Inducing Expression and Reaction Characteristic of Nitrile Hydratase from Rhodococcus sp. SHZ-1

作     者：王超 张根林 徐小琳 李春 

作者机构：Department of Environmental and Biochemical Engineering School of Chemistry and Chemical EngineeringShihezi University Shihezi 832003 China School of Life Science and Technology Beijing Institute of Technology Beijing 100081 China 

出 版 物：《Chinese Journal of Chemical Engineering》 (中国化学工程学报（英文版）)

年 卷 期：2007年第15卷第4期

页      面：573-578页

核心收录：

学科分类：081703[工学-生物化工] 08[工学] 0817[工学-化学工程与技术] 0836[工学-生物工程] 082203[工学-发酵工程] 0822[工学-轻工技术与工程] 

基　　金：Supported by the National Natural Science Foundation of China (No.20466002)  the Program for New Century Excellent Talents in University (NCET-04-089) and the Key Research Projects in the Uygur Autonomous Region of Xinjiang (No.200332109) 

主　　题：nitrile hydratase biocatalysis acrylamide characteristic Rhodococcus sp. SHZ- 1 

摘      要：Inducing expression and the reaction characteristic of nitrile hydratase （NHase） from Rhodococcus sp. SHZ-1 were investigated. The results showed that the expression of NHase was greatly enhanced with the cooperation of acrylonitrile and ammonium chloride as inducer in the medium and the specific activity of NHase was increased of 44%. Then the temperature, pH, concentration of acrylonitrile and acrylamide were evaluated, which affected the activity and reaction characteristic of NHase. It was found that the temperature and concentration of acrylarnide were the most important factors for the catalyzation of NHase. The optimal catalysis temperature of NHase from Rhodococcus sp. SHZ-1 was 30℃, and the activation energy of the hydration of NHase was 90.2kJ·mol^-1 in the temperature range from 5℃ to 30℃. Kmof NHase was 0.095mol·L^-1 using acrylonitrile（AN） as substrate, and NHase activity was inhibited seriously when acrylonitrile concentration was up to 40g·L^-1, the substrate inhibition constant Ki is 0.283mol·L^-1. Moreover, the NHase from Rhodococcus sp. SHZ-1 had very strong tolerance to acrylamide, in which the final concentration of acrylamide reached to 642g·L^-1 and the residual activity of NHase still maintained 8.6% of the initial enzyme activity.