Heterologous expression and biochemical characterization of a GHF9 endoglucanase from the termite Reticulitermes speratus in Pichia pastoris.

ABSTRACT:

Background

Cellulases are of great significance for full utilization of lignocellulosic biomass. Termites have an efficient ability to degrade cellulose. Heterologous production of the termite-origin cellulases is the first step to realize their industrial applications. The use of P. pastoris for the expression of recombinant proteins has become popular. The endoglucanase from Reticulitermes speratus (RsEG), belonging to glycoside hydrolase family 9 (GHF9), has not been produced in P. pastoris yet.

Results

A mutant RsEG_m (G91A/Y97W/K429A) was successfully overexpressed in P. pastoris. RsEG_m, with optimum pH 5.0, was active over the pH range of 4.0 to 9.0, and exhibited superior pH stability over between pH 4.0 and pH 11.0. It displayed the highest activ

SUBMITTER: Zhang P 

PROVIDER: S-EPMC5984754 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature