Over-expression in Escherichia coli of a thermally stable and regio-selective nitrile hydratase from Comamonas testosteroni 5-MGAM-4D |
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Authors: | Kelly L Petrillo Shijun Wu Eugenia C Hann Frederick B Cooling Arie Ben-Bassat John E Gavagan Robert DiCosimo Mark S Payne |
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Institution: | (1) Central Research and Development Department, E.I. du Pont de Nemours and Co., Experimental Station, P.O. Box 80328, Wilmington, Delaware 19880–0328, USA |
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Abstract: | The genes encoding a thermally stable and regio-selective nitrile hydratase (NHase) and an amidase from Comamonas testosteroni 5-MGAM-4D have been cloned and sequenced, and active NHase has been over-produced in Escherichia coli. Maximal activity requires co-expression of a small open reading frame immediately downstream from the NHase beta subunit gene. Compared to the native organism, the E. coli biocatalyst has nearly threefold more NHase activity on a dry cell weight basis, and this activity is significantly more thermally stable. In addition, this biocatalyst converts a wide spectrum of nitrile substrates to the corresponding amides. Such versatility and robustness are desirable attributes of a biocatalyst intended for use in commercial applications. |
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