Casein and cheese peptide degradation by Enterococcus durans FC12 isolated from feta cheese

dc.contributor.authorIgoumenidou, V.en
dc.contributor.authorLambropoulos, I.en
dc.contributor.authorRoussou, I.en
dc.contributor.authorRoussis, I. G.en
dc.date.accessioned2015-11-24T16:53:25Z
dc.date.available2015-11-24T16:53:25Z
dc.identifier.issn0890-5436-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10015
dc.rightsDefault Licence-
dc.subjectenterococcus duransen
dc.subjectcaseinen
dc.subjectcheese peptideen
dc.subjectgrowthen
dc.subjectproteinaseen
dc.subjectsensory characteristicsen
dc.subjectlactobacillus-caseien
dc.subjectlactococcus-lactisen
dc.subjectmozzarella cheeseen
dc.subjectmilk cheeseen
dc.subjectgoats-milken
dc.subjectmanufactureen
dc.subjectstartersen
dc.subjectmicrofloraen
dc.subjectidentificationen
dc.titleCasein and cheese peptide degradation by Enterococcus durans FC12 isolated from feta cheeseen
heal.abstractThe growth of Enterococcus durans FC12 isolated from Feta cheese in broths containing casein, casein hydrolysate or cheese water-soluble extract as sole nitrogen source was studied. FC12 assimilated casein hydrolysate and casein, the former at a higher extent, while it also grew in the presence of 4% NaCl. It assimilated at a similar extent cow, ewe or goat casein, and it grew rapidly using cheese soluble nitrogenous materials. The cell-envelope enzyme preparation of E. durans FC12 hydrolysed both a-casein and beta-caseins, the latter more rapidly, producing three main peptides. It also hydrolysed two peptides analog to the cheese peptide alpha s1-CNf1-23 that is a key peptide in the first steps of cheese proteolysis. FC12 cell-envelope enzyme preparation degraded the above caseins and peptides in the presence of 4% NaCl. The ability of E. durans FC12 to assimilate casein and cheese soluble nitrogenous materials along with the ability of its cell-envelope enzyme preparation to hydrolyse caseins and peptides analog to the alpha s1-CNf1-23 indicates that the FC12 strain may be useful in cheese proteolysis as an adjunct culture.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDoi 10.1081/Fbt-200063468-
heal.identifier.secondary<Go to ISI>://000231562000006-
heal.identifier.secondaryhttp://www.tandfonline.com/doi/pdf/10.1081/FBT-200063468-
heal.journalNameFood Biotechnologyen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2005-
heal.publisherTaylor & Francisen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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