Modifying Surface Charges of a Thermophilic Laccase Toward Improving Activity and Stability in Ionic Liquid.

ABSTRACT: The multicopper oxidase enzyme laccase holds great potential to be used for biological lignin valorization alongside a biocompatible ionic liquid (IL). However, the IL concentrations required for biomass pretreatment severely inhibit laccase activity. Due to their ability to function in extreme conditions, many thermophilic enzymes have found use in industrial applications. The thermophilic fungal laccase from Myceliophthora thermophila was found to retain high levels of activity in the IL [C₂C₁Im][EtSO₄], making it a desirable biocatalyst to be used for lignin valorization. In contrast to [C₂C₁Im][EtSO₄], the biocompatibility of [C₂C₁Im][OAC] with the laccase was markedly lower. Severe inhibitio

SUBMITTER: Stevens JC 

PROVIDER: S-EPMC9213733 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature