详细信息
Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia coli ( EI收录)
文献类型:期刊文献
英文题名:Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia coli
作者:Cui, J.D.[2]; Jia, S.R.[1,2]; Sun, A.Y.[3]
机构:[1] Tianjin Key Laboratory of Industry Microbiology, Tianjin University of Science and Technology, 29 Thirteenth Street, Tai Da Development Area, Tianjin 300457, China; [2] Tianjin Key Laboratory of Industry Microbiology, Tianjin University of Science and Technology, Tianjin, China; [3] State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China
年份:2008
卷号:46
期号:6
起止页码:631
外文期刊名:Letters in Applied Microbiology
收录:EI(收录号:20231113726625)
语种:英文
外文关键词:Acetone - Ammonia - Enzyme activity - Escherichia coli - Organic solvents - Surface active agents
摘要:Aim: To improve phenylalanine ammonia lyase (E.C.4.3.1.5-PAL) activity in recombinant Escherichia coli. Some methods for enrichment of PAL activity in recombinant E. coli JM109 were described. In an effort to create a rich enzyme source these methods would lead to improvements in the production of L-phenylalanine. Methods and Results: The possibilities of enriching PAL activity in recombinant E. coli was investigated by using individual and combinations of amino acids, organic solvents and surfactants. PAL activity was induced by adding combination of L-phenylalanine and L-tyrosine, activities as high as 64.3 U g-1of cells were obtained and enzyme activity was enriched by over 3.5-fold in comparison with the control. Permeabilization with cetyl trimethyl ammonium bromide or the acetone significantly enriched cellular PAL activity, which improved over 8.2- and 9.0-fold compared with the control, as high as 148.5 and 164.5 U g-1of cells respectively. Conclusion: These efforts may provide some effective methods for enhancing L-phenylalanine ammonia lyase activity. Significance and Impact of the Study: These approaches for manipulating recombinant E. coli in an effort to create a rich enzyme source would serve as a biotechnologically important protocol for production of l-phenylalanine. ? 2008 The Authors.
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