Determinants for the improved thermostability of a mesophilic family 11 xylanase predicted by computational methods.

ABSTRACT:

Background

Xylanases have drawn much attention owing to possessing great potential in various industrial applications. However, the applicability of xylanases, exemplified by the production of bioethanol and xylooligosaccharides (XOSs), was bottlenecked by their low stabilities at higher temperatures. The main purpose of this work was to improve the thermostability of AuXyn11A, a mesophilic glycoside hydrolase (GH) family 11 xylanase from Aspergillus usamii E001, by N-terminus replacement.

Results

A hybrid xylanase with high thermostability, named AEXynM, was predicted by computational methods, and constructed by substituting the N-terminal 33 amino acids of AuXyn11A with the corresponding 38 ones of EvXyn11TS, a hyperthermostable family 11 xylanase. Two AuXyn11A- and AEXynM

SUBMITTER: Zhang H 

PROVIDER: S-EPMC3895927 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature