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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Roussis, I. G. | en |
| dc.contributor.author | Matselis, E. | en |
| dc.contributor.author | Papamichael, E. M. | en |
| dc.contributor.author | Sakarellos-Daitsotis, M. | en |
| dc.contributor.author | Triantafyllidou, M. | en |
| dc.date.accessioned | 2015-11-24T16:58:21Z | - |
| dc.date.available | 2015-11-24T16:58:21Z | - |
| dc.identifier.issn | 0026-3788 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10680 | - |
| dc.rights | Default Licence | - |
| dc.subject | flavobacterium mtr3 (extracellular enzymes) | en |
| dc.subject | psychrotrophic bacteria | en |
| dc.subject | cheddar cheese | en |
| dc.subject | milk-proteins | en |
| dc.subject | proteolysis | en |
| dc.subject | pseudomonas | en |
| dc.title | Extracellular proteinase and lipase activity of Flavobacterium MTR3 | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000079672400005 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1999 | - |
| heal.abstract | Flavobacterium MTR3 by culturing in skim milk produced significant proteinase but limited lipase activity. Proteinase activity at 25 and 5 degrees C was observed during idiophase, when bacterial counts were 10(7)-10(8) cfu/ml. Proteinase production was higher in agitated cultures and it was not affected by iron addition. Lipase production was not stimulated by culture agitation or iron addition. Addition of ascorbic acid limited maximum bacterial counts and enzyme production. Extracellular proteinase preparation from Fl. MTR3 was heat labile and was not stabilised by calcium. It exhibited maximum activity at 37-45 degrees C and in alkaline pH region. Kinetic parameters, K-m and V-max values, were estimated 0.06 mM and 32.3 units/.g protein respectively, using casein as substrate. It hydrolysed faster beta- than alpha-casein, and cow's than ewe's milk caseins. Proteinase studied exhibited leucine aminopeptidase activity, but casein peptide hydrolysis was low. | en |
| heal.publisher | VOLKSWIRTSCHAFTLICHER VERLAG | en |
| heal.journalName | Milchwissenschaft-Milk Science International | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
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