{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Liu Z"],"funding":["Jiangsu Agricultural Science and Technology Independent Innovation Fund","National Natural Science Foundation of China"],"pubmed_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 <i>Planomicrobium glaciei</i> 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 <i>E. coli</i> 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 Ca<sup>2+</sup> and Mg<sup>2+</sup>, while it was strongly inhibited by Mn<sup>2+</sup>. The analysis of hydrolysis products showed that Pg-Xyn"],"journal":["Frontiers in bioengineering and biotechnology"],"pagination":["618979"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7928332"],"repository":["biostudies-literature"],"pubmed_title":["Expression, Characterization and Its Deinking Potential of a Thermostable Xylanase From <i>Planomicrobium glaciei</i> CHR43."],"pmcid":["PMC7928332"],"pubmed_authors":["Hao N","Liu Z","Li Y","Wu B","Jia H","Shao T"],"additional_accession":[]},"is_claimable":false,"name":"Expression, Characterization and Its Deinking Potential of a Thermostable Xylanase From <i>Planomicrobium glaciei</i> CHR43.","description":"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 <i>Planomicrobium glaciei</i> 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 <i>E. coli</i> 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 Ca<sup>2+</sup> and Mg<sup>2+</sup>, while it was strongly inhibited by Mn<sup>2+</sup>. The analysis of hydrolysis products showed that Pg-Xyn","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021","modification":"2026-05-09T08:57:48.864Z","creation":"2021-03-12T08:16:20Z"},"accession":"S-EPMC7928332","cross_references":{"pubmed":["33681158"],"doi":["10.3389/fbioe.2021.618979"]}}