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dc.creatorStanić, Dragana
dc.creatorRadosavljević, Jelena
dc.creatorPolović, Natalija
dc.creatorJadranin, Milka
dc.creatorPopović, Milica
dc.creatorVučković, Olga
dc.creatorBurazer, Lidija
dc.creatorJankov, Ratko
dc.creatorVeličković, Tanja
dc.date.accessioned2021-02-18T10:34:53Z
dc.date.available2021-02-18T10:34:53Z
dc.date.issued2009
dc.identifier.issn0958-6946
dc.identifier.urihttp://intor.torlakinstitut.com/handle/123456789/292
dc.description.abstractThe use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on β-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used.en
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142020/RS//
dc.rightsrestrictedAccess
dc.sourceInternational Dairy Journal
dc.titleRemoval of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparationen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage752
dc.citation.issue12
dc.citation.other19(12): 746-752
dc.citation.rankM21
dc.citation.spage746
dc.citation.volume19
dc.identifier.doi10.1016/j.idairyj.2009.05.008
dc.identifier.rcubconv_543
dc.identifier.scopus2-s2.0-69949182410
dc.type.versionpublishedVersion


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