Over-expression in Escherichia coli of a thermally stable and regio-selective nitrile hydratase from Comamonas testosteroni 5-MGAM-4D.
作者： Kelly L. Petrillo , Shijun Wu , Eugenia C. Hann , Frederick B. Cooling , Arie Ben-Bassat
DOI: 10.1007/S00253-004-1842-9
关键词: Biochemistry 、 Escherichia coli 、 Open reading frame 、 Nitrile 、 Biology 、 Comamonas testosteroni 、 Enterobacteriaceae 、 Enzyme 、 Nitrile hydratase 、 Amidase
摘要: The genes encoding a thermally stable and regio-selective nitrile hydratase (NHase) an amidase from Comamonas testosteroni 5-MGAM-4D have been cloned sequenced, active NHase has over-produced in Escherichia coli. Maximal activity requires co-expression of small open reading frame immediately downstream the beta subunit gene. Compared to native organism, E. coli biocatalyst nearly threefold more on dry cell weight basis, this is significantly stable. In addition, converts wide spectrum substrates corresponding amides. Such versatility robustness are desirable attributes intended for use commercial applications.
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