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dc.rights.licenseopenen_US
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorTHERON, Louwrens Wiid
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorBELY, Marina
dc.contributor.authorDIVOL, Benoit
dc.date.accessioned2021-04-27T12:42:16Z
dc.date.available2021-04-27T12:42:16Z
dc.date.issued2017-02-14
dc.identifier.issn0022-5142en_US
dc.identifier.urioai:crossref.org:10.1002/jsfa.8217
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/27116
dc.description.abstractEnBACKGROUND MpAPr1, encoding an acid protease from the wine yeast Metschnikowia pulcherrima IWBT Y1123, was previously isolated and shown to display potential activity against casein and grape proteins. However, its characterisation remained partial. RESULTS MpAPr1 was cloned into the pGAPZαA vector and transformed into Komagataella pastoris X33 for heterologous expression. After verification of activity, the enzyme properties were characterised. Protease activity within the concentrated supernatant was retained over a pH range of 3.0 to 5.0 and between 10 °C and 50 °C. Optimal conditions for protease activity were found at 40 °C and pH 4.5. Activity was mostly unaffected by the presence of metal ions with the exception of Cu2+ and Ni2+. Furthermore, proteolytic activity was retained in the presence of sugar and ethanol. pH and temperature conditions for MpAPr1 expression in K. pastoris were optimised. Purification was achieved by means of cation exchange chromatography and kinetic parameters (Km and Vmax) were determined. MpAPr1 activity against grape proteins was confirmed, but the extent of the degradation was dependent on the nature of these proteins and the environmental conditions. CONCLUSION Overall, the results suggest that MpAPr1 could be applied in food biotechnology processes such as winemaking.
dc.language.isoENen_US
dc.sourcecrossref
dc.subject.enMetschnikowia pulcherrima; MpAPr1
dc.subject.enAspartic protease
dc.subject.enEnzyme characterisation
dc.subject.enProtein purification
dc.subject.enWine
dc.title.enCharacterisation of the enzymatic properties of MpAPr1, an aspartic protease secreted by the wine yeast Metschnikowia pulcherrima
dc.title.alternativeJ Sci Food Agric.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1002/jsfa.8217en_US
dc.subject.halSciences du Vivant [q-bio]/Biologie végétaleen_US
dc.identifier.pubmed28098337en_US
bordeaux.journalJournal of the Science of Food and Agricultureen_US
bordeaux.page3584-3593en_US
bordeaux.volume97en_US
bordeaux.hal.laboratoriesUnité de Recherche Oenologie - EA 4577en_US
bordeaux.issue11en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionINRAE
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcedissemin
hal.exportfalse
workflow.import.sourcedissemin
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