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Biotransformation of 3-cyanopyridine to nicotinic acid by free and immobilized cells of recombinant Escherichia coli
Affiliation:1. Department of Pharmaceutical Technology (Biotechnology), National Institute of Pharmaceutical Education and Research, Sector-67, S.A.S. Nagar 160 062, Punjab, India;2. School of Engineering, Massey University, Private Bag 11 222, Palmerston North, New Zealand;1. Istituto di Ricerche sulla Combustione, Consiglio Nazionale delle Ricerche (IRC)-CNR, p.le V. Tecchio, 80, 80125 Napoli, Italy;2. Dipartimento di Ingegneria Chimica, dei Materiali e della Produzione Industriale, Università di Napoli “Federico II”, p.le V. Tecchio, 80, 80125 Napoli, Italy;3. CSGI, Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase, Italy;4. Dipartimento di Fisica, Università di Napoli “Federico II”, and SPIN-CNR UOS, via Cintia, 80126 Napoli, Italy;1. State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, PR China;2. Enzyme and Fermentation Technology Laboratory, College of Light Industry Science and Engineering, Nanjing Forestry University, Nanjing 210037, PR China;1. Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, China;2. National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, China;1. Institute of Bioengineering, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China;2. Engineering Research Center of Bioconversion and Biopurification of Ministry of Education, Zhejiang University of Technology, Hangzhou 310014, China
Abstract:An efficient biocatalytic process for the production of nicotinic acid (niacin) from 3-cyanopyridine was developed using cells of recombinant Escherichia coli JM109 harboring the nitrilase gene from Alcaligenes faecalis MTCC 126. The freely suspended cells of the biocatalyst were found to withstand higher concentrations of the substrate and the product without any signs of substrate inhibition. Immobilization of the cells further enhanced their substrate tolerance, stability and reusability in repetitive cycles of nicotinic acid production. Under optimized conditions (37 °C, 100 mM Tris buffer, pH 7.5) for the immobilized cells, the recombinant biocatalyst achieved a 100% conversion of 1 M 3-cyanopyridine to nicotinic acid within 5 h at a cell mass concentration (fresh weight) of 500 mg/mL. The high substrate/product tolerance and stability of the immobilized whole cell biocatalyst confers its potential industrial use.
Keywords:Biotransformation  3-Cyanopyridine  Nicotinic acid
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