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dc.contributor.authorKara, Hatibe Ertürk
dc.contributor.authorTuran, Yusuf
dc.contributor.authorEr, Aylin
dc.contributor.authorAcar, Mesut
dc.contributor.authorTumay, Sabiha
dc.contributor.authorSinan, Selma
dc.date.accessioned2019-10-17T07:43:34Z
dc.date.available2019-10-17T07:43:34Z
dc.date.issued2014en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12462/7684
dc.descriptionEr, Aylin (Balıkesir Author)en_US
dc.description.abstractThe greater wax moth, Galleria mellonella, is one of the most ruinous pests of honeycomb in the world. Beta-glucosidases are a type of digestive enzymes that hydrolytically catalyzes the beta-glycosidic linkage of glycosides. Characterization of the beta-glucosidase in G. mellonella could be a significant stage for a better comprehending of its role and establishing a safe and effective control procedure primarily against G. mellonella and also some other insect pests. Laboratory reared final instar stage larvae were randomly selected and homogenized for beta-glucosidase activity assay and subsequent analysis. The enzyme was purified to apparent homogeneity by salting out with ammonium sulfate and using sepharose-4B-L-tyrosine-1-naphthylamine hydrophobic interaction chromatography. The purification was 58-fold with an overall enzyme yield of 29%. The molecular mass of the protein was estimated as ca. 42 kDa. The purified beta-glucosidase was effectively active on para/ortho-nitrophenyl-beta-D-glucopyranosides (p-/o-NPG) with Km values of 0.37 and 1.9 mM and Vmax values of 625 and 189 U/mg, respectively. It also exhibits different levels of activity against para-nitrophenyl-beta-D-fucopyranoside (p-NPF), para/ortho-nitrophenyl beta-D-galactopyranosides (p-/o-NPGal) and p-nitrophenyl 1-thio-beta-D-glucopyranoside. The enzyme was competitively inhibited by beta-gluconolactone and also was very tolerant to glucose against p-NPG as substrate. The Ki and IC50 values of delta-gluconolactone were determined as 0.021 and 0.08 mM while the enzyme was more tolerant to glucose inhibition with IC50 value of 213.13 mM for p-NPG.en_US
dc.publisherWiley-Blackwellen_US
dc.rightsinfo:eu-repo/semantics/embargoedAccessen_US
dc.subjectGalleria Mellonellaen_US
dc.subjectBeta-Glucosidaseen_US
dc.subjectPurificationen_US
dc.subjectCharacterizationen_US
dc.titlePurification and characterization of beta-glucosidase from greater wax moth galleria mellonella l. (lepidoptera: pyralidaei)en_US
dc.typearticleen_US
dc.relation.journalArchives of Insect Biochemistry and Physiologyen_US
dc.contributor.departmentFen Edebiyat Fakültesien_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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