| 特基拉芽孢杆菌精氨酸酶基因的重组表达及酶学性质 |
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| 引用本文： | 赵齐,冯志彬,秦雪,徐勤省,任梦云,潘潇,张洪霞,张娟.特基拉芽孢杆菌精氨酸酶基因的重组表达及酶学性质[J].食品科学,2018,39(8):77-82. |
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| 作者姓名： | 赵齐 冯志彬 秦雪 徐勤省 任梦云 潘潇 张洪霞 张娟 |
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| 作者单位： | （1.鲁东大学农学院，山东?烟台 264025；2.鲁东大学生命科学学院，山东?烟台 264025） |
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| 基金项目： | 农业部转基因生物新品种培育重大专项（2016ZX08004002）；烟台市科技计划项目（2015ZH071） |
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| 摘 要： | 精氨酸酶是一种能够催化精氨酸生成尿素和L-鸟氨酸的碱性水解酶。利用分子克隆的方法得到特基拉芽孢杆菌（Bacillus tequilensis）PanD37的精氨酸酶基因，在大肠杆菌中异源表达该基因后分析重组酶的性质。结果表明：该精氨酸酶编码297?个氨基酸序列；酶的最适反应温度为45?℃，最适反应pH值为10.0，在pH?8.0～10.0及50～60?℃范围内酶活力稳定，Mn2＋、Ni2＋、Co2＋对酶活力有明显的激活作用，粗酶的活力可达1?109.8?U/mL。
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| 关 键 词： | 精氨酸酶 特基拉芽孢杆菌 L-鸟氨酸 酶学特性 |
Expression in Escherichia coli and Characterization of Arginase from Bacillus tequilensis |
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| ZHAO Qi,FENG Zhibin,QIN Xue,XU Qinxing,REN Mengyun,PAN Xiao,ZHANG Hongxia,ZHANG Juan.Expression in Escherichia coli and Characterization of Arginase from Bacillus tequilensis[J].Food Science,2018,39(8):77-82. |
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| Authors: | ZHAO Qi FENG Zhibin QIN Xue XU Qinxing REN Mengyun PAN Xiao ZHANG Hongxia ZHANG Juan |
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| Affiliation: | (1. School of Agriculture, Ludong University, Yantai 264025, China; 2. School of Life Sciences, Ludong University, Yantai 264025, China) |
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| Abstract: | Arginase is an alkaline hydrolases that catalyzes the production of urea and L-ornithine from arginine. An arginase gene encoding 297 amino acids was cloned from Bacillus tequilensis PanD37. By recombinant DNA technique, a genetically engineered strain of Escherichia coli was constructed for heterologous expression of the gene. Enzymatic assays indicated that the recombinant enzyme exhibited maximum activity at pH 10.0 and 45 ℃. Its activity was stable in the temperature range of 50–60 ℃ and in the pH range of 8.0–10.0. The enzymatic activity could be significantly activated by Mn2+, Ni2+, and Co2+. The activity of crude enzyme was 1 109.8 U/mL. |
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| Keywords: | L-arginase Bacillus tequilensis L-ornithine enzymatic properties |
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