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dc.contributor.authorTriantafyllidou, M.en
dc.contributor.authorRoussis, I. G.en
dc.date.accessioned2015-11-24T16:53:33Z-
dc.date.available2015-11-24T16:53:33Z-
dc.identifier.issn0026-3788-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10036-
dc.rightsDefault Licence-
dc.subjectpseudomonas (proteinase)en
dc.subjectinactivationen
dc.subjectmilken
dc.titleChanges in the apparent hydrophobicity of Pseudomonas 31 proteinase after heat treatmentsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000083056600005-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1999-
heal.abstractProteinase from Pseudomonas 31 appeared to be a metalloenzyme. The remaining activity and the increase in the apparent hydrophobicity after heating the proteinase at 55 degrees C for 15 min were 10 and 60%, respectively, relating to unheated samples. On the other hand, the above parameters after the treatment at 95 degrees C for 15 min were 14 and 140%, respectively, indicating that different phenomena occur at these 2 temperatures. After heating the proteinase at 55 degrees C for 15 min in the presence of casein, the above 2 parameters were 16 and 35%, respectively, indicating the involvement in the inactivation of the proteinase at 55 degrees C.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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