Product Introduction
Pepsin is an enzyme, specifically an aspartic protease, produced in the stomach that breaks down proteins into smaller peptides. It is one of the major digestive enzymes and is essential for the digestion of proteins in the stomach. Pepsin is produced by chief cells in the stomach lining and is secreted as an inactive zymogen called pepsinogen, its activation requires an acidic environment (pH < 6), which converts pepsinogen into pepsin that then cleaves proteins. [1] Pepsin functions optimally in acidic conditions, with an ideal pH between 1.5 and 2.5, found in the stomach. Pepsin's activity is inhibited at a pH above 6.5. [2]
Production Process
The production of pepsin typically involves extraction from the glandular layer of hog stomachs, a commonly used method for obtaining this enzyme. [3] The stomachs are first cleaned and the glandular layer is separated, then the layer undergoes an extraction process where pepsinogen is released, this pepsinogen is then activated into pepsin through acidification, usually with hydrochloric acid; the pepsin is then purified; this may involve several steps such as filtration and precipitation, to remove unwanted materials, and the pepsin is then concentrated to increase its enzymatic activity. The final step is drying. [4]
Product Effects and Benefits
Pepsin is useful for protein digestion, breaking down complex proteins into smaller, more easily absorbed peptides and amino acids. [5] It supports gastrointestinal health by improving the efficiency of digestion; this is particularly beneficial for individuals with digestive issues or those who require additional support in breaking down proteins. In addition, pepsin supports nutrient absorption, ensuring the body receives the full benefits of the proteins consumed. [6]
Product Applications
Pepsin finds use in digestive aids that help to alleviate symptoms of indigestion and enhance protein digestion, particularly for those with reduced gastric function. [7] Pepsin is also utilized in the food industry for modifying and hydrolyzing proteins in food products, enhancing flavor, texture, and digestibility. [8] As well as this, pepsin is used in leather tanning. [9]
Packaging and Storage
Pepsin is packaged in airtight containers to protect it from moisture and air, which can degrade its enzymatic activity. [10] It should be stored in a cool, dry place, ideally between 2°C to 8°C (35°F to 46°F), to maintain its stability and activity, because high temperatures can denature the enzyme, reducing its effectiveness. [11] Proper labeling is necessary, including the product name, batch number, manufacturing date, and expiration date, to ensure traceability and proper use, ensuring users are aware of the product's shelf life and storage requirements. [12]
Citations:
[1] Weber, R. E., & Hvidt, A. (1991). pH and temperature effects on pepsin structure and proteolysis. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 98(4), 549–557.
[2] Fruton, J. S. (1976). The mechanism of the catalytic action of pepsin and related acid proteases. Advances in Enzymology and Related Areas of Molecular Biology, 44, 1–36.
[3] Herriott, R. M. (1938). Isolation, crystallization and properties of swine pepsinogen. Journal of General Physiology, 21(5), 501–514.
[4] Ryle, A. P. (1970). The porcine pepsins and pepsinogens. Methods in Enzymology, 19, 316–336.
[5] Koelsch, K. M. (2012). Treatment of exocrine pancreatic insufficiency in dogs and cats. Veterinary Clinics of North America: Small Animal Practice, 42(6), 1199–1207.
[6] Marten, B., Pfeuffer, M., & Schrezenmeir, J. (2002). Medium-chain triglycerides. International Dairy Journal, 12(9), 735–763.
[7] Holtmann, G., Goebel, H., Talley, N. J., Drossman, D. A., & Whitehead, W. E. (2016). Functional gastrointestinal disorders. The Lancet, 388(10061), 2853–2864.
[8] Adler-Nissen, J. (1986). Enzymic hydrolysis of food proteins. Elsevier Applied Science.
[9] Covington, A. K. (1997). Tanning chemistry: the science of leather. Royal Society of Chemistry.
[10] Shahidi, F., & Zhong, Y. (2010). Lipid oxidation: measurement and impact on food quality. Food Science and Technology.
[11] Blanchard, J. (1992). Current perspectives on the stability of peptide pharmaceuticals. Journal of Parenteral Science and Technology, 46(3), 90–95.
[12] Code of Federal Regulations, Title 21, Part 101—Food Labeling.
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