Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase.

ABSTRACT:

Background

A mesophilic xylanase PjxA from Penicillium janthinellum MA21601 has high specific activity under acidic condition and holds great potential for applications in the animal feed industry. To enhance the thermostability of xylanase PjxA, two mutation strategies in the N-terminal region were examined and then integrated into the xylanase to further improvement. The recombinant xylanase PTxA-DB (The meaning of DB is disulfide-bridge.) was constructed by replacement of five residues in the mutated region in TfxA (T10Y, N11H, N12D, Y15F, N30 L), combined with an additional disulfide bridge in the N-terminal region.

Results

The T_m value of mutant PTxA-DB was improved from 21.3 °C to 76.6 °C, and its half-life was found to be 53.6 min at 60 °C, 107-fold higher

SUBMITTER: Xiong K 

PROVIDER: S-EPMC6659274 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature