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

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.

Multifunctional Silica Nanoparticles for Covalent Immobilization of Highly Sensitive Proteins

“…We will demonstrate below that these proteins are inappropriate models for testing biocompatible surface properties and mild immobilization methods due to their robust tertiary architecture. Although stable lipases have been shown to be active after sol-gel immobilization, [ 12,13 ] the incorporation of proteins even into the channels of porous nanoparticles [ 14 ] suffers from the presence of diffusion barriers as well as potential leakage.…”

Synergistic effects of amine and protein modified epoxy-support on immobilized lipase activity

“…However, lipase-based catalysts are usually expensive, unstable, and are difficult to be efficiently separated from reaction systems used in industrial production [5]. To address this, various immobilization techniques have been developed to improve their stabilization, reutilization [6,7] and other properties [8][9][10]. For example, the enzyme aggregation reduced in the immobilization processes compared to free enzyme and generated favorable environment [11,12].…”

Immobilizing Yarrowia lipolytica Lipase Lip2 via Improvement of Microspheres by Gelatin Modification

“…Various immobilization techniques have been developed to improve the stability, reutilization, and other properties of biocatalyst [6,7]. During the immobilization process, enzyme aggregation was reduced when compared to the free enzyme, thus generating a more favorable environment [8].…”