Expression, Characterization and Its Deinking Potential of a Thermostable Xylanase From Planomicrobium glaciei CHR43
| Autor: | Ning Hao, Honghua Jia, Yan Li, Zhaoxing Liu, Tingting Shao, Bin Wu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
0301 basic medicine Histology Sequence analysis lcsh:Biotechnology Biomedical Engineering Bioengineering 01 natural sciences law.invention 03 medical and health sciences chemistry.chemical_compound law 010608 biotechnology lcsh:TP248.13-248.65 Hydrolase enzymatic deinking Glycosyl Homology modeling Original Research psychrotolerant bacterium Chemistry endo-xylanase Bioengineering and Biotechnology thermostable Deinking thermo-alkali-stable 030104 developmental biology Biochemistry GenBank Xylanase Heterologous expression Biotechnology |
| Zdroj: | Frontiers in Bioengineering and Biotechnology, Vol 9 (2021) Frontiers in Bioengineering and Biotechnology |
| ISSN: | 2296-4185 |
| DOI: | 10.3389/fbioe.2021.618979 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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