Expression, Characterization and Its Deinking Potential of a Thermostable Xylanase From Planomicrobium glaciei CHR43.

ABSTRACT: Genome mining is more and more widely used in identifying new enzymes from database. In the present study, we reported a putative xylanase, Pg-Xyn (WP_053166147.1), which originated from a psychrotolerant strain Planomicrobium glaciei CHR 43, and was identified from Genbank by genome mining. Sequence analysis and homology modeling showed that Pg-Xyn belongs to glycosyl hydrolase family 10. On the basis of heterologous expression in E. coli and biochemical characterization, we found Pg-Xyn was most active at pH 9.0 and 80°C and exhibited good stability from pH 5.0 to 12.0 and below 90°C. Pg-Xyn was slightly activated in the presence of Ca²⁺ and Mg²⁺, while it was strongly inhibited by Mn²⁺. The analysis of hydrolysis products showed that Pg-Xyn

SUBMITTER: Liu Z 

PROVIDER: S-EPMC7928332 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature