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

Zhaoxing Liu, Tingting Shao, Yan Li, Bin Wu, Honghua Jia, Ning Hao

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

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 was an endo-β-1,4-xylanase. In addition, Pg-Xyn performed good deinking ability in a paper deinking test. In consideration of its unique properties, Pg-Xyn might be a promising candidate for application in the paper and pulp industries.

Original languageEnglish
Article number618979
JournalFrontiers in Bioengineering and Biotechnology
Volume9
DOIs
StatePublished - 17 Feb 2021

Keywords

  • endo-xylanase
  • enzymatic deinking
  • psychrotolerant bacterium
  • thermo-alkali-stable
  • thermostable

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