Asymmetric hydrolysis of α-aminonitriles to optically active amino acids by a nitrilase of Rhodococcus rhodochrous PA-34 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-05

AUTHORS

Tek Chand Bhalla, Akira Miura, Akiko Wakamoto, Yoichi Ohba, Keizo Furuhashi

ABSTRACT

Rhodococcus rhodochrous PA-34 isolated from soil as a propionitrile-utilizing microorganism, hydrolysed several α-aminonitriles to optically active amino acids. The hydrolysis of α-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 kDa and acts as a monomer. The optimum pH 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 L-form, except for alanine. In the case of leucine production from α-aminoisocapronitrile, the enantiomeric ratio of L-leucine to D-leucine was about 60. More... »

PAGES

184-190

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00178168

DOI

http://dx.doi.org/10.1007/bf00178168

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049966309


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