Purification and characterization of the enantioselective nitrile hydratase from Rhodococcus equi A4

Applied Microbiology and Biotechnology
I PrepechalováVladimír Kren

Abstract

The nitrile hydratase from Rhodococcus equi A4 consisted of two kinds of subunits which slightly differed in molecular weight (both approximately 25 kDa) and showed a significant similarity in the N-terminal amino acid sequences to those of the nitrile hydratase from Rhodococcus sp. N-774. The enzyme preferentially hydrated the S-isomers of racemic 2-(2-, 4-methoxyphenyl)propionitrile, 2-(4-chlorophenyl)propionitrile and 2-(6-methoxynaphthyl)propionitrile (naproxennitrile) with E-values of 5-15. The enzyme functioned in the presence of 5-98% (v/v) of different hydrocarbons, alcohols or diisopropyl ether. The addition of 5% (v/v) of n-hexane, n-heptane, isooctane, n-hexadecane, pristane and methanol increased the E-value for the enzymatic hydration of 2-(6-methoxynaphthyl)propionitrile.

Citations

Jul 2, 2011·Journal of Industrial Microbiology & Biotechnology·Zhi-Jian LinYin-Chu Shen
May 5, 2007·Biotechnology Letters·Vojtech VejvodaLudmila Martínková
Aug 29, 2014·Applied Biochemistry and Biotechnology·Sheng ChenJing Wu
Aug 6, 2010·Biotechnology Advances·Shreenath Prasad, Tek Chand Bhalla
May 12, 2018·Bioprocess and Biosystems Engineering·Rajendra SinghDuni Chand
Mar 8, 2011·Organic & Biomolecular Chemistry·S van PeltR A Sheldon
Sep 2, 2021·Journal of Agricultural and Food Chemistry·Shilei SunMiaomiao Sheng

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