{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Bessonnet T"],"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 <i>Escherichia coli</i>, the enzyme Nit <i><sub><i>phym</i></sub> </i> from the mesophilic organism <i>Paraburkholderia phymatum</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"],"journal":["Frontiers in bioengineering and biotechnology"],"pagination":["686362"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8280356"],"repository":["biostudies-literature"],"pubmed_title":["Purification and Characterization of Nit <i><sub><i>phym</i></sub> </i> , a Robust Thermostable Nitrilase From <i>Paraburkholderia phymatum</i>."],"pmcid":["PMC8280356"],"pubmed_authors":["Vergne-Vaxelaire C","Bessonnet T","Mariage A","Pellouin V","de Berardinis V","Petit JL","Zaparucha A","Debard A"],"additional_accession":[]},"is_claimable":false,"name":"Purification and Characterization of Nit <i><sub><i>phym</i></sub> </i> , a Robust Thermostable Nitrilase From <i>Paraburkholderia phymatum</i>.","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 <i>Escherichia coli</i>, the enzyme Nit <i><sub><i>phym</i></sub> </i> from the mesophilic organism <i>Paraburkholderia phymatum</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","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021","modification":"2026-05-08T07:57:18.28Z","creation":"2022-02-10T21:07:54.637Z"},"accession":"S-EPMC8280356","cross_references":{"pubmed":["34277586"],"doi":["10.3389/fbioe.2021.686362"]}}