Kadam S K, Demain A L
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Biochem Biophys Res Commun. 1989 Jun 15;161(2):706-11. doi: 10.1016/0006-291x(89)92657-0.
A thermostable beta-glucosidase from Clostridium thermocellum which is expressed in Escherichia coli was used to determine the substrate specificity of the enzyme. A restriction map of the beta-glucosidase gene cloned in plasmid pALD7 was determined. Addition of the E. coli cell extract (containing the beta-glucosidase) to the cellulase complex from C. thermocellum increased the conversion of crystalline cellulose (Avicel) to glucose. The increase was specifically due to hydrolysis of the accumulated cellobiose. A cellulose degradation process using beta-glucosidase to assist the potent cellulase complex of C. thermocellum, as shown here can open the way for industrial saccharification of cellulose to glucose.
一种在大肠杆菌中表达的来自热纤梭菌的耐热β-葡萄糖苷酶被用于确定该酶的底物特异性。测定了克隆在质粒pALD7中的β-葡萄糖苷酶基因的限制酶切图谱。将大肠杆菌细胞提取物(含有β-葡萄糖苷酶)添加到热纤梭菌的纤维素酶复合物中,可提高结晶纤维素(微晶纤维素)向葡萄糖的转化率。这种增加具体是由于积累的纤维二糖的水解。如本文所示,利用β-葡萄糖苷酶辅助热纤梭菌强大的纤维素酶复合物进行纤维素降解过程,可为纤维素工业糖化生产葡萄糖开辟道路。