Stewart P, Whitwam R E, Kersten P J, Cullen D, Tien M
Department of Bacteriology, University of Wisconsin, Madison 53706, USA.
Appl Environ Microbiol. 1996 Mar;62(3):860-4. doi: 10.1128/aem.62.3.860-864.1996.
A manganese peroxidase gene (mnp1) from Phanerochaete chrysosporium was efficiently expressed in Aspergillus oryzae. Expression was achieved by fusing the mature cDNA of mnp1 with the A. oryzae Taka amylase promoter and secretion signal. The 3' untranslated region of the glucoamylase gene of Aspergillus awamori provided the terminator. The recombinant protein (rMnP) was secreted in an active form, permitting rapid detection and purification. Physical and kinetic properties of rMnP were similar to those of the native protein. The A. oryzae expression system is well suited for both mechanistic and site-directed mutagenesis studies.
来自黄孢原毛平革菌的一种锰过氧化物酶基因（mnp1）在米曲霉中得到了高效表达。通过将mnp1的成熟cDNA与米曲霉Taka淀粉酶启动子和分泌信号融合来实现表达。泡盛曲霉葡糖淀粉酶基因的3'非翻译区提供了终止子。重组蛋白（rMnP）以活性形式分泌，便于快速检测和纯化。rMnP的物理和动力学性质与天然蛋白相似。米曲霉表达系统非常适合进行机理研究和定点诱变研究。
