<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9</volume><submitter>Sadaqat B</submitter><pubmed_abstract>&lt;i>Thermotoga maritima&lt;/i> (&lt;i>Tma&lt;/i>) contains genes encoding various hyperthermophilic enzymes with great potential for industrial applications. The gene TM1752 in &lt;i>Tma&lt;/i> genome has been annotated as cellulase gene encoding protein Cel5B. In this work, the gene TM1752 was cloned and expressed in &lt;i>Escherichia coli&lt;/i>, and the recombinant enzyme was purified and characterized. Interestingly, the purified enzyme exhibited specific activities of 416 and 215 U/mg on substrates galactomannan and carboxy methyl cellulose, which is the highest among thermophilic mannanases. However, the putative enzyme did not show sequence homology with any of the previously reported mannanases; therefore, the enzyme Cel5B was identified as bifunctional mannanase and cellulase and renamed as Man/Cel5B. </pubmed_abstract><journal>Frontiers in bioengineering and biotechnology</journal><pagination>637649</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8007966</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment.</pubmed_title><pmcid>PMC8007966</pmcid><pubmed_authors>Zuo W</pubmed_authors><pubmed_authors>Shao W</pubmed_authors><pubmed_authors>Rupani PF</pubmed_authors><pubmed_authors>Sadaqat B</pubmed_authors><pubmed_authors>Wang H</pubmed_authors><pubmed_authors>Sha C</pubmed_authors></additional><is_claimable>false</is_claimable><name>Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment.</name><description>&lt;i>Thermotoga maritima&lt;/i> (&lt;i>Tma&lt;/i>) contains genes encoding various hyperthermophilic enzymes with great potential for industrial applications. The gene TM1752 in &lt;i>Tma&lt;/i> genome has been annotated as cellulase gene encoding protein Cel5B. In this work, the gene TM1752 was cloned and expressed in &lt;i>Escherichia coli&lt;/i>, and the recombinant enzyme was purified and characterized. Interestingly, the purified enzyme exhibited specific activities of 416 and 215 U/mg on substrates galactomannan and carboxy methyl cellulose, which is the highest among thermophilic mannanases. However, the putative enzyme did not show sequence homology with any of the previously reported mannanases; therefore, the enzyme Cel5B was identified as bifunctional mannanase and cellulase and renamed as Man/Cel5B. </description><dates><release>2021-01-01T00:00:00Z</release><publication>2021</publication><modification>2025-04-03T21:04:45.233Z</modification><creation>2022-02-09T13:37:43.495Z</creation></dates><accession>S-EPMC8007966</accession><cross_references><pubmed>33796509</pubmed><doi>10.3389/fbioe.2021.637649</doi></cross_references></HashMap>