{"title":"[UV-Modification of Free and Immobilized Trypsin].","authors":"M G Holyavka, V G Artyukhov, S M Sazykina","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>We investigated the mechanism of UV-radiation influence on trypsin in free and immobilized (on chitosan) states. The catalytic activity of free enzyme under the action of UV-light is subjected to changes to a greater extent than that of the immobilized one. We assume that the photoprotection effect of chitosan is caused for the following reasons: firstly, through interactaction with trypsin molecules chitosan forms a more photoresistant complex as compared to the native protein; secondly, chitosan probably binds the active photopro- ducts of a free radical nature, thus preventing oxidation (destruction) of several amino acids of the enzyme under its UV-radiation.</p>","PeriodicalId":79368,"journal":{"name":"Radiatsionnaia biologiia, radioecologiia","volume":"57 1","pages":"66-70"},"PeriodicalIF":0.0000,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Radiatsionnaia biologiia, radioecologiia","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
We investigated the mechanism of UV-radiation influence on trypsin in free and immobilized (on chitosan) states. The catalytic activity of free enzyme under the action of UV-light is subjected to changes to a greater extent than that of the immobilized one. We assume that the photoprotection effect of chitosan is caused for the following reasons: firstly, through interactaction with trypsin molecules chitosan forms a more photoresistant complex as compared to the native protein; secondly, chitosan probably binds the active photopro- ducts of a free radical nature, thus preventing oxidation (destruction) of several amino acids of the enzyme under its UV-radiation.
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