Preparation of salidroside with n-butyl β-D-glucoside as the glycone donor via a two-step enzymatic synthesis catalyzed by an immobilized β-glucosidase from bitter almond
Authors
Wang, Feng
Huang, Dengfa
Ma, Yong
Zhang, Fuming
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2019-07-04
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Preparation of salidroside with n-butyl β-D-glucoside as the glycone donor via a two-step enzymatic synthesis catalyzed by an immobilized β-glucosidase from bitter almond, F. Wang, D. Huang, Y. Ma, F. Zhang, R. J. Linhardt, Biocatalysis and Biotransformation, 37, 246–260, 2019.
Abstract
β-Glucosidase from bitter almonds was immobilized on epoxy group-functionalized beads for catalyzing salidroside synthesis in a two-step process with n-butyl-β-D-glucoside (BG) as the glucosyl donor. The formation of salidroside ((0.59 ± 0.02) M) at a yield of 39.04%±1.25% was accomplished in 8 h by the transglucosylation of immobilized β-glucosidase at pH 8.0 and 50 °C when the ratio of BG to tyrosol was 1:2 (mol/mol). A study on the influence of different glycosyl acceptors demonstrated that the yield of the glucosylation reaction of phenylmethanol and cyclohexanol was higher than that of either phenol or cyclohexanol. This may account for the selectivity of the immobilized enzyme towards the alcoholic hydroxyl group of tyrosol in the salidroside synthesis reaction. A study on the synthesis of BG via the reverse hydrolysis of immobilized β-glucosidase showed that a yield of 78.04%±2.2% BG can be obtained with a product concentration of (0.23 ± 0.015) M.
Description
Biocatalysis and Biotransformation, 37, 246–260
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.
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)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Biocatalysis and Biotransformation
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
Biocatalysis and Biotransformation
https://harc.rpi.edu/
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https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1080/10242422.2018.1549236