Miettinen-Oinonen A, Torkkeli T, Paloheimo M, Nevalainen H
Primalco Ltd Biotec, Rajamäki, Finland.
J Biotechnol. 1997 Oct 2;58(1):13-20. doi: 10.1016/s0168-1656(97)00121-1.
An Aspergillus gene coding for a pH 2.5 acid phosphatase enzyme was successfully overexpressed in Trichoderma reesei under the strong main cellobiohydrolase I (cbh 1) promoter. The best transformants produced up to 240 times more of the acid phosphatase than the Aspergillus strain from which the phosphatase gene was originally isolated. The recombinant enzyme was effectively secreted into the culture medium both by its own and the cbh 1 secretion signal. The heterologous pH 2.5 acid phosphatase enzyme produced by the Trichoderma transformants was seen as four protein bands of about 55-66 kD resulting from variable glycosylation in Trichoderma. The activity of the recombinant enzyme was not affected. Enzyme preparations rich in both cellulose and phytate hydrolysing enzymes are of interest in the animal feed industry.
一个编码pH 2.5酸性磷酸酶的曲霉基因在里氏木霉中，在强大的主要纤维二糖水解酶I（cbh 1）启动子控制下成功实现了过表达。最佳转化体产生的酸性磷酸酶比最初分离磷酸酶基因的曲霉菌株多240倍。重组酶通过自身的和cbh 1的分泌信号有效地分泌到培养基中。里氏木霉转化体产生的异源pH 2.5酸性磷酸酶被视为约55 - 66 kD的四条蛋白带，这是里氏木霉中可变糖基化的结果。重组酶的活性未受影响。富含纤维素和植酸水解酶的酶制剂在动物饲料工业中具有重要意义。
