Food and Fermentation Industries

Study on chiral resolution of DL-valine valine catalyzed by valine-pyruvate transaminase

  • Zhang Fei ,
  • Wei Tao ,
  • Liu Yin ,
  • Han Ya-wei ,
  • He Pei-xin
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Online published: 2013-02-25

Abstract

An engineered strain with catalytic activity of valine-pyruvate transaminase was used in chiral resolution of DL-valine.The effect of reaction conditions such as reaction temperature,pH,substrate mole ratio,substrate concentration and metal ions on enzyme activity was studied.Results showed that the optimal conditions were 45℃ and pH9.The optimal substrate ratio of L-valine to pyruvic acid was 1∶ 8(mol∶ mol).The initial substrate concentration of DL-valine and pyruvic acid were 0.6 mol/L and 2.4 mol/L respectively.Enzyme activity was improved by addition of 0.5 mmol/L Mg2+ and Na+.

Cite this article

Zhang Fei , Wei Tao , Liu Yin , Han Ya-wei , He Pei-xin . Study on chiral resolution of DL-valine valine catalyzed by valine-pyruvate transaminase[J]. Food and Fermentation Industries, 2013 , 39(02) : 41 -44 . DOI: 10.13995/j.cnki.11-1802/ts.2013.02.015

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