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Improved Alkyl Glycoside Synthesis by trans‐Glycosylation through Tailored Microenvironments of Immobilized β‐Glucosidase
Author(s) -
Hoffmann Christian,
Grey Carl,
Pinelo Manuel,
Woodley John M.,
Daugaard Anders E.,
Adlercreutz Patrick
Publication year - 2020
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.201900680
Subject(s) - selectivity , chemistry , glycosylation , alkyl , imidazole , thiol , immobilized enzyme , hydrolysis , glycoside , enzyme , enzymatic hydrolysis , thermotoga maritima , combinatorial chemistry , stereochemistry , organic chemistry , biochemistry , catalysis , escherichia coli , gene
We present how the microenvironment can directly improve biocatalytic selectivity of immobilized β‐glucosidase. β‐Glucosidase from Thermotoga neapolitana was immobilized on a variety of functionalized off‐stoichiometric thiol‐ene (OSTE) particles, where highest activities were observed for thiol and imidazole functional particles. Compared to the soluble enzyme, the selectivity (r s /r h ) between trans‐glycosylation of p‐nitrophenyl β‐D‐glucopyranoside (pNPG) with 1‐propanol over hydrolysis was increased by a factor of 2–3 using particles containing imidazole (r s /r h of 6.7) and carboxylic acid moieties (r s /r h of 9.2), respectively. These results demonstrate clearly that enzyme selectivity depends directly on the local environment of the enzyme with the support.