食品科学 ›› 2005, Vol. 26 ›› Issue (4): 104-107.

• 基础研究 • 上一篇    下一篇

乳酸菌谷氨酸脱羧酶的酶学性质研究

 刘清, 姚惠源, 张晖   

  1. 江南大学食品学院
  • 出版日期:2005-04-15 发布日期:2011-09-19

Studies on Some Properties of Glutamate Decarboxylase from Lactic Acid Bacterium

 LIU  Qing, YAO  Hui-Yuan, ZHANG  Hui   

  1. School of Food Science and Technology, Southern Yangtze University
  • Online:2005-04-15 Published:2011-09-19

摘要: 本文对一株乳酸菌所产谷氨酸脱羧酶的酶学性质进行了较系统的研究,其中包括酶的热稳定性、pH稳定性及温度、pH和一些化学物质对酶活的影响。结果表明:此酶的最适温度为52℃,最适pH为4.5,米氏常数Km=24mmol。PLP、VB6及Ca2+在一定程度上都能促进酶活,且在含量小于100μmol时,作用程度为PLP>VB6>Ca2+。乙酸浓度小于0.05mol/L也能提高酶活力。

关键词: 乳酸菌, 谷氨酸脱羧酶, &gamma, -氨基丁酸, 酶学性质

Abstract: This article has made a systematic research on the property of glutamate decarboxylase which was produced by a lactic acid bacterium. The heat stability, pH stability as well as the effect of pH, temperature and some chemical substances were studied. The reasult showed that the optimum temperature and pH were 52℃ and 4.5 respectively. The Km value of the enzyme was 24mmol. PLP, VB6 and Ca2+ showed positive effect on the activity of GAD in the following order: PLP>VB6>Ca2+ even when their concentration was under 100μmol. If the concentration of the acetate was under 0.05mmol, the enzyme activity was also enhanced.

Key words: lactic acid bacterium, glutamate decarboxylase(GAD), γ-amino butyric acid(GABA), enzyme activity