Biotechnology Letters

, Volume 27, Issue 17, pp 1325–1328

A Metal Ion as a Cofactor Attenuates Substrate Inhibition in the Enzymatic Production of a High Concentration of D-glutamate Using N-acyl-D-glutamate Amidohydrolase

Authors

  • Kazuaki Yoshimune
    • Department of Applied Chemistry, Faculty of EngineeringOita University
  • Ai Hirayama
    • Department of Applied Chemistry, Faculty of EngineeringOita University
    • Department of Applied Chemistry, Faculty of EngineeringOita University
Article

DOI: 10.1007/s10529-005-0480-3

Cite this article as:
Yoshimune, K., Hirayama, A. & Moriguchi, M. Biotechnol Lett (2005) 27: 1325. doi:10.1007/s10529-005-0480-3

Abstract

N-Acyl-D-glutamate amidohydrolase (D-AGase) was inhibited by 94 % when 1 mol/l N-acetyl-DL- glutamate was used as a substrate. The addition of 1 mM Co2+ stabilized D-AGase. Moreover, the substrate inhibition was weakened to 88% with the addition of 0.4 mM Co2+ to the reaction mixture. Although D-AGase is a zinc-metalloenzyme, the addition of Zn2+ from 0.01 to 10 mM did not increase the D-glutamic acid production in the saturated substrate. Under optimal conditions, 0.38 MD-glutamic acid was obtained from N-acyl-DL-glutamate with 100% of the theoretical yield after 48 h.

Key words

D-aminoacylaseD-aspartateD-glutamate productionN-acyl-D-aspartate amidohydrolaseN-acyl-D-glutamate amidohydrolase

Copyright information

© Springer 2005