<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9</volume><submitter>Bessonnet T</submitter><pubmed_abstract>Despite the success of some nitrilases in industrial applications, there is a constant demand to broaden the catalog of these hydrolases, especially robust ones with high operational stability. By using the criteria of thermoresistance to screen a collection of candidate enzymes heterologously expressed in &lt;i>Escherichia coli&lt;/i>, the enzyme Nit &lt;i>&lt;sub>&lt;i>phym&lt;/i>&lt;/sub> &lt;/i> from the mesophilic organism &lt;i>Paraburkholderia phymatum&lt;/i> was selected and further characterized. Its quick and efficient purification by heat treatment is of major interest for large-scale applications. The purified nitrilase displayed a high thermostability with 90% of remaining activity after 2 days at 30°C and a half-life of 18 h at 60°C, together with a broad pH range of 5.5-8.5. Its high resistance to variou</pubmed_abstract><journal>Frontiers in bioengineering and biotechnology</journal><pagination>686362</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8280356</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Purification and Characterization of Nit &lt;i>&lt;sub>&lt;i>phym&lt;/i>&lt;/sub> &lt;/i> , a Robust Thermostable Nitrilase From &lt;i>Paraburkholderia phymatum&lt;/i>.</pubmed_title><pmcid>PMC8280356</pmcid><pubmed_authors>Vergne-Vaxelaire C</pubmed_authors><pubmed_authors>Bessonnet T</pubmed_authors><pubmed_authors>Mariage A</pubmed_authors><pubmed_authors>Pellouin V</pubmed_authors><pubmed_authors>de Berardinis V</pubmed_authors><pubmed_authors>Petit JL</pubmed_authors><pubmed_authors>Zaparucha A</pubmed_authors><pubmed_authors>Debard A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Purification and Characterization of Nit &lt;i>&lt;sub>&lt;i>phym&lt;/i>&lt;/sub> &lt;/i> , a Robust Thermostable Nitrilase From &lt;i>Paraburkholderia phymatum&lt;/i>.</name><description>Despite the success of some nitrilases in industrial applications, there is a constant demand to broaden the catalog of these hydrolases, especially robust ones with high operational stability. By using the criteria of thermoresistance to screen a collection of candidate enzymes heterologously expressed in &lt;i>Escherichia coli&lt;/i>, the enzyme Nit &lt;i>&lt;sub>&lt;i>phym&lt;/i>&lt;/sub> &lt;/i> from the mesophilic organism &lt;i>Paraburkholderia phymatum&lt;/i> was selected and further characterized. Its quick and efficient purification by heat treatment is of major interest for large-scale applications. The purified nitrilase displayed a high thermostability with 90% of remaining activity after 2 days at 30°C and a half-life of 18 h at 60°C, together with a broad pH range of 5.5-8.5. Its high resistance to variou</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021</publication><modification>2026-05-08T07:57:18.28Z</modification><creation>2022-02-10T21:07:54.637Z</creation></dates><accession>S-EPMC8280356</accession><cross_references><pubmed>34277586</pubmed><doi>10.3389/fbioe.2021.686362</doi></cross_references></HashMap>