z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom