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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Triantafyllidou, M. | en |
dc.contributor.author | Roussis, I. G. | en |
dc.date.accessioned | 2015-11-24T16:53:33Z | - |
dc.date.available | 2015-11-24T16:53:33Z | - |
dc.identifier.issn | 0026-3788 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10036 | - |
dc.rights | Default Licence | - |
dc.subject | pseudomonas (proteinase) | en |
dc.subject | inactivation | en |
dc.subject | milk | en |
dc.title | Changes in the apparent hydrophobicity of Pseudomonas 31 proteinase after heat treatments | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.secondary | <Go to ISI>://000083056600005 | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.publicationDate | 1999 | - |
heal.abstract | Proteinase 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.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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