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