Yabuki M, Ono N, Hoshino K, Fukui S
Appl Environ Microbiol. 1977 Jul;34(1):1-6. doi: 10.1128/aem.34.1.1-6.1977.
A rapid induction system for synthesis of alpha-amylase by the funga Aspergillus oryzae M-13 was established. The mycelia were prepared from 20-h cultures grown on a peptone-glycerol medium and starved for 5 h; maltose was the optimum inducer tested. During h 1 of induction, formation of both intra- and extracellular alpha-amylases occurred at an almost identical rate (70 to 80 microgram/g of cells-h) without a detectable lag period. After a 1-h induction period, a remarkable increase in the extracellular concentration of the enzyme occurred, and a maximum rate (330 microgram/g of cells-h) was reached after 1.5 h of induction. During h 2 of induction, no significant change in mycelial weight was observed. Purified samples of intra- and extracellular enzymes formed in the induction system showed identical properties as examined by behavior in diethylaminoethyl-cellulose column chromatography, gel filtration, discontinuous gel electrophoresis, electrofocusing, optimal conditions for the reaction, heat stability, and molecular weight.
建立了一种用于米曲霉M-13合成α-淀粉酶的快速诱导系统。菌丝体取自于在蛋白胨-甘油培养基上培养20小时并饥饿5小时的培养物；麦芽糖是所测试的最佳诱导剂。在诱导的第1小时内，细胞内和细胞外α-淀粉酶的形成速率几乎相同（70至80微克/克细胞·小时），且无明显延迟期。经过1小时的诱导期后，酶的细胞外浓度显著增加，诱导1.5小时后达到最大速率（330微克/克细胞·小时）。在诱导的第2小时内，未观察到菌丝体重量有显著变化。在诱导系统中形成的细胞内和细胞外酶的纯化样品，通过二乙氨基乙基纤维素柱色谱行为、凝胶过滤、不连续凝胶电泳、等电聚焦、反应最佳条件、热稳定性和分子量检测，显示出相同的特性。
