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Asymmetric hydrolysis of α-aminonitriles to optically active amino acids by a nitrilase ofRhodococcus rhodochrousPA-34

✍ Scribed by Tek Chand Bhalla; Akira Miura; Akiko Wakamoto; Yoichi Ohba; Keizo Furuhashi

Book ID: 104652570
Publisher: Springer
Year: 1992
Tongue: English
Weight: 750 KB
Volume: 37
Category: Article
ISSN: 1432-0614
DOI: 10.1007/bf00178168

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✦ Synopsis

Rhodococcus rhodochrous PA-34 isolated from soil as a propionitrile-utilizing microorganism, hydrolysed several a-aminonitriles to optically active amino acids. The hydrolysis of a-aminonitriles was found to be catalysed by a nitrilase. The characteristics of the purified enzyme revealed that this is a new nitrilase as it has a molecular mass of 45 k D a and acts as a monomer. The optimum p H and temperature for the activity of the purified enzyme were 7.5 and 35 ° C, respectively. Thiol-specific reagents caused inhibition whereas chelators did not significantly alter the activity of this enzyme. The amino acids produced were of Lform, except for alanine. In the case of leucine production from a-aminoisocapronitrile, the enantiomeric ratio of L-leucine to D-leucine was about 60.

R e f e r e n c e s

Arnaud A, Galzy P, Jallageas J (1980) Production d'acides a-amines stereospecifiques par hydrolyse biolofique d'a-aminonitriles racemiques.

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