourings, enzymes, processing aids and added nutrients are regulated separately and do not appear on it. | ||
| Great Britain | No listed food uses foundThis site has not matched this substance to any food use on this jurisdiction’s list of authorised food additives. A food additive may be used only in foods that list names. Flavourings, enzymes, processing aids and added nutrients are regulated separately and do not appear on it. | ||
| Japan | No listing matchedThis site imports only Japan’s list of designated additives (Appended Table 1 to the Regulations for Enforcement of the Food Sanitation Act), matched by English name. Existing additives, natural flavouring agents and ordinary foods used as additives are permitted outside that list and are not imported, so an empty row does not show that Japan does not permit the substance. | ||
| South Korea | Permitted, with conditions | Designated food additive: Standards and Specifications for Food Additives, Part III, 2. …Designated food additive: Standards and Specifications for Food Additives, Part III, 2. 가공보조제 (processing aids), 트립신 (“Trypsin”, the English the Code prints beside it). Main use (주용도) of 트립신: 효소제. Standard for use (사용기준) of 트립신: (1) [to be used under the general standard for use in II. 2. 1), the minimum amount that achieves the technical effect, with no limit set for this additive in particular] “II. 2. 1)의 규정에 따라 사용하여야 한다.” The Korean is the standard as published. There is no official English translation of the current Code (the English version on MFDS’s website is the 2020 edition and has no legal effect); the English in square brackets is this site’s description of what each sentence does, not a translation of the foods or the levels. Compositional specifications (Part IV) are not imported, nor are the general standards in Part II, which apply to every additive. | Standards and Specifications for Food Additives (식품첨가물의 기준 및 규격), MFDS Notification, Part III (Standards for use, by item)retrieved 2026-10-18 |
| United States | Permitted | 21 CFR 184.1914retrieved 2026-10-17 | |
| Codex Alimentarius | Not listedDoes not appear on this jurisdiction’s permitted list. That is not the same as being prohibited. |
How much is permitted
A listing usually limits the quantity as well as the food. Only one of the forms that takes is a figure: quantum satis and good manufacturing practice permit the amount the technological effect requires and no more, which is a limit rather than the absence of one. Figures below are the range across every food category this page is listed in, and categories differ between regulators — see how much is permitted.
| South Korea | — | 1 no quantity stated |
|---|---|---|
| United States | — | 1 no quantity stated |
No regulator sets a figure for Trypsin. That is not an absence of control: where the listing says quantum satis or good manufacturing practice, the quantity is limited to what the effect requires.
What it is made from
Extracted from the pancreatic tissue of cattle or pigs, a slaughterhouse by-product.
- Not vegan
- Not vegetarian
- May raise a halal question
- May raise a kosher question
Compare other additives on the dietary indexes.
- CAS registry number
- 9002-07-7
How JECFA defines it
The international specification for identity and purity, prepared by the Joint FAO/WHO Expert Committee on Food Additives and published by FAO. It is a different document from any above, written by a different body and revised on its own cycle; it is advisory, and a country adopts it or does not.
Serine Protease with Trypsin Specificity from Fusarium Oxysporum Expressed in Fusarium Venenatum
Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase EC 3.4.21.4
Assay, identification and purity criteria
Description and assay
- Specification history
- SERINE PROTEASE WITH TRYPSIN SPECIFICITY FROM FUSARIUM OXYSPORUM EXPRESSED IN FUSARIUM VENENATUM New specifications prepared at the 76th JECFA (2012) and published in FAO JECFA Monographs 13 (2012). An ADI “not specified” was established at the 76th JECFA (2012)
- SOURCES
- Produced by submerged fermentation of a genetically modified non-pathogenic and non-toxigenic strain of Fusarium venenatum which contains a gene coding for serine protease with trypsin specificity from Fusarium oxysporum. The enzyme is secreted into the broth. The cell mass and other solids are secreted into the fermentation broth, separated by vacuum drum filtration or centrifugation. Ultrafiltration and/or evaporation are applied for concentration and further purification. Residual production strain microorganisms are removed by germ filtration. The final product is formulated using food-grade stabilizing and preserving agents and is standardized to the desired activity.
- Active principles
- Serine protease with trypsin specificity
- Systematic names and beta-Glucanase: EC 3.4.21.4, CAS number: 9002-07-7 numbers Xylanase: 1,4- CAS number: 90 Reactions catalysed
- Preferential cleavage: Arg, Lys
- Secondary enzyme activities
- None
- DESCRIPTION
- Brown liquid.
- FUNCTIONAL USES
- Enzyme preparation. Used in the production of partially or extensively hydrolyzed proteins of vegetable and animal origin. These hydrolyzed proteins may be used for various applications as ingredients in food and beverages, for protein fortification or as ingredients providing functional effects such as emulsification or flavour enhancement.
- GENERAL SPECIFICATIONS
- Must conform to the current edition of the JECFA General Specifications and Considerations for Enzyme Preparations Used in Food Processing.
Identification
- Serine protease activity with trypsin specificity
- The sample shows serine protease activity with trypsin specificity. See descriptions under TESTS
- Serine protease activity with trypsin specificity
- Principle: Serine protease with trypsin specificity hydrolyses the substrate Ac-Arg-p-nitro-Anilide (Ac-Arg- p NA). The release of p -nitroaniline ( p NA) results in an increase of absorbance at 405 nm and is proportional to the enzyme activity. Enzyme activity is measured in Kilo Microbial Trypsin Units (KMTU). 1 KMTU is the amount of enzyme that releases 1μmol of p -nitroaniline from 1mM substrate (Ac-Arg-pNA) per minute at pH 9.0 and temperature 37°. Reagents and Solutions: Preparation of 15% Brij 35 solution: Bring the stock Brij 35 (30% solution) to room temperature. Pour out 1L into a 2L volumetric flask. Make up the volume with demineralized water. Stir vigorously. Store in a bottle with label up to 2 months at 4°. Preparation of 1M Tris buffer: Weigh and transfer 121.1g Tris (tris(hydroxymethyl)- aminomethane) into a 1L volumetric flask. Add about 800 ml of deionised water and stir on a magnetic stirrer until dissolved. Make up the volume with deionised water. This solution can be stored at room temperature for up to 1 month. Preparation of dilution buffer (1.5 mM CaCl 2 , 0.225 g/l Brij, 100 mM Tris, pH 8.0): Example Volume, 10 L: Weigh and transfer 2.20 g CaCl 2 .2H 2 O into a 10 L volumetric flask. Add 1000 ml of 1 M Tris buffer. Add 15 ml of 15% Brij 35 solution, approximately 7000 ml of deionised water, and 275 ml of 2M hydrochloric acid. Mix until completely dissolved. Ensure that the solution temperature is between 23° to 25°. Adjust pH to 8.00+0.05. Make up the volume with deionised water. Mix thoroughly. This solution can be stored at room temperature up to 8 days. Ensure that the dilution buffer is adjusted to 23-25° prior to use by stirring. Preparation of 5 mM Ac-Arg- p NA solution (Substrate Solution): It is important to obtain a high quality substrate as well as to prepare, store and measure the substrate solution accurately. This affects the quality of analysis. Frozen substrate must be thawed completely before use, and discarded after. Weigh and transfer quantitatively 186.0+0.2 mg Ac-Arg- p NA into a 100 ml volumetric flask. Make up the volume with dilution buffer. Wrap the flask immediately with aluminum foil to protect from light. Mix for 5 min (max of 10 min). Aliquot the solution into tubes of 10 ml protected from light. Solution can be stored frozen up to 28 days (no yellow colouring appears). It is recommended to store at least 6 stock samples (at 1g aliquots) per lot for enabling bridging studies. Preparation of Standard and Sample Solutions: Preparation of stock standard solution: Weigh and transfer an amount corresponding to 20.00 KMTU (+0.02 KMTU) of the serine protease with trypsin specificity standard into a 250 ml volumetric flask. Make up the volume with dilution buffer. Mix the solution for about 15 min. Preparation of sample Weigh between 0.5 g to 1.78 g of the serine protease with trypsin specificity sample. Ensure that samples are homogeneous. Dilute in a measuring flask with dilution buffer. NOTE: A typical dissolution volume is 250 ml of diluent buffer. Stock sample solutions can be stored up to 8 h at room temperature. The stock sample solution is further diluted with the dilution buffer, to reach an activity of about 4.7 mKMTU/ml after final dilution. This solution can be stored at room temperature, covered, for up to 6 h. Procedure Prepare a standard curve using the stock standard solution as shown below: Standard # Dilution Stock Dilution Concentration, Ratio standard Buffer, μl mKMTU/ml solution, μl 1 50 30 1470 1.6 2 25 60 1440 3.2 3 15 100 1400 5.3 4 12 125 1375 6.7 5 10 150 1350 8.0 Prepared Working standard solutions can be stored, covered, up to 6 h at room temperature. Place the 5 mM Ac-Arg- p NA solution (substrate solution) in a water bath set to 37.0+1.0°. Set the spectrophotometer at 405 nm and the temperature of the cuvette holder at 37.0+0.5°. Pipette 2.5 ml of it into the cuvette. Add 340 ml of the working standard solution, reference standard working solution or sample to the cuvette. Place the cuvette in the spectrophotometer set to 37.0+0.5°. Set and start stopwatch to 12 sec. Read absorbance at 20 sec intervals for 3.5 min at 405 nm. Calculations Calculate the average absorbance per minute for each standard via linear regression. Plot the standard curve using the average absorbance per minute calculated against the activity of the standards (mKMTU/ml). Read the absorbance of the sample from the standard curve generated and calculate the enzyme activity as shown below: S V F Activity , KMTU / g W 1000 where, S, is the reading in mKMTU/ml, from the standard curve, V is the volume of the measuring flask used in ml, F is the dilution factor, W is the weight of the sample in g and 1000 is the conversion factor from mKMTU to KMTU.
Every name it appears under
2 recorded names. A label may use any of them.
CAS registry number
- 9002-07-7
As it appears in regulation
- Trypsin
Hazard reference values
| Type | Value | Population | Assessed by | Opinion |
|---|---|---|---|---|
| ADI | not limited | — | JECFA | 1971 |
Evidence and how bodies read it
Studies, and the differing conclusions regulators drew from them, are curated rather than machine-read, and none has been written for this substance yet.
Common questions
Assembled from what is above, in the words the questions are usually asked in. Each answer is the same statement the relevant section makes, with the same citations behind it.
- What is Trypsin?
- Trypsin is a protein-digesting enzyme used to make protein hydrolysates and to modify proteins in food processing. It is obtained from animal pancreas.
- What is Trypsin used for in food?
- It is listed as an enzyme — the role the US assigns it. This page shows every function each regulator records, with the citation for each.
- Is Trypsin banned in Europe?
- No. Trypsin is not on the EU's list of authorised food additives, but it would not be expected to be: every role regulators give it — enzyme — the EU regulates under separate law. Its absence from the additives list says nothing about whether it is permitted in Europe.
- Where is Trypsin permitted?
- Of the seven regulators this site reads, South Korea and the US permit it. Each permission is for named foods at named levels, not a blanket one; the table on this page gives them with citations.
- Is Trypsin vegan?
- No. Trypsin is animal-derived, and is not vegetarian either. This page says what it is made from.
Sources for this page
- kr retrieved 2026-10-18
- ecfr retrieved 2026-10-17
- jecfaspecs retrieved 2026-09-23
Full licence terms and publisher details on Sources. How this page is built and updated: Method.
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