Abstract
AbstractWe 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 (rs/rh) 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 (rs/rh of 6.7) and carboxylic acid moieties (rs/rh of 9.2), respectively. These results demonstrate clearly that enzyme selectivity depends directly on the local environment of the enzyme with the support.
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