Hydrolysis of wine proteins by means of pepsin, immobilized to ultra-fil-tration membranes

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dc.contributor.authorKarasavova M.
dc.contributor.authorKrysteva M.
dc.contributor.authorShopova B.
dc.contributor.authorYotova L.
dc.date.accessioned2024-07-10T14:27:03Z
dc.date.accessioned2024-07-10T14:48:30Z
dc.date.available2024-07-10T14:27:03Z
dc.date.available2024-07-10T14:48:30Z
dc.date.issued1993-01-01
dc.description.abstractPepsin 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.
dc.identifier.doi10.1080/13102818.1993.10819425
dc.identifier.issn1310-2818
dc.identifier.scopusSCOPUS_ID:84950642490en
dc.identifier.urihttps://rlib.uctm.edu/handle/123456789/361
dc.language.isoen
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84950642490&origin=inward
dc.titleHydrolysis of wine proteins by means of pepsin, immobilized to ultra-fil-tration membranes
dc.typeArticle
oaire.citation.issue3
oaire.citation.volume7
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