Purification and characterization of a novel cellobiohydrolase (PdCel6A) from Penicillium decumbens JU-A10 for bioethanol production
Purification and characterization of a novel cellobiohydrolase (PdCel6A) from Penicillium decumbens JU-A10 for bioethanol production
复制标题
用于生物乙醇生产的斜卧青霉 JU-A10 的新型纤维二糖水解酶 (PdCel6A) 的纯化和表征
DOI：
10.1016/j.biortech.2011.06.033
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发表时间：
2011-09-01
影响因子：
11.4
通讯作者：
Qu, Yinbo
中科院分区：
文献类型：
--
作者：
Gao, Le;Wang, Fenghui;Qu, Yinbo
从德肯青霉中分离纯化出一种酸性Cel6A，命名为PdCel6A。推导出的新型CBH的内部氨基酸序列与烟曲霉菌CBH II具有高度的同源性。令人惊讶的是，PdCel6A表现出与CBH I和CBH II相似的特性。与CBH I相似，新型CBH对对-硝基苯基-β-D-纤维二糖苷的比活性为1.9IU/mg。该酶在pH值为2.0的条件下孵育4h后仍保持最大活力的80%左右。以脱木素玉米芯残渣为底物，添加低剂量PdCel6A(0.2 mg/g底物)，可使同时糖化发酵过程中乙醇浓度提高20%。据我们所知，这是第一个涉及CBH I类CBH II的报告。本论文为CBH II在纤维素降解中的作用提供了新的见解。(C)2011爱思唯尔有限公司。保留所有权利。
An acidic Cel6A, cellobiohydrolase (CBH) II, was purified from Penicillium decumbens and designated as PdCel6A. The deduced internal amino acid sequence of the novel CBH has a high degree of sequence identity with the CBH II from Aspergillus fumigatus. Surprisingly, PdCel6A exhibits characteristics comparable to that of CBH I, as well as CBH II. Similar to CBH I, the novel CBH has a specific activity of 1.9 IU/mg against p-nitrophenyl-beta-D-cellobioside. The enzyme retains about 80% of its maximum activity after 4 h of incubation at pH 2.0. Using delignified corncob residue as the substrate, ethanol concentration increased by 20% during simultaneous saccharification and fermentation when supplemented with low doses of PdCel6A (0.2 mg/g substrate). To our knowledge, this is the first report involving a CBH I-like CBH II. The present paper provides new insight into the role of CBH II in cellulose degradation. (C) 2011 Elsevier Ltd. All rights reserved.