Chen Mei, Qin Yuqi, Liu Ziyong, Liu Kai, Wang Fengshan, Qu Yinbo
State Key Laboratory of Microbial Technology, Shandong University, 27 Shanda South Road, Jinan, Shandong 250100, PR China.
National Glycoengineering Research Center, Shandong University, 27 Shanda South Road, Jinan, Shandong 250100, PR China; School of Pharmaceutical Sciences, Shandong University, 27 Shanda South Road, Jinan, Shandong 250100, PR China.
Enzyme Microb Technol. 2010 May 5;46(6):444-9. doi: 10.1016/j.enzmictec.2010.01.008. Epub 2010 Feb 4.
A β-glucosidase from Penicillium decumbens was purified and characterized. The enzyme presented as a single band of 120kDa on SDS-PAGE, showed optimal temperature of 65-70°C and optimal pH of 4.5-5.0. The β-glucosidase showed relatively higher affinity to pNPG and the highest affinity to salicin with the Km value as 0.0064 and 0.0188mM, respectively. The gene coding for it was obtained with an ORF of 2586bp coding for 861 amino acids belonging to glycoside hydrolases family 3. The purified enzyme could improve the saccharifying ability of cellulose when it was added to the cellulase systems of Trichoderma reesei QM 9414. The several properties of it, including its pH and temperature optima, the high affinity to substrates and high specific activity, make it has great potential to be utilized as supplementation in conversion of corncob residue and other lignocellulosic biomass into simple sugars.
对一株斜卧青霉来源的β-葡萄糖苷酶进行了纯化和表征。该酶在SDS-PAGE上呈现为一条120kDa的单带，最适温度为65-70°C，最适pH为4.5-5.0。该β-葡萄糖苷酶对pNPG的亲和力相对较高，对水杨苷的亲和力最高，其Km值分别为0.0064和0.0188mM。获得了编码该酶的基因，其开放阅读框为2586bp，编码861个氨基酸，属于糖苷水解酶家族3。将纯化后的酶添加到里氏木霉QM 9414的纤维素酶体系中时，可提高纤维素的糖化能力。该酶的几个特性，包括其最适pH和温度、对底物的高亲和力和高比活性，使其在将玉米芯残渣和其他木质纤维素生物质转化为单糖的过程中作为补充剂具有巨大的应用潜力。
