{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dai AD"],"funding":["Natural Science Foundation of Zhejiang Province","National Key R&amp;D Program of China"],"pagination":["50"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8795250"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(2)"],"pubmed_abstract":["2-chloronicotinic acid (2-CA) is a key precursor for the synthesis of a series of pesticides and pharmaceuticals. Nitrilase-catalyzed bioprocess is a promising method for 2-CA production from 2-chloronicotinonitrile (2-CN). In this study, a mutant of nitrilase from <i>Rhodococcus zopfii</i> (<i>Rz</i>NIT/W167G) was constitutively overexpressed with <i>Escherichia coli</i> as host, which exhibited a onefold increase in enzymatic activity compared with inducible expression. Biosynthesis of 2-CA using whole cells harboring nitrilase as biocatalysts were investigated and 318.5 mM 2-CA was produced, which was the highest level for 2-CA production catalyzed by nitrilase to date. 2-CA was recovered from the reaction mixture through a simple acidification step with a recovery yield of 90%. This st"],"journal":["3 Biotech"],"pubmed_title":["Constitutive expression of nitrilase from <i>Rhodococcus zopfii</i> for efficient biosynthesis of 2-chloronicotinic acid."],"pmcid":["PMC8795250"],"funding_grant_id":["LR19B060001","2017YFE0129400"],"pubmed_authors":["Zheng YG","Dai AD","Zheng RC","Wu ZM"],"additional_accession":[]},"is_claimable":false,"name":"Constitutive expression of nitrilase from <i>Rhodococcus zopfii</i> for efficient biosynthesis of 2-chloronicotinic acid.","description":"2-chloronicotinic acid (2-CA) is a key precursor for the synthesis of a series of pesticides and pharmaceuticals. Nitrilase-catalyzed bioprocess is a promising method for 2-CA production from 2-chloronicotinonitrile (2-CN). In this study, a mutant of nitrilase from <i>Rhodococcus zopfii</i> (<i>Rz</i>NIT/W167G) was constitutively overexpressed with <i>Escherichia coli</i> as host, which exhibited a onefold increase in enzymatic activity compared with inducible expression. Biosynthesis of 2-CA using whole cells harboring nitrilase as biocatalysts were investigated and 318.5 mM 2-CA was produced, which was the highest level for 2-CA production catalyzed by nitrilase to date. 2-CA was recovered from the reaction mixture through a simple acidification step with a recovery yield of 90%. This st","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2025-04-19T17:58:49.858Z","creation":"2025-04-19T17:58:49.858Z"},"accession":"S-EPMC8795250","cross_references":{"pubmed":["35127305"],"doi":["10.1007/s13205-022-03119-0"]}}