Author
Cheng, Leiyu; Zhang, Han; Liang, Hao; Sun, Xinxiao; Shen, Xiaolin; Wang, Jia; Wang, Wenya; Yuan, Qipeng; Ri, Hyon Il; Kim, Tae Mun; Kang, Myong Su; Linhardt, Robert J.
Other Contributors
Date Issued
2020-03-01
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Enzymatic Bioconversion of Cycloastragenol-6-O-β-D-glucoside into Cycloastragenol by a Novel Recombinant β-Glucosidase from Phycicoccus sp. Soil748, L. Cheng, H. Zhang, H. Liang, X. Sun, X. Shen, J. Wang, W. Wang, Q. Yuan, H.-I. Ri, T.-M. Kim, M.-S. Kang, R. J. Linhardt, Process Biochemistry, 90, 81–88, 2019.
Abstract
Cycloastragenol (CA), the genuine sapogenin of astragaloside from Astragalus membranaceus, exhibits diverse pharmaceutical activities. Recently, the efficient production of CA has received considerable attention due to rapidly increasing market demands. In this study, enzyme mining was conducted, based on skeleton and glycosyl similarity, to explore an efficient β-glucosidase for CA preparation. A novel β-glucosidase from Phycicoccus sp. Soil748 (Bgps) was discovered, possessing the efficient conversion rate for cycloastragenol-6-O-β-D-glucoside (CMG) into CA. The optimum temperature and pH value of Bgps were determined as 45 °C and 7.0. The results of kinetic analysis suggested that Bgps catalyzed deglycosylation of CMG more efficiently than other substrates. Furthermore, the optimal substrate concentration of Bgps was up to 80 mg/mL with the conversion rate as 99.2%, suggesting its potential application in CA industrial production by biotransformation.;
Description
Process Biochemistry, 90, 81–88; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Process Biochemistry; https://harc.rpi.edu/;
Access
https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.procbio.2019.11.006;
