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Protein engineering of Acidovorax facilis 72W nitrilase for bioprocess development
Author(s) -
Wu Shijun,
Fogiel Arthur J.,
Petrillo Kelly L.,
Hann Eugenia C.,
Mersinger Lawrence J.,
DiCosimo Robert,
O'Keefe Daniel P.,
BenBassat Arie,
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.21289
Subject(s) - nitrilase , bioprocess , bioprocess engineering , chemistry , escherichia coli , bioreactor , enzyme , biochemistry , monomer , metabolic engineering , combinatorial chemistry , organic chemistry , polymer , microbiology and biotechnology , chemical engineering , biology , gene , engineering
Abstract Hydroxycarboxylic acid monomers can be used to prepare industrially important polymers. Enzymatic production of such hydroxycarboxylic acids is often preferred to chemical production since the reactions are run at ambient temperature, do not require strongly acidic or basic reaction conditions, and produce the desired product with high selectivity at high conversion. However, native enzymes often do not perform desired reactions with the efficiency required for commercial applications. Protein engineering was used to significantly increase the specific activity of nitrilase from Acidovorax facilis 72W for the conversion of 3‐hydroxyvaleronitrile to 3‐hydroxyvaleric acid. Overexpression of engineered nitrilase enzymes in Escherichia coli , combined with immobilization of whole cells in alginate beads that can be recycled many times has facilitated the development of a commercially viable bioprocess for production of 3‐hydroxyvaleric acid. Biotechnol. Bioeng. 2007;97: 689–693. © 2006 Wiley Periodicals, Inc.