| 基因工程菌1016氨基酰化酶的酶学性质研究 |
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| 引用本文： | 李环,李睿,陈国广,韦萍.基因工程菌1016氨基酰化酶的酶学性质研究[J].氨基酸和生物资源,2004,26(1):32-35. |
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| 作者姓名： | 李环 李睿 陈国广 韦萍 |
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| 作者单位： | 南京工业大学制药与生命科学学院,南京,210009 |
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| 摘 要： | 研究了基因工程菌 1 0 1 6所产的氨基酰化酶的酶学特性。该酶的拆分速率符合米氏方程 ,且在 0 .5mol/L的高底物浓度下 ,无底物抑制现象。 37℃时的米氏常数和最大反应速率分别为 0 .0 4 8mmol/L和 2 .1 78mmol/L·h。最适反应温度为 5 5℃。5 5℃时 ,Km为 0 .0 37mmol/L ,Vmax为 2 .5 5 8mmol/L·h。最适底物为乙酰蛋氨酸 ;热稳定性好。
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| 关 键 词： | 氨基酰化酶 动力学 拆分 蛋氨酸 |
| 文章编号： | 1006-8376(2004)01-0032-03 |
| 修稿时间： | 2003年9月8日 |
Characterization of L-aminoacylase in Bioengineered Bacterium 1016 |
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| LI Huan,LI Rui,CHENG Guo-guang,WEI Ping.Characterization of L-aminoacylase in Bioengineered Bacterium 1016[J].Amino Acids & Biotic Resources,2004,26(1):32-35. |
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| Authors: | LI Huan LI Rui CHENG Guo-guang WEI Ping |
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| Abstract: | The aminoacylase characteristics of bioengineered bacterium 1016 were investigated. The results showed that the reaction adhered to Michcelis-Menten equation and there was no substrate inhibition when substrate concentration was not higher than 0.5mol.L -. At 37℃, kinetic constants Km and Vm were 0.048mmol.L - and 2.178 mmol.L -h - respectively. At 55℃,Km was 0.037mmol.L - and Vm was 2.558mmol.L -h -. The optimal substrate and temperature for aminoacylase were N-AC-D,L-Met and 55℃ respectively. The aminoacylase activities could keep steady at higher temperatures. |
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| Keywords: | aminoacylase kinetics resolution L-methionine |
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