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- W2392177776 abstract "Using ammonium sulfate precipitation,ultrafiltration desalination,ion-exchange and gel filtration column chromatography,a β-xylosidase with molecular weight of 110.8 ku and specific activity of 61.99 IU/mg was purified to homogeneity from culture xylanase solution of Trichoderma reesei Rut C-30.Results of enzymatic properties showed that the optimal reaction condition of the enzyme was: pH value of 3.5;reaction temperature of 60 ℃.The enzyme was stable below 60 ℃ and pH value ranges from 3.0 to 8.0.It had a Km value of 0.29 μmol/mL and Vmax value of 169.99 IU/mg by using p-nitrophenyl-β-D-xylopyranoside as the substrate.Results of enzymatic hydrolysis mechanism indicated that β-xylosidase released xylose from non-reducing ends of xylooligosaccharides by cutting off β-1,4-glycosidic bond.The optimum substrate of β-xylosidase was short-chain xylooligosaccharides.With chain length of xylooligosaccharides increased,the enzyme hydrolysis efficiency decreased gradually and xylan was hardly to be degraded." @default.
- W2392177776 created "2016-06-24" @default.
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- W2392177776 date "2013-01-01" @default.
- W2392177776 modified "2023-09-24" @default.
- W2392177776 title "Purification,Characterization and Hydrolysis Mechanism of β-Xylosidase from Trichoderma reesei" @default.
- W2392177776 hasPublicationYear "2013" @default.
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