A novel nitrilase from Ralstonia eutropha H16 and its application to nicotinic acid production
文献类型： 外文期刊
作者： Fan, Haiyang 1 ; Chen, Lifeng 1 ; Sun, Huihui 2 ; Wang, Hualei 1 ; Ren, Yuhong 1 ; Wei, Dongzhi 1 ;
作者机构： 1.East China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Shandong, Peoples R China
关键词： Nitrilase;Ralstonia eutropha;Nicotinic acid;Biotransformation
期刊名称：BIOPROCESS AND BIOSYSTEMS ENGINEERING （ 影响因子：3.21； 五年影响因子：2.97 ）
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收录情况： SCI
摘要： A novel aliphatic nitrilase, REH16, was found in Ralstonia eutropha H16 and overexpressed in Escherichia coli BL21(DE3), and its enzymatic properties were studied. The temperature and pH optima were 37 A degrees C and 6.6, respectively, and the best thermostability of the nitrilase was observed at 25 A degrees C, which preserved 95% of activity after 120 h of incubation. REH16 has a broad hydrolytic activity toward aliphatic and heterocyclic nitriles and showed high tolerance of 3-cyanopyridine; this enzyme could hydrolyze as high as 100 mM 3-cyanopyridine completely. To improve the 3-cyanopyridine conversion efficiency in an aqueous reaction system, water-miscible organic solvents were tested, and ethanol (10% v/v) was chosen as the optimal co-solvent. Finally, under optimized conditions, using the fed-batch reaction mode, total of 1050 mM 3-cyanopyridine was hydrolyzed completely in 20.8 h with eight substrate feedings, yielding 129.2 g/L production of nicotinic acid and thus showing a potential for industrial application.
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