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Inducing Expression and Reaction Characteristic of nitrile hydratase from Rhodococcus sp. SHZ-1

Chinese Journal of Chemical Engineering 2007年第4期15卷 573-578页

作者：王超张根林徐小琳李春 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

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.

关键词： nitrile hydratase biocatalysis acrylamide characteristic Rhodococcus sp. SHZ- 1

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Deactivation Kinetics of nitrile hydratase in Free Resting Cells

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Chinese Journal of Chemical Engineering 2009年第5期17卷 822-828页

作者：孙旭东于慧敏沈忠耀 Department of Chemical Engineering Tsinghua University Beijing 100084 China

nitrile hydratase (NHase) is an important industrial enzyme used for acrylamide production from *** deactivation kinetics of NHases in free resting cells of Rhodococcus *** presented based on a bi-steady state *** of hydration temperature,product concentration and substrate concentration on NHase deactivation were investigated experimentally and correlated with a first order deactivation *** results showed that the hydration temperature and product concentration were major factors governing the deactivation of NHases under substrate-feeding *** acrylamide concentration was higher than 250 g·L1,the deactivation of NHases became serious and the bi-steady state assumption was not *** the hydration temperature was controlled at a relatively higher level such as 28°C,the total deactivation rate constant was about 2.8-fold of that at 20°C.

关键词： nitrile hydratase deactivation kinetics free resting cell bi-steady state assumption total deactivation rate constant

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Biocatalytic Synthesis of Highly Enantiopure 1,4-Benzodioxane-2-carboxylic Acid and Amide

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Chinese Journal of Chemistry 2006年第11期24卷 1665-1668页

作者：刘军王德先郑企雨王梅祥 Beijing National Laboratory for Molecular Sciences Laboratory for Chemical Biology Institute of Chemistry Chinese Academy of Sciences Beijing 100080 China

Catalyzed by Rhodococcus erythropolis AJ270, a nitrile hydratase and amidase containing microbial whole-cell catalyst, at 10 ℃ and with the use of methanol as a co-solvent, nitrile and amide biotransformations produce 2S-1,4-benzodioxane-2-carboxamide and 2R-1,4-benzodioxane-2-carboxylic acid in high yields with excellent enantioselectivity.

关键词： 1,4-benzodioxane-2-carboxylic acid 1,4-benzodioxane-2-carboxamide biotransformation nitrile hydratase amidase enantioselectivity

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Synthesis of Optically Active β-Alkyl-α-methylene-γ-butyro- lactones from Enantioselective Biotransformation of nitriles, an Unusual Inversion of Enantioselectivity

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Chinese Journal of Chemistry 2002年第11期20卷 1291-1299,1129页

作者：赵生敏王梅祥 Center for Molecular Science Institute of Chemistry Chinese Academy of Sciences Beijing 100080 China Email: Mei-Xiang Wang (rmwang@***)

A new approach to optically active β-alkyl-α-methylene-γ-butyrolactone derivatives was reported from the Rhodococcus sp. AJ270-catalyzed hydrolysis of appropriate nitriles. The inversion of enantioselectivity of th... 详细信息

关键词： biotransformation nitrile hydratase amidase optically active β-alkyl-α-methylene-γ-butyrolactone inversion of enantioselectivity

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