Probing the role of cation-π interaction in the thermotolerance and catalytic performance of endo-polygalacturonases.

ABSTRACT: Understanding the dynamics of the key pectinase, polygalacturonase, and improving its thermotolerance and catalytic efficiency are of importance for the cost-competitive bioconversion of pectic materials. By combining structure analysis and molecular dynamics (MD) simulations, eight mutagenesis sites having the potential to form cation-π interactions were identified in the widely used fungal endo-polygalacturonase PG63. In comparison to the wild-type, three single mutants H58Y, T71Y and T304Y showed improved thermostability (the apparent T_ms increased by 0.6-3.9 °C) and catalytic efficiency (by up to 32-fold). Chromatogram analysis of the hydrolysis products indicated that a larger amount of shorter sugars were released from the polygalacturonic acid by these three mutants than

SUBMITTER: Tu T 

PROVIDER: S-EPMC5143973 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature