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Continuous production of 3‐fluoro‐ L ‐alanine with alanine dehydrogenase
Author(s) -
Ohshima Toshihisa,
Wandrey Christian,
Conrad Dietrich
Publication year - 1989
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.260340313
Subject(s) - formate dehydrogenase , alanine , chemistry , ammonium formate , formate , dehydrogenase , nad+ kinase , biochemistry , ammonia , cofactor , enzyme , nuclear chemistry , catalysis , amino acid , formic acid
Alanine dehydrogenase catalyzed the conversion of 3‐fluoropyruvate into 3‐fluoro‐ L ‐alanine in the presence of NADH and ammonia. The optimum pH of the reaction was 7.8. The K m values of the enzyme for 3‐fluoropyruvate, polyethylene glycol‐bound NADH, and ammonia were 2.94, 0.56, and 105m M , respectively. 3‐Fluoro‐ L ‐alanine was selectively and continuously produced from 3‐fluoropyruvate and ammonium formate in an enzyme membrane reactor by the multienzyme reaction system of alanine dehydrogenase and formate dehydrogenase with a simultaneous coenzyme regeneration. The average conversion and the space–time yield were 73% and 75 g/L day, respectively, with operation of the reactor for 4 days. Alanine dehydrogenase and formate dehydrogenase consumed were 11, 370 and 22, 950 units/kg 3‐fluoro‐ L ‐alanine, respectively. The cycle number was 3150 mol/mol NAD.