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Pepsin from porcine gastric mucosa

lyophilized powder, ≥3,200 units/mg protein

Pepsin from hog stomach, Pepsin A
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:

Quality Level

biological source

Porcine gastric mucosa


lyophilized powder

specific activity

≥3,200 units/mg protein

mol wt

35 kDa


salt, essentially free


white to off-white


deionized water: soluble 10 mg/mL
10 mM HCl: soluble 4.0 mg/mL (Cold)

UniProt accession no.


diagnostic assay manufacturing

shipped in

wet ice

storage temp.


Gene Information

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Pepsin from Sigma has been used along with other enzymes for the determination of enzyme-resistant starch (RS) in bread. It has also been used to simulate in vitro gastrointestinal digestion of pea or whey protein isolates.
Pepsin is a peptidase used to digest proteins and is commonly used in the preparation of Fab fragments from antibodies. Pepsin, from porcine gastric mucosa, has been used to hydrolyze dry cervical samples in mice. Product P6887 is provided as a lyophilized powder and has been used to digest protein during dietary fiber analysis.
Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at


250 mg in glass bottle
1, 5, 10 g in glass bottle

Biochem/physiol Actions

Unlike many other peptidases, pepsin hydrolyzes only peptide bonds, not amide or ester linkages. The cleavage specificity includes peptides with an aromatic acid on either side of the peptide bond, especially if the other residue is also an aromatic or a dicarboxylic amino acid. Increased susceptibility to hydrolysis occurs if there is a sulfur-containing amino acid close to the peptide bond, which has an aromatic amino acid. Pepsin will also preferentially cleave at the carboxyl side of phenylalanine and leucine, and to a lesser extent at the carboxyl side of glutamic acid residues. It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.
Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin

Unit Definition

One unit will produce a ΔA280 of 0.001 per min at pH 2.0 at 37°C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 ml. Light path = 1 cm.)

Analysis Note

Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5.
Protein determined by E1%/280

Other Notes

View more information on pepsin at


Exclamation markHealth hazard

Signal Word


Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

J A Marlett et al.
The American journal of clinical nutrition, 50(3), 479-485 (1989-09-01)
The effects of different methods on the distribution of total neutral sugars (TNS), uronic acids (UA), and beta-glucans (beta G) between the soluble (S) and insoluble (I) fractions of dietary fiber (DF) were determined for peas, kidney beans, oat bran
V Vermeirssen et al.
Journal of dairy science, 86(2), 429-438 (2003-03-22)
Pea and whey protein were fermented by Lactobacillus helveticus and Saccharomyces cerevisiae in monoculture and in combination at 28 and 37 degrees C in order to release angiotensin-I-converting enzyme (ACE) inhibitory peptides. The fermentation products were subjected to in vitro
Oksana Lockridge et al.
The Journal of biological chemistry, 283(33), 22582-22590 (2008-06-26)
Human albumin is thought to hydrolyze esters because multiple equivalents of product are formed for each equivalent of albumin. Esterase activity with p-nitrophenyl acetate has been attributed to turnover at tyrosine 411. However, p-nitrophenyl acetate creates multiple, stable, acetylated adducts
Enzyme-resistant starch. III. The quality of straight-dough bread containing varying levels of enzyme-resistant starch.
Eerlingen, R. C., et al.
Cereal Chem., 71(2), 165-169 (1994)
Arno G B Wouters et al.
Journal of agricultural and food chemistry, 65(6), 1263-1271 (2017-01-27)
The relationship between structural and foaming properties of two tryptic and two peptic wheat gluten hydrolysates was studied at different pH conditions. The impact of pH on foam stability (FS) of the samples heavily depended on the peptidase used and


Fluorescent in situ Hybridization (FISH)

Available Fluorescent in situ hybridization (FISH) procedures, reagents and equipment.


Enzymatic Assay of Pepsin (

This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.

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