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- W2387254101 abstract "β-Glucosidases,as a specific group of glycosyl hydrolase could catalyze the hydrolysis of β-1,4-glycosidic bond presented in short-chain oligosaccharides(containing 2—6 monosaccharides),are widely used in the degradation of cellulose,the improvement of food flavor and so on.The gene of Aspergillus aculeatus NO.F-50 β-glucosidase Ⅰ was cloned and integrated into Pichia pastoris GS115,in which β-glucosidase Ⅰ can be expressed and secreted in an active form.The recombinant β-glucosidase Ⅰ had an optimum pH of 5.0 and an optimum temperature of 65 ℃ using 4-nitrophenyl-β-D-glucopyranoside(pNPG) as substrate.The highest hydrolytic activity and protein expression level at 50 ℃ in the culture supernatant of recombinant strain were up to 33.8 U/mL and 0.388 mg/mL,respectively.The recombinant β-glucosidase Ⅰ was found to be able to catalyze the synthesis of alkyl glucoside through reverse-hydrolysis or trans-glycosylation reaction.Some major influential factors in water/organic two-phase system such as pH value,water content,overall concentration of glucose and enzyme concentration were optimized.The yield of butyl glucoside,hexyl glucoside,octyl glucoside and decyl glucoside was 51.4%,28.8%,6.9% and 3.0%,respectivly." @default.
- W2387254101 created "2016-06-24" @default.
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- W2387254101 date "2012-01-01" @default.
- W2387254101 modified "2023-09-25" @default.
- W2387254101 title "Expression of Aspergillus aculeatus β-Glucosidase I Gene in Pichia pastoris and Its Application on the Synthsis of Alkyl Glucoside" @default.
- W2387254101 hasPublicationYear "2012" @default.
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