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dc.contributor.authorTriantafyllidou, M.en
dc.contributor.authorRoussis, I. G.en
dc.date.accessioned2015-11-24T16:53:39Z-
dc.date.available2015-11-24T16:53:39Z-
dc.identifier.issn0026-3788-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10048-
dc.rightsDefault Licence-
dc.subjectpseudomonas fluorescens (proteinase)en
dc.subjectpsychrotrophic pseudomonadsen
dc.subjectstable proteasesen
dc.subjectmilk-proteinsen
dc.subjectpurificationen
dc.subjectproteolysisen
dc.subjectaft-36en
dc.titleCharacterization and heat inactivation of extracellular proteinase from Pseudomonas fluorescens TR2en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000081757500005-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1999-
heal.abstractExtracellular proteinase from Pseudomonas fluorescens was purified to SDS-PAGE homogeneity. The enzyme appeared to be a neutral endopeptidase containing zinc. It had a molecular weight of 43.5 KDa with K-m 0.07 mM and Vmax 20.2 units/mu g protein, for casein as substrate. It was heat resistant at temperatures above 80 degrees C in the presence of calcium, while it appeared to be sensitive at lower temperatures. The enzyme was autolyzed at 60 degrees C, while it was not in the presence of casein. In the latter case, proteinase hydrolyzed the casein. Proteinase studied hydrolyzed both beta- and alpha(s)- caseins of cow's and ewe's milks in the order beta->alpha(s). Ewe's caseins appeared to be more resistant to proteinase hydrolysis than cow's caseins.en
heal.publisherVOLKSWIRTSCHAFTLICHER VERLAGen
heal.journalNameMilchwissenschaft-Milk Science Internationalen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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