Zappe H, Jones D T, Woods D R
J Gen Microbiol. 1986 May;132(5):1367-72. doi: 10.1099/00221287-132-5-1367.
Clostridium acetobutylicum P262 endoglucanase and cellobiase genes, cloned on a 4.9 kb DNA fragment in the recombinant plasmid pHZ100, were expressed from their own promoter in Escherichia coli. Active carboxymethylcellulase and cellobiase enzymes were produced, but there was no degradation of Avicel. The endoglucanase activities observed in cell extracts of E. coli HB101(pHZ100) differed in their pH and temperature optima from those previously reported for C. acetobutylicum P270. Complementation of E. coli arg and his mutations by cloned C. acetobutylicum DNA was also observed.
丙酮丁醇梭菌P262内切葡聚糖酶和纤维二糖酶基因克隆于重组质粒pHZ100的4.9 kb DNA片段上，在大肠杆菌中由其自身启动子进行表达。产生了具有活性的羧甲基纤维素酶和纤维二糖酶，但微晶纤维素未被降解。在大肠杆菌HB101(pHZ100)细胞提取物中观察到的内切葡聚糖酶活性，其最适pH和温度与先前报道的丙酮丁醇梭菌P270的不同。还观察到克隆的丙酮丁醇梭菌DNA对大肠杆菌arg和his突变的互补作用。
