In silico Design of Laccase Thermostable Mutants From Lacc 6 of Pleurotus Ostreatus.

ABSTRACT: Fungal laccase enzymes have a great biotechnological potential for bioremediation processes due to their ability to degrade compounds such as ρ-diphenol, aminophenols, polyphenols, polyamines, and aryldiamines. These enzymes have activity at different pH and temperature values, however, high temperatures can cause partial or total loss of enzymatic activity, so it is appropriate to do research to modify their secondary and/or tertiary structure to make them more resistant to extreme temperature conditions. In silico, a structure of the Lacc 6 enzyme of Pleurotus ostreatus was constructed using a laccase of Trametes versicolor as a template. From this structure, 16 mutants with possible resistance at high temperature due to ionic interactions, salt bridges and disulfide

SUBMITTER: Diaz R 

PROVIDER: S-EPMC6247816 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature