Isolation,purification and enzymatic properties ofβ-glucosidase from Aspergillus versicolor
The experiment aimed to isolate and purify β-glucosidase from Aspergillus versicolor fermentation broth and study the enzymatic properties of β-glucosidase.β-glucosidase was isolated from Aspergillus versicolor and purified by ENrich Q,10×100 anion exchange chromatography.The molecular weight was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)and the properties of the enzyme were studied.The results showed that the β-glucosidase with molecular mass 88.5 kDa was obtained after purification.The purification fold,recovery and specific enzyme activity were 53.44,70.78％and 1438.11 U/mg,respectively.The optimum reaction temperature and pH of the β-glucosidase were 50 ℃ and 5.5,respectively,and the enzyme had good stability at 20～50 ℃ and pH 5.0～7.0.The metal ions Mn2+could promote the β-glucosidase activity,while metal ions Co2+,Cu2+,Cd2+could inhibit the β-glucosidase activity,whereas Na+,Mg2+,K+,Ca2+,Ba2+had no effect.With salicylin as substrate,the Km was 0.48 mg/mL and the Vm was 0.04 mg/(min·mL).The study isolated a strain from the fermentation broth of Aspergillus versicolor successfully and its enzymatic properties were studied,providing data support for the application of cellulose based feed.
Aspergillus versicolorβ-glucosidaseisolation and purificationenzymatic property
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