| 米曲氨基酰化酶的提取及其酶学性质的表征 |
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| 引用本文： | 钟琦,关怡新,姚善泾.米曲氨基酰化酶的提取及其酶学性质的表征[J].食品与发酵工业,2004,30(3):36-41. |
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| 作者姓名： | 钟琦 关怡新 姚善泾 |
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| 作者单位： | 浙江大学化学工程与生物工程学系,杭州,310027 |
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| 基金项目： | 国家自然科学基金资助项目 (No .2 0 2 76 0 6 5 ) |
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| 摘 要： | 通过硫酸铵分级沉淀、SephadexG5 0凝胶层析和DEAE Sepharose阴离子交换层析 ,从米曲霉 3 0 42中提取得到了米曲氨基酰化酶 ,该酶的纯化倍数为 5 4.2 9,比活为 647.66U/mg ,总收率为49 5 3 %。详细考察了温度、pH、缓冲体系的离子强度和金属离子对米曲氨基酰化酶酶活的影响。结果表明 ,该酶促反应的最适pH为 7 5～ 8 0 ,最适反应温度随催化反应时间的延长而降低 ,缓冲体系中的离子对酶活有抑制作用 ,而低浓度的Co2 +对酶活有激活作用。
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| 关 键 词： | 米曲氨基酰化酶 纯化 酶学性质 |
| 修稿时间： | 2003年9月25日 |
Purification and Characterization of Aminoacylase from Aspergillus oryzae 3042 |
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| Zhong Qi,Guan Yixin,Yao Shanjing.Purification and Characterization of Aminoacylase from Aspergillus oryzae 3042[J].Food and Fermentation Industries,2004,30(3):36-41. |
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| Authors: | Zhong Qi Guan Yixin Yao Shanjing |
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| Abstract: | The aminoacylase from Aspergillus oryzae 3042 was partially purified by ammonium sulfate fractionation, Sephadex G50 and DEAE-Sepharose cloumn chromatography. The specific activity of aminoacylase was 647.66*#U/mg. The purification ratio and recovery was 54.29 and 49.53% respectively. The optimal pH of the aminoacylase was 7.5～8.0, and with the increase of catalysis time, the optimal reaction temperature decreased correspondingly. The ions in the buffer lowered the activity of aminoacylase, but the Co 2+ in low concentration activated the aminoacylase. |
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| Keywords: | aminoacylase isolation characterization |
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