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dc.contributor.authorAlbaser, Abdulhadi
dc.contributor.authorKazana, Eleanna
dc.contributor.authorBennett, Mark
dc.contributor.authorCebeci, Fatma
dc.contributor.authorLuang-In, Vijitra
dc.contributor.authorSpanu, Pietro D.
dc.contributor.authorRossiter, John T.
dc.date.accessioned2020-12-03T12:20:30Z
dc.date.available2020-12-03T12:20:30Z
dc.date.issued2016en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12403/2274
dc.description.abstractA Citrobacter strain (WYE1) was isolated from a UK soil by enrichment using the glucosinolate sinigrin as sole carbon source. The enzyme myrosinase was purified using a combination of ion exchange and gel filtration to give a pure protein of approximately 66 kDa. The N-terminal amino acid and internal peptide sequence of the purified protein were determined and used to identify the gene, which, based on InterPro sequence analysis, belongs to the family GH3, contains a signal peptide, and is a periplasmic protein with a predicted molecular mass of 71.8 kDa. A preliminary characterization was carried out using protein extracts from cell-free preparations. The apparent KM and Vmax were 0.46 mM and 4.91 mmol dm(-3) min(-1) mg(-1), respectively, with sinigrin as substrate. The optimum temperature and pH for enzyme activity were 25 °C and 6.0, respectively. The enzyme was marginally activated with ascorbate by a factor of 1.67.en_US
dc.language.isoengen_US
dc.relation.isversionof10.1021/acs.jafc.5b05381en_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.titleDiscovery of a bacterial glycoside hydrolase family 3 (GH3) #-glucosidase with myrosinase activity from a Citrobacter strain isolated from soilen_US
dc.typearticleen_US
dc.contributor.departmentBayburt Üniversitesi, Sağlık Bilimleri Fakültesi, Beslenme ve Diyetetik Bölümüen_US
dc.contributor.authorID0000-0003-4715-6689en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Başka Kurum Yazarıen_US
dc.contributor.institutionauthorCebeci, Fatma


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