| Co-Investigator(Kenkyū-buntansha) |
趙 洪よん 韓国高麗大学校, 自然科学大学, 副教授
成 文喜 韓国科学技術研究院, 生命工学研究所, 責任研究員
張 樹政 中国科学院, 微生物学研究所, 教授
SAMARKIN V.A ロシア科学アカデミー, 微生物生化学生理学研究所, 高等研究員
KELLER J.W. アラスカ大学, 化学部, 教授
KURIHARA Tatsuo Institute for Chemical Research, Kyoto University, Instructor, 化学研究所, 助手 (70243087)
YOSHIMURA Tohru Institute for Chemical Research, Kyoto University, Associate Professor, 化学研究所, 助教授 (70182821)
SODA Kenji Faculty of Engineering, Kansai University, Professor, 工学部, 教授 (30027023)
CHO Hong Yon Graduate School of Biotechnology Korea University, Associate Professor
SUNG Moon-Hee Korea Research Institute of Bioscience and Biotechnology, KIST,Principal Researc
ZHANG Shu Chen Institute of Microbiology, Academica Cinica, Professor
SAMARKIN Vladimir A Institute of Soil Science and Photosynthesis, Russion Academy of Sciences, Senio
KELLER John W Department of Chemistry University of Alaska Fairbanks, Professor
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| Research Abstract |
Enzymes showing the high activities at low temperature are applicable to the additives for the detergent, food processing, enzymatic synthesis of the thermolabile materials, and so on. We tried to find these enzymes from the psychrotrophic and psychrophilic bacteria grown under the extreme conditions. Two lipase-like genes were cloned to E.coli cells from Pseudomonas sp.B11-1 and Acinetobacter sp.No.6 cells which were isolated from the cold environment. The former gene encodes the 676-aminoacid protein with the molecular weight of 72,900. This lipase contains no GxSyG motif which is considered to be common in all lipases so far studied. The gene from Acinetobacter sp.No.6 encodes the 258-amino-acid protein with the molecular weight of 28,423. The primary structure of the protein is similar to that o^f beta-ketoadipate enol lactone hydrolase of Acinetobacter calcoaceticus. The activation energies in the rho-nitrophenyl-butyl-ester hydrolysis catalyzed by both enzymes were obtained from the Arrhenius plots of the reactions. The activation energies were calculated to be 11.2 and 11.3 (Kcal/mol) with the Pseudomonas enzyme and Acinetobacter enzyme, respectively. These values are lower that that in the reaction with the lipase from the mesophile, Pseudomonas aeruginosa (25Kcal/mol).
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