Evaluation of a novel bifunctional xylanase-cellulase constructed by gene fusion
Evaluation of a novel bifunctional xylanase-cellulase constructed by gene fusion
复制标题
DOI：
10.1016/j.enzmictec.2005.01.030
复制
发表时间：
2005-05-16
影响因子：
3.4
通讯作者：
Yun, HD
中科院分区：
文献类型：
--
作者：
An, JM;Kim, YK;Yun, HD
利用基因融合技术制备了一种人工双功能酶木聚糖酶-纤维素酶。构建了编码不同长度融合蛋白的三个嵌合基因。当cel 5 Z：：Omega融合在xynX的下游时，融合蛋白表现出木聚糖酶（XynX）和纤维素酶（Ce 15 Z：：Omega）两者的活性，但当xynX融合在cel 5 Z：：Omega的下游时不表现出。当融合一个较短的木聚糖酶肽时，双功能酶的活性降低。纯化了三种融合酶，并通过CMC-SDS-PAGE和XYN-SDS-PAGE估计酶的分子量分别为149、129和87 kDa。该融合酶在pH8.0和50 ℃下具有最佳的纤维素酶活性，在pH8.0和70 ℃下具有最佳的木聚糖酶活性。(c)2005年由Elsevier Inc.出版
An artificial bifunctional enzyme, xylanase-cellulase, has been prepared by gene fusion. Three chimeric genes were constructed that encoded fusion proteins of different lengths. The fusion proteins exhibited both xylanase (XynX) and cellulase (Ce15Z::Omega) activity when cel5Z::Omega was fused downstream of xynX, but not when xynX was fused downstream of cel5Z::Omega. Activities of bifunctional enzymes decreased when a shorter xylanase peptide was fused. Three fusion enzymes were purified, and the molecular weights of the enzymes were estimated by CMC-SDS-PAGE and XYN-SDS-PAGE to be 149, 129, and 87 kDa, respectively. The fusion enzymes displayed optimum cellulase activity at pH 8.0 and 50 degrees C and optimum xylanase activity at pH 8.0 and 70 degrees C. (c) 2005 Published by Elsevier Inc.