| 诺卡氏菌株胞外β-淀粉酶的分离和鉴定 |
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| 引用本文： | 王银定,杨秀琴,王建平,冀星.诺卡氏菌株胞外β-淀粉酶的分离和鉴定[J].河北大学学报(自然科学版),1997(2). |
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| 作者姓名： | 王银定 杨秀琴 王建平 冀星 |
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| 作者单位： | Wang Yinding(Department of Biology，Hebei University，Baoding 071002)Yang Xinqin; Wang Jianping(The Research Centre of Biotechnology，Hebei University，Baoding 071002)Ji Xing(Department of Chemistry，Hebei University，Baoding 071002) |
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| 摘 要： | 诺卡氏菌株（Nocaridasp．）82除去菌体的发酵液经硫酸镀沉淀、DEAE-纤维素离子交换层析、SephadexG－200凝胶过滤，得到高纯度的β-淀粉酶。用SDS－PAGE测定酶蛋白分子量为53000，不具亚基；酶反应最适pH和温度分别为7．0和60℃，有较高的热稳定性；Fe2十和Zn2+对酶活力有促进作用，而Hg2+对酶活力有抑制作用。
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| 关 键 词： | β-淀粉酶 诺卡氏菌 麦芽糖 高效毛细管电泳 |
The Separation and Characterization of Amylase Produced by Nocardia sp.82 |
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| Wang Yinding.The Separation and Characterization of Amylase Produced by Nocardia sp.82[J].Journal of Hebei University (Natural Science Edition),1997(2). |
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| Authors: | Wang Yinding |
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| Abstract: | A thermostableβ-amylase from the culture supernatant of Nocardia sp.82 was purified to PAGE homogenous by ammonium sulfate precipitation DEAE-cellulose column chromatography and sephadex G-200 filtration with 33.02 fold purification and 37.2% recovery. The molecular weight estimated with SDS-PAGE was 53000. The optimum conditions for activity were pH7.0, temperature 60℃, and it remained 40% activi ty at 100℃ (30min). Theβ-amylase was activated by Fe2+、 Zn2+ and it was inhibied by Hg2+. |
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| Keywords: | β-amylase Nocardia sp 82 Maltose Capillary electrophoresis |
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