HOU Yuan-ce,LI Xiu-liang,HE Qiang.Studies on Related Properties of Glutamate Decarboxylase from Pediococcus Acidilactici[J].HEILONGJIANG AGRICULTURAL SCIENCES,2011,(10):10-13.
乳酸片球菌产谷氨酸脱羧酶的相关酶学性质研究
- Title:
- Studies on Related Properties of Glutamate Decarboxylase from Pediococcus Acidilactici
- 文章编号:
- 1002-2767（2011）10-0010-04
- Keywords:
- glutamicacid decarboxylase(GAD); γ-aminobutyric acid; Lactococcus lactis; enzyme character
- 分类号:
- TQ922+.1
- 文献标志码:
- A
- 摘要:
- 为研究乳酸片球菌谷氨酸脱羧酶（GAD）的性质，采用比色法测其酶活。结果表明：当底物L-MSG的浓度为100 mmol·L-1时，GAD的活力达到最大。GAD的浓度为3.16%，最适温度为37℃，最适pH为5.0，PLP浓度为0.1 mol·L-1时，GAD酶活力最大。Mg2+和Mn2+使GAD活力提高10%左右，KCl和EDTA对GAD的活力稍有抑制，KI、Ag2+、SDS和CH3COOH均对乳酸片球菌GAD的活力具有较大抑制。乳酸片球菌GAD的米氏常数Km=0.365 8 mmol·L-1，最大反应速度Vmax=3.03 μmol·L-1。
- Abstract:
- This article researched on the property of glutamate decarboxylase,colorimetric method was used to measure the activity of GAD.The result showed that when the concentration of L-MSG was 100 mmol·L-1,GAD had the highest activity,the concentration of GAD was 3.16%，the optimal temperature was about 37℃,the optimal pH was 5,when the addition amount of PLP was 0.1mol·L-1,GAD had the highest activity.Mg2+and Mn2+ increased the enzyme activity by 10%,KCl,EDTA had decreased the enzyme activity,and KI,Ag2+,SDS and CH3COOH could decrease more seriously.The michaelis constant of GAD was Km=0.365 8 mmol·L-1,Vmax was 3.03 μmol·L-1.
参考文献/References:
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