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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Konstantinou, P. | en |
| dc.contributor.author | Roussis, I. G. | en |
| dc.date.accessioned | 2015-11-24T16:47:39Z | - |
| dc.date.available | 2015-11-24T16:47:39Z | - |
| dc.identifier.issn | 0026-3788 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9217 | - |
| dc.rights | Default Licence | - |
| dc.subject | pseudomonas-fluorescens-mc50 | en |
| dc.subject | inactivation | en |
| dc.subject | purification | en |
| dc.title | Some properties of extracellular lipase from Pseudomonas 92 | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000077770400007 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1998 | - |
| heal.abstract | Extracellular lipase from Pseudomonas 92 was partially purified. Enzyme preparation exhibited lipase rather than esterase activity, since it hydrolysed p-nitrophenyl-caproate and beta-naphthyl-caproate to a greater extent in the presence of sodium taurocholate. It was sensitive to EDTA and serine specific inhibitors, and exhibited maximum activity at 37 degrees C and pH 8.0. Lipase retained 50% of its activity at 55 or 65 degrees C and 25% at 95 degrees C. Calcium stabilised the enzyme at 55 or 65 degrees C, but not at 95 degrees C. It exhibited no increase in apparent hydrophobicity after treatments at 55 or 65 degrees C. | 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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