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当前位置: 首页 > 文章 > 黑曲霉N5-5单宁酶的纯化及酶学性质测定 食品科学 2017,38 (6) 142-146
Position: Home > Articles > Purification and Enzymatic Properties of Tannase from Aspergillus niger N5-5 FOOD SCIENCE 2017,38 (6) 142-146

黑曲霉N5-5单宁酶的纯化及酶学性质测定

作  者：
张帅;曹庸;梁晓莹;林婉如
单  位：
肇庆学院化学化工学院;华南农业大学食品学院
关键词：
单宁酶;黑曲霉;纯化;纯酶;性质测定
摘  要：
采用中空纤维膜超滤和葡聚糖凝胶层析相结合的方法对黑曲霉N5-5单宁酶进行纯化,然后对纯酶性质进行测定。结果显示,黑曲霉N5-5单宁酶用该方法纯化后,可纯化近20倍,酶活力可回收23.30%。对纯酶作十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析,可知黑曲霉N5-5单宁酶为分子质量64.2 k D的单肽链蛋白。纯酶的酶促反应最适温度为45℃,且在25~45℃范围内热稳定性良好;酶促反应最适p H值为5.0,且在p H 5.0~5.5范围内酸碱稳定性良好。另外,反应动力学测定结果表明,该酶对底物没食子酸丙酯的米氏常数K_m为0.916 mmol/L,最大反应速率vmax为0.877 mmol/(L·min)。
译  名：
Purification and Enzymatic Properties of Tannase from Aspergillus niger N5-5
作  者：
ZHANG Shuai;CAO Yong;LIANG Xiaoying;LIN Wanru;College of Chemistry and Chemical Engineering, Zhaoqing University;College of Food Science, South China Agricultural University;
关键词：
tannase;;Aspergillus niger;;purification;;purified enzyme;;characterization
摘  要：
The crude tannase from Aspergillus niger N5-5 was purified by hollow fiber membrane ultrafiltration and Sephadex G-150 gel chromatography. The properties of the purified tannase were then determined. The results showed that the tannase from Aspergillus niger N5-5 could be purified about 20 folds with a 23.30% recovery. The enzyme was a 64.2 k D protein with a single peptide chain by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The optimal temperature for the enzyme was 45 ℃, and it had good thermostability in the range of 25–45 ℃; the optimal p H value was 5.0, and the enzyme displayed good p H stability in the p H range of 5.0–5.5. In addition, the results of reaction kinetics showed that the K_m and vmax values towards the substrate propyl gallate were 0.916 mmol/L and 0.877 mmol/(L·min), respectively.

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