Improving the thermostability of a fungal GH11 xylanase via site-directed mutagenesis guided by sequence and structural analysis.

ABSTRACT:

Background

Xylanases have been widely employed in many industrial processes, and thermophilic xylanases are in great demand for meeting the high-temperature requirements of biotechnological treatments. In this work, we aim to improve the thermostability of XynCDBFV, a glycoside hydrolase (GH) family 11 xylanase from the ruminal fungus Neocallimastix patriciarum, by site-directed mutagenesis. We report favorable mutations at the C-terminus from B-factor comparison and multiple sequence alignment.

Results

C-terminal residues 207-NGGA-210 in XynCDBFV were discovered to exhibit pronounced flexibility based on comparison of normalized B-factors. Multiple sequence alignment revealed that beneficial residues 207-SSGS-210 are highly conserved in GH11 xylanases. Thus, a recomb

SUBMITTER: Han N 

PROVIDER: S-EPMC5442702 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature