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Room‐Temperature Synthesis of l ‐Alanine Using the Alanine Dehydrogenase of the Hyperthermophilic Archaeon Archaeoglobus fulgidus
Author(s) -
Vadas Alexander J. H.,
Schröder Imke,
Monbouquette Harold G.
Publication year - 2002
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp025528h
Subject(s) - alanine , biochemistry , chemistry , formate dehydrogenase , reductive amination , formate , enzyme , lactate dehydrogenase , amino acid , catalysis
Alanine dehydrogenase from the hyperthermophilic archaeon Archaeoglobus fulgidus was used at room temperature for batch synthesis of l ‐alanine by the reductive amination of pyruvate. The reaction mixture included yeast formate dehydrogenase for regeneration of NADH with formate as electron donor. The synthesis of l ‐alanine at room temperature was accompanied by no detectable loss of alanine dehydrogenase activity over 139 h and ≥99% consumption of pyruvate. The total number of enzyme turnovers was 5.1 million. This work demonstrates the potential utility of novel hyperthermostable enzymes that can be both very active and highly stable at moderate temperature.