In Silico Screening of Laccases with Universality based on Structural Analysis

Abstract Laccases have the advantages of non-specific oxidation and excellent catalytic activity. It is widely used in biomedicine, biosensor, and pollutant degradation. However, there are differences in the structure, substrate range, and fermentative expression of laccases depending on the source. In order to select a laccase with universality, we selected four representative laccases to analyze their catalytic properties from the aspects of sequence homology, isoelectric point, charged characteristics, active pocket, binding energy and the distance between the catalytic site and the substrate. The correlation analysis showed that the screening strategy was mainly based on structural analysis for a comprehensive evaluation through its activity and stability. The B. subtilis-derived laccase (CotA) with large and hydrophilic substrate binding pocket was screened out efficiently. It has the advantages of broad extent for substrates and strong alkali-resistance abilities. Therefore, this silico screening method can screen out suitable enzymes for specific application targets conveniently, which can lay the theoretical foundation for subsequent catalytic application studies.