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dc.creatorVujčić, Zoran
dc.creatorLončar, Nikola L.
dc.creatorDojnov, Biljana
dc.creatorMilovanovic, Aleksandra
dc.creatorVujčić, Miroslava
dc.creatorBožić, Nataša
dc.date.accessioned2018-11-22T00:16:08Z
dc.date.available2018-11-22T00:16:08Z
dc.date.issued2010
dc.identifier.issn0308-8146
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/1060
dc.description.abstractPotato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa. (C) 2009 Elsevier Ltd. All rights reserved.en
dc.publisherElsevier Sci Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142026/RS//
dc.rightsrestrictedAccess
dc.sourceFood Chemistry
dc.subjectLeucyl aminopeptidaseen
dc.subjectPotato tuberen
dc.subjectSolanum tuberosumen
dc.subjectBiotechnologyen
dc.subjectFooden
dc.titleCharacterisation of leucyl aminopeptidase from Solanum tuberosum tuberen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractМиловановиц, Aлександра; Вујциц, Мирослава; Вујчић, Зоран; Дојнов, Биљана; Лончар, Никола; Бозиц, Натаса;
dc.citation.volume121
dc.citation.issue2
dc.citation.spage418
dc.citation.epage423
dc.identifier.wos000276038400016
dc.identifier.doi10.1016/j.foodchem.2009.12.058
dc.citation.other121(2): 418-423
dc.citation.rankaM21
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-76849097216
dc.identifier.rcubKon_2060


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