Heterologous expression characteristics of trichoderma viride endoglucanase V in the Silkworm, Bombyx mori L.

文献类型： 外文期刊

第一作者： Miao, Yun-gen

作者： Miao, Yun-gen;Li, Xing-hua;Wang, Mei-xian;Zhang, Peng;Hu, Jia-biao;Sun, Chun-guang;Zhou, Fang;Niu, Yan-shan;Malik, Firdose Ahmad;Bhaskar, Roy;Yang, Hua-jun;Miao, Yun-gen;Liu, Xin-ju

作者机构：

关键词： Bombyx mori;Cellulase;Trichoderma viride

期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）

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收录情况： SCI

摘要： Efficient degradation of cellulose needs a synergistic reaction of the cellulolytic enzymes, which include exoglucanases, endoglucanases, and β-1,4-glucosidase. In this study, we used an improved Bac-to-Bac/BmNPV baculovirus expression system, which lacks the virus-encoded chitinase cathepsin (v-cath) genes of Bombyx mori nucleopolyhedrovirus (BmNPV), to express the endoglucanase V (EG V) gene from Trichoderma viride in silkworm BmN cells and silkworm larvae, and analyzed the characteristics of the recombinant enzyme in silkworm larvae. The result showed that an around 36-kDa protein was visualized in BmN cellsat 48 h after the second-generation recombinant mBacmid/BmNPV/EG V baculovirus infection.The crude enzyme extract from the recombinant baculoviruses-infected silkworms exhibited a significant maximum activity at the environmental condition of pH 5.0 and a temperatureof 50 °C, and increased 39.86% and 37.76% compared with that from blank mBacmid/BmNPVbaculovirus- infected silkworms and normal silkworms, respectively. It was stable at pH rangefrom 5.0 to 10.0 and at temperature range from 40 to 60 °C. The availability of large quantities of EG V that the silkworm provides might greatly facilitate the future research and the potential application in industries.

分类号： Q5

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