来自青霉属 G5 的两种中性热稳定纤维素酶协同作用于滤纸的水解。
Two neutral thermostable cellulases from Phialophora sp. G5 act synergistically in the hydrolysis of filter paper.
机构信息
Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
出版信息
Bioresour Technol. 2012 Oct;121:404-10. doi: 10.1016/j.biortech.2012.07.027. Epub 2012 Jul 20.
Two novel cellulase genes, cbh6A and egGH45, were cloned from Phialophora sp. G5 and successfully expressed in Pichia pastoris. The putative polypeptide of CBH6A consists of a family 1 CBM and a catalytic domain of glycosyl hydrolase family 6 cellobiohydrolases, while deduced EgGH45 only contains a catalytic domain of family 45 endoglucanases. CBH6A and EgGH45 were optimally active at pH 7.0 and 65°C, and pH 6.0 and 60°C, respectively. Both enzymes exhibited high activities and stabilities over a wide pH range and had good thermostability at 70°C. CBH6A and EgGH45 had significant resistance to SDS (10mM), remaining 35% and 54% activities, respectively. These enzymes had synergic effect on the hydrolysis of filter paper, showing the highest efficiency in the ratio of CBH6A to EgGH45 at 80:20. The properties make this enzyme combination potential for application in textile and detergents industries.
从木霉属 G5 中克隆了两个新型纤维素酶基因 cbh6A 和 egGH45，并在毕赤酵母中成功表达。推测的 CBH6A 多肽包含一个家族 1 CBM 和一个糖苷水解酶家族 6 纤维二糖水解酶的催化结构域，而推导的 EgGH45 仅包含一个家族 45 内切葡聚糖酶的催化结构域。CBH6A 和 EgGH45 的最适活性分别为 pH7.0 和 65°C，以及 pH6.0 和 60°C。这两种酶在宽 pH 范围内均表现出高活性和稳定性，在 70°C 下具有良好的热稳定性。CBH6A 和 EgGH45 对 SDS（10mM）具有很强的抗性，分别保持 35%和 54%的活性。这两种酶对滤纸的水解具有协同作用，在 CBH6A 与 EgGH45 的比例为 80:20 时效率最高。这些特性使该酶组合具有在纺织和洗涤剂工业中应用的潜力。
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