dc.contributor.author | Kara, Hatibe Ertürk | |
dc.contributor.author | Turan, Yusuf | |
dc.contributor.author | Er, Aylin | |
dc.contributor.author | Acar, Mesut | |
dc.contributor.author | Tumay, Sabiha | |
dc.contributor.author | Sinan, Selma | |
dc.date.accessioned | 2019-10-17T07:43:34Z | |
dc.date.available | 2019-10-17T07:43:34Z | |
dc.date.issued | 2014 | en_US |
dc.identifier.uri | https://hdl.handle.net/20.500.12462/7684 | |
dc.description | Er, Aylin (Balıkesir Author) | en_US |
dc.description.abstract | The 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.publisher | Wiley-Blackwell | en_US |
dc.rights | info:eu-repo/semantics/embargoedAccess | en_US |
dc.subject | Galleria Mellonella | en_US |
dc.subject | Beta-Glucosidase | en_US |
dc.subject | Purification | en_US |
dc.subject | Characterization | en_US |
dc.title | Purification and characterization of beta-glucosidase from greater wax moth galleria mellonella l. (lepidoptera: pyralidaei) | en_US |
dc.type | article | en_US |
dc.relation.journal | Archives of Insect Biochemistry and Physiology | en_US |
dc.contributor.department | Fen Edebiyat Fakültesi | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |