Karasavova M.Krysteva M.Shopova B.Yotova L.2024-07-102024-07-102024-07-102024-07-101993-01-011310-281810.1080/13102818.1993.10819425SCOPUS_ID:84950642490https://rlib.uctm.edu/handle/123456789/361Pepsin is covalentlyimmobilized via hydroxymethyl groups to ultrafiltration membrane, composed of acrylonitrile and acrylamide copolymer. The properties of the immobolized enzyme showed high relative activity of 75%, pH optimum at pH 2.3 and temperature optimum at 50°C. Isolated wine proteins were treated with immobilized pepsin. This treatment shows not the production of small fragments in limited proteolysis conditions. The bound pepsin to ultra-filtration membrane by hydroxymethyl groups has considerable adventages for protein hydrolysis in comparison with the method used till now: one step activation of membrane with formaldehyde; high relative activity of immobilized enzyme; controlled degree of hydrolysis; no introduction of additional substances in hydrolysates. © 1993 Taylor & Francis Group, LLC.enArticle