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Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia coli  ( SCI-EXPANDED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.[1];Jia, S. R.[1];Sun, A. Y.[2]

机构:[1]Tianjin Univ Sci & Technol, Tianjin Key Lab Ind Microbiol, Tai Da Dev Area, Tianjin 300457, Peoples R China;[2]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R 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:;WOS:【SCI-EXPANDED(收录号:WOS:000255945200005)】;

语种:英文

外文关键词:amino acid; organic solvents; phenylalanine ammonia lyase; recombinant Escherichia coli; surfactants

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(-1)of 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(-1)of 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.

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