Department of Fermentation Technology, Faculty of Engineering, Osaka University, Yamada-oka, Suita-shi, Osaka 565, and Biochemical Research Laboratories, Ezaki Glico Co., Ltd., Nishiyodogawa-ku, Osaka 555, Japan.
Appl Environ Microbiol. 1988 Nov;54(11):2881-3. doi: 10.1128/aem.54.11.2881-2883.1988.
A thermostable pullulanase (alpha-dextrin 6-glucanohydrolase [EC 3.2.1.41]) from a newly isolated Bacillus stearothermophilus strain (TRS128) was purified and characterized. The enzyme hydrolyzed (1-->6)-alpha-d-glucosidic linkages of pullulan to produce maltotriose, and the optimum temperature was 65 degrees C. About 90% of the enzyme activity was retained after treatment at 65 degrees C for 60 min. By using pTB522 as a vector plasmid, the pullulanase gene was cloned and expressed in Bacillus subtilis.
一株嗜热解聚酶（α-糊精 6-葡聚糖水解酶[EC3.2.1.41]）从一个新分离的嗜热脂肪芽孢杆菌菌株（TRS128）中被纯化并进行了特性描述。该酶水解普鲁兰的（1-->6）-α-D-葡萄糖苷键，产生麦芽三糖，最适温度为 65℃。在 65℃处理 60 分钟后，约 90%的酶活性得以保留。利用 pTB522 作为载体质粒，在枯草芽孢杆菌中克隆并表达了该解聚酶基因。
