Hydrolysis of wine proteins by means of pepsin, immobilized to ultra-fil-tration membranes
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1993-01-01
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Abstract
Pepsin 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.