title: Purification and Characterization of Thermostable Pullulanase from Bacillus stearothermophilus and Molecular Cloning and Expression of the Gene in Bacillus subtilis.
abstract: 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.
authors.affiliation: 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.
authors.forename: T
authors.initials: T
authors.lastname: Kuriki
authors.forename: J H
authors.initials: JH
authors.lastname: Park
authors.forename: S
authors.initials: S
authors.lastname: Okada
authors.forename: T
authors.initials: T
authors.lastname: Imanaka