Enzymatic hydrolysis of cyanohydrins with recombinant nitrile hydratase and amidase from Rhodococcus erythropolis.
Nitrile hydratase and amidase from Rhodococcus erythropolis CIMB11540 were both cloned and expressed in Escherichia coli. Crude cell free extracts were used for the hydrolysis of different aromatic cyanohydrins. Nitrile hydratase expression was increased up to 5-fold by redesign of the expression cassette. The recombinant enzymes were successfully used for the conversion of several cyanohydrins to the corresponding alpha-hydroxy amides and acids while retaining enantiopurity.
Reisinger
Ch
Ch
Institute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, Graz, 8010, Austria.
Osprian
I
I
Glieder
A
A
Schoemaker
H E
HE
Griengl
H
H
Schwab
H
H
D000581:Amidohydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006836:Hydro-Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D009570:Nitriles / Q000737:chemistry / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D012240:Rhodococcus / Q000145:classification / Q000201:enzymology* / Q000235:genetics
D009570:Nitriles; D011994:Recombinant Proteins; C430593:cyanohydrin; D000581:Amidohydrolases; C019665:amidase; D006836:Hydro-Lyases; C048831:nitrile hydratase