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Improved Alkyl Glycoside Synthesis by trans‐Glycosylation through Tailored Microenvironments of Immobilized β‐Glucosidase
ChemPlusChem ( IF 3.0 ) Pub Date : 2019-12-17 , DOI: 10.1002/cplu.201900680
Christian Hoffmann 1 , Carl Grey 2 , Manuel Pinelo 1 , John M. Woodley 1 , Anders E. Daugaard 1 , Patrick Adlercreutz 2
Affiliation  

Here, we present for the first time, how the micro‐environment can directly improve biocatalytic selectivity of immobilized ß‐glucosidase. ß‐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 ß‐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.

中文翻译:

通过固定化的β-葡萄糖苷酶微环境的反式糖基化改善烷基糖苷的合成

在这里,我们首次展示了微环境如何直接改善固定化β-葡萄糖苷酶的生物催化选择性。来自Theratoga neapolitana的β-葡萄糖苷酶被固定在各种功能化的非化学计量的硫醇烯(OSTE)颗粒上,其中硫醇和咪唑功能颗粒的活性最高。与可溶性酶相比,使用含咪唑的颗粒(对-硝基苯基ß-D-吡喃葡萄糖苷(pNPG)与1-丙醇进行水解的糖基化之间的选择性(rs / rh)比水解增加了2-3倍) / rh为6.7)和羧酸部分(rs / rh为9.2)。这些结果清楚地表明,酶的选择性直接取决于带有支持物的酶的局部环境。
更新日期:2019-12-18
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