Enzymatic characteristics of β-glucosidase produced by endophytic fungus Aspergillus aculeatus HZ001 from Polygonum cuspidatum
YU Jie1,2, XU Qinqian1,2, LI Ziyuan1,2, LIU Hongyang1,2, HAO Zaibin1,2, LI Haiyun1,2*
1(College of Chemistry & Bioengineering, Guilin University of Technology, Guilin 541004, China) 2(Guangxi Colleges and Universities Key Laboratory of Food Safety and Detection, Guilin University of Technology, Guilin 541004, China)
Abstract: Polydatin is abundant in the traditional Chinese medicine Polygonum cuspidatum, and the conversion of polydatin to resveratrol by biotransformation technology is an effective method to prepare natural resveratrol products. The cells of endophytic fungus Aspergillus aculeatus HZ001, which isolated from P. cuspidatum, can catalyze polydatin to resveratrol. The enzymatic characteristics of intracellular β-glucosidase produced by this strain were studied. The results showed that the optimum reaction temperature was 60 ℃, good stability was obtained below 60 ℃; and the optimum reaction pH was 4.8 with good stability at pH 3.6-4.0. The β-glucosidase could be activated by Fe2+ with a relative enzyme activity of 120% and significantly inhibited by Ca2+, Co2+, and Mg2+. SDS, mercaptoethanol, and dimethyl sulfoxide also inhibited the enzyme activity, and the highest inhibitory rate of 90% was obtained with EDTA. Under the optimal catalytic conditions, the kinetic parameters of the enzymatic reaction were established with the Km of 2.571 mmol/L and the Vmax of 0.594 μmol/(mL·h).
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