Purification and characterization of an alkaline pectin lyase produced by a newly isolated brevibacillus borstelensis (p35) and its applications in fruit juice and oil extraction

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dc.authorid35511537500
dc.authorid6506121388
dc.authorid7006472528
dc.authorid56079018600
dc.authorid36448719800
dc.authorid6507268431
dc.authorid6602542681
dc.contributor.authorDemir N.
dc.contributor.authorNadaroglu H.
dc.contributor.authorDemir Y.
dc.contributor.authorIsik C.
dc.contributor.authorTaskin E.
dc.contributor.authorAdiguzel A.
dc.contributor.authorGulluce M.
dc.date.accessioned20.04.201910:49:12
dc.date.accessioned2019-04-20T21:44:10Z
dc.date.available20.04.201910:49:12
dc.date.available2019-04-20T21:44:10Z
dc.date.issued2014
dc.departmentBayburt Üniversitesien_US
dc.description.abstractAn alkaline pectin lyase (Pnl) (EC 4.2.2.10) secreted by Brevibacillus borstelensis P35 (genBank number: FJ417406) was purifed using ammonium sulfate fractionation, anion exchange chromatography on DEaE-cellulose and gel fltration chromatography on Sephadex g-150. The pH and temperature optima of the enzyme were found to be 8.0 and 60 °C. The enzyme does not loose activity up to 60 °C if exposed for 1 h. The values of Kmand Vmax of the enzyme were 0.625 mg/ml and 126.32 s-1, respectively. The molecular weight was found to be 36 ± 01 kDa. The presence of 10 mM concentration of Ca2+, Cu2+, Mn2+, Mg2+, Zn2+, Hg2+, Fe2+ and EDTa, L-cystein, ascorbic acid signifcantly enhanced the Pnl of the purifed enzyme. In the course of the laboratory trials, it was demonstrated that Pnl from B. borstelensis (P35) could be successfully applied to the production and clarif-cation of fruit juice and oil extraction. © Springer-Verlag Berlin Heidelberg 2014en_US
dc.identifier.doi10.1007/s00217-014-2198-8
dc.identifier.endpage135
dc.identifier.issn1438-2377
dc.identifier.issue1
dc.identifier.scopus2-s2.0-85027933604en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage127
dc.identifier.urihttps://dx.doi.org/10.1007/s00217-014-2198-8
dc.identifier.urihttps://hdl.handle.net/20.500.12403/787
dc.identifier.volume239
dc.identifier.wosWOS:000338224600013en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringer Verlag
dc.relation.ispartofEuropean Food Research and Technologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBrevibacillus borstelensis (P35)
dc.subjectJuice clarification
dc.subjectOil extraction
dc.subjectPectin
dc.subjectPectin lyase
dc.subjectPurifcation
dc.subjectAlkalinity
dc.subjectAscorbic acid
dc.subjectChromatography
dc.subjectEnzymes
dc.subjectExtraction
dc.subjectFruit juices
dc.subjectFruits
dc.subjectIon exchange
dc.subjectManganese
dc.subjectOil shale
dc.subjectBrevibacillus borstelensis (P35)
dc.subjectOil extraction
dc.subjectPectin
dc.subjectPectin-lyase
dc.subjectPurifcation
dc.subjectEnzyme activity
dc.subjectBrevibacillus borstelensis
dc.subjectBrevibacillus borstelensis (P35)
dc.subjectJuice clarification
dc.subjectOil extraction
dc.subjectPectin
dc.subjectPectin lyase
dc.subjectPurifcation
dc.subjectAlkalinity
dc.subjectAscorbic acid
dc.subjectChromatography
dc.subjectEnzymes
dc.subjectExtraction
dc.subjectFruit juices
dc.subjectFruits
dc.subjectIon exchange
dc.subjectManganese
dc.subjectOil shale
dc.subjectBrevibacillus borstelensis (P35)
dc.subjectOil extraction
dc.subjectPectin
dc.subjectPectin-lyase
dc.subjectPurifcation
dc.subjectEnzyme activity
dc.subjectBrevibacillus borstelensis
dc.titlePurification and characterization of an alkaline pectin lyase produced by a newly isolated brevibacillus borstelensis (p35) and its applications in fruit juice and oil extractionen_US
dc.typeArticleen_US

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