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黑曲霉内切β-葡聚糖酶的纯化和性质

Purification and Characteristics of an Endo-beta-1,4 -D-glucanase from Aspergillus Niger

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【作者】 郭春腾傅蓉邓文汉林向阳饶平凡

【Author】 Guo Chunteng Fu Rong Deng Wenhan Lin Xiangyang Rao Pingfan Institute of Biotechnology, Fuzhou University Fuzhou 350002

【机构】 福州大学生物工程研究所福州大学生物工程研究所 福州 350002福州 350002

【摘要】 黑曲霉(Aspergillus niger)的粗酶滤液经过硫酸铵沉淀和四种色谱CM-Sephadex C-50离子交换色谱、DEAE-Sephadex A-50离子交换色谱、POROS 20 HQ离子交换色谱和TSK-G3000SW凝胶色谱,从中提纯了一个新的内切β-葡聚糖苷酶该酶经SDS-PAGE电泳检测分子量为36.0KD,该酶活力的最适温度为70℃,最适pH值为3.6 纯化后的该酶只能降解羧甲基纤维素,不能降解微晶纤维素,对蔗糖、麦芽糖和纤维素也不起作用。其N-末端部分氨基酸序列为V F E W F G C N E C G A E F Tx N I P G。

【Abstract】 A novel cellulase (endo-beta-1 ,4-D-glucanase, EC 3.2. 1.4)from commercial Aspergillus niger was purified to homogeneity by a combination of ammonium sulfate fractionation and four chromatographic procedures, CM chromatographv, DEAE chromatography,POROS 20 HQ chromatographv and TSK-G3000SW chromatograph) . The enzyme has an apparent molecular mass of 36.0 KD, as determined by SDS-polyacrylamide gel electrophoresis. The optimal pH of the enzyme is 3.6 and the optimal temperature at 70℃. The purified enzyme readily hydrolyzed carboxymethyl cellulose but displays no hydrolytic activity towards crystalline cellulose and had no action on sucrose, maltose, and cellulose; The N-terminal amino acid sequence of the cellulase is V F E W F G C N E C G A E F T X N I P G .

  • 【文献出处】 中国食品学报 ,Journal of Chinese Institute of Food Science and Technology , 编辑部邮箱 ,2002年01期
  • 【分类号】TS201
  • 【被引频次】6
  • 【下载频次】139
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