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通过溶胶-凝胶固定化提高脂肪酶的活性和对映选择性:具有实际意义的进一步进展。

Increasing the activity and enantioselectivity of lipases by sol-gel immobilization: further advancements of practical interest.

机构信息

Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim/Ruhr, Germany.

出版信息

Nanoscale. 2014 Jun 21;6(12):6220-8. doi: 10.1039/c3nr06317h.

DOI:10.1039/c3nr06317h
PMID:24676487
Abstract

The entrapment of lipases in hydrophobic silicate matrices formed by sol-gel mediated hydrolysis of RSi(OCH3)3/Si(OCH3)4 as originally reported in 1996 has been improved over the years by a number of modifications. In the production of second-generation sol-gel lipase immobilizates, a variety of additives during the sol-gel process leads to increased activity and enhanced stereoselectivity in esterifying kinetic resolution. Recent advances in this type of lipase immobilization are reviewed here, in addition to new results regarding the sol-gel entrapment of the lipase from Burkholderia cepacia. It constitutes an excellent heterogeneous biocatalyst in the acylating kinetic resolution of two synthetically and industrially important chiral alcohols, rac-sulcatol and rac-trans-2-methoxycyclohexanol. The observation that the catalyst can be used 10 times in recycling experiments without losing its significant activity or enantioselectivity demonstrates the practical viability of the sol-gel approach.

摘要

1996 年首次报道的通过 RSi(OCH3)3/Si(OCH3)4 的溶胶-凝胶介导水解形成疏水性硅酸盐基质来捕获脂肪酶,多年来通过多种改进得到了改善。在第二代溶胶-凝胶脂肪酶固定化剂的生产中,溶胶-凝胶过程中的各种添加剂导致酯化动力学拆分的活性和对映选择性增强。本文综述了这种脂肪酶固定化的最新进展,以及关于伯克霍尔德氏菌脂肪酶溶胶-凝胶包埋的新结果。它是酰化动力学拆分两种合成和工业上重要的手性醇(rac-苏氨酸和 rac-反式-2-甲氧基环己醇)的优良非均相生物催化剂。观察到催化剂在回收实验中可以使用 10 次而不会失去其显著的活性或对映选择性,证明了溶胶-凝胶方法的实际可行性。

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