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    Enzymatic Bioconversion of Cycloastragenol-6-O-β-D-glucoside into Cycloastragenol by a Novel Recombinant β-Glucosidase from Phycicoccus sp. Soil748

    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.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    Other Contributors
    Date Issued
    2020-03-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    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.
    Metadata
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    URI
    https://doi.org/10.1016/j.procbio.2019.11.006; https://hdl.handle.net/20.500.13015/5527
    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;
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