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Protein engineering of nitrilase for chemoenzymatic production of glycolic acid

✍ Scribed by Shijun Wu; Arthur J. Fogiel; Kelly L. Petrillo; Raymond E. Jackson; Kimberley N. Parker; Robert DiCosimo; Arie Ben-Bassat; Daniel P. O'Keefe; Mark S. Payne

Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
127 KB
Volume
99
Category
Article
ISSN
0006-3592

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✦ Synopsis

Abstract

A key step in a chemoenzymatic process for the production of high‐purity glycolic acid (GLA) is the enzymatic conversion of glycolonitrile (GLN) to ammonium glycolate using a nitrilase derived from Acidovorax facilis 72W. Protein engineering and over‐expression of this nitrilase, combined with optimized fermentation of an E. coli transformant were used to increase the enzyme‐specific activity up to 15‐fold and the biocatalyst‐specific activity up to 125‐fold. These improvements enabled achievement of the desired volumetric productivity and biocatalyst productivity for the conversion of GLN to ammonium glycolate. Biotechnol. Bioeng. 2008;99: 717–720. © 2007 Wiley Periodicals, Inc.

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