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Protein engineering of nitrilase for chemoenzymatic production of glycolic acid
Author(s) -
Wu Shijun,
Fogiel Arthur J.,
Petrillo Kelly L.,
Jackson Raymond E.,
Parker Kimberley N.,
DiCosimo Robert,
BenBassat Arie,
O'Keefe Daniel P.,
Payne Mark S.
Publication year - 2007
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.21643
Subject(s) - nitrilase , biocatalysis , glycolic acid , chemistry , biochemistry , enzyme , fermentation , ammonium , protein engineering , metabolic engineering , organic chemistry , catalysis , biology , bacteria , reaction mechanism , lactic acid , genetics
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.