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真菌融合子R201纤维素酶的纯化及性质研究

Purification and properties of the cellulase from fungi crasis R201

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【作者】 刘长江连芙菲刘玲

【Author】 LIU Chang-jiang, LIAN Fu-fei, LIU Ling (College of Food Science, Shenyang Agricultural University, Shenyang 110161)

【机构】 沈阳农业大学食品学院沈阳农业大学食品学院 沈阳110161沈阳110161

【摘要】 采用两株真菌康宁木霉3.2774和白腐真菌5.776融合产生的融合菌株R201对秸秆进行液态发酵,发酵粗酶液经硫酸铵盐析,SephadexG-100柱层析2次后酶活可提纯8.89倍。经SDS-PAGE测得3种纤维素酶的分子量约为66.3、52.7ku和37.0ku。酶作用的最适温度为50℃,最适pH值为5.0,在40℃以下,pH值4~6之间酶活较稳定。浓度为5mmol/L的Fe2+对酶反应有明显促进作用。

【Abstract】 Cellulase was separated and purified from a culture filtrate of crasis R201 that was fused between Trichoderma koningii 3.2774 and Phanerochaete chrysosporium 5.776 through ammonium sulfate precipitation and twice Sephadex G-100 column chromatography. It was purified to 8.89 folds. The molecular weights of the three purified cellulase were about 66.3, 52.7ku and 37.0ku respectively. The optimum temperature and pH value for cellulose activity were 50℃ and 5.0, respectively.It was more stable below the temperature 40℃ and in the pH rang of 4~6. The enzymic reaction can be strongly activated by 5mmol/L Fe2+.

【基金】 辽宁省科技厅科技攻关课题(2000050107);校青年基金资助项目
  • 【文献出处】 食品科技 ,Food Science and Technology , 编辑部邮箱 ,2007年12期
  • 【分类号】TQ925
  • 【被引频次】1
  • 【下载频次】115
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