| Project/Area Number |
11555209
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 展開研究 |
|---|
| Research Field |
反応・分離工学
|
|---|
| Research Institution | Osaka Prefecture University |
|---|
Principal Investigator |
ISHIKAWA Haruo Osaka Prefecture University, Graduated School of Engineering, Professor, 大学院・工学研究科, 教授 (00081349)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
OGINO Hiroyasu Osaka Prefecture University, Graduated School of Engineering, Lecturer, 大学院・工学研究科, 講師 (80233443)
GOTO Masahiro Kyushu University, Graduated School of Engineering, Professor, 大学院・工学研究科, 教授 (10211921)
FURUSAKI Shintaro Sojo University, Faculty of Engineering, Professor, 工学部, 教授 (40011209)
SHIBATANI Takeji Tanabe Seiyaku Co. Ltd., Discovery Research Laboratory, Department Manager, 創薬研究所, 部長研究員
YASUDA Masahiro Osaka Prefecture University, Graduated School of Engineering, Assistant Professor, 大学院・工学研究科, 助手 (40264808)
|
|---|
| Project Period (FY) |
1999 – 2001
|
| Keywords | nonaqueous Bioprocess / organic solvent-tolerant enzyme / organic solvent-tolerant immobilized enzyme / modified enzyme material / organic solvent-tolerant microorganism / peptide synthesis / amphiphilic polymer particle / surfactant |
|---|
| Research Abstract |
An organic solvent-tolerant protease (PST-01 protease) from Pseudomonas aeruginosa PST-01 was purified and characterized. The PST-01 protease was stable in the presence of various organic solvents. Peptide syntheses were performed in monophasic aqueous solution containing an organic solvent using PST-01 protease. The initial reaction rate and the equilibrium yield of the peptide in the presence of 60%(v/v) DMSO were 5.1 times and 7.0 times higher than that in the absence of an organic solvent, respectively.
Amphiphilic polymer particles which have hydrophilic guanidino groups and hydrophobic stearoyl groups were the best particles for the immobilization of Rhizopus delemar lipase. The hydrolytic activity of the immobilized lipase prepared with the amphiphilic polymer particles was 150-8700 times higher than those of the immobilized lipases prepared by previous investigators using Dowex MWA-1, porous glass beads, and Sepharose 4B. The stability and the transesterification activity of lipase were both enhanced by immobilizing lipase on the amphiphilic polymer particles. The specific transesterification activity of the immobilized lipase prepared with the amphiphilic polymer particles was 93.4 times higher than that of the lyophilized lipase.
Surfactant-coated protease was prepared with a synthesized surfactant. The peptide synthetic activity and transeste rification activity of the surfactant-coated protease in organic solvents were higher than that of the powder protease. The activity of the surfactant-coated protease was 260 times higher that of the powder protease.
|
