Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases

Abstract

Oxidoreductases are widely recognized for their capability to degrade phenolic pollutants and versatile. However, the lack of enzyme stability makes this technique unrealistic for industrial applications. In order to enhance their catalytic activity, stability and reusability, oxidoreductases namely laccases and peroxidases were entrapped in sol–gel silica and their catalytic activities were measured by an enzymatic assay using 2,6-dimethoxyphenol and guaiacol as substrates, respectively. The sol–gel silica matrices acted as a polymeric framework around the enzyme is a promising tool for improving enzyme stability. After entrapment, the catalytic activity and stability of sol–gel laccase and peroxidase toward pH, temperature and storage duration remarkably enhanced. [Figure not available: see fulltext.]