Producing of supercritical carbon dioxide-tolerant enzyme based on halo-tolerant enzyme and syntheses of chitin oligosaccharide
Project/Area Number |
23550177
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Environmental chemistry
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Research Institution | Tokyo Institute of Technology |
Principal Investigator |
YATSUNAMI Rie 東京工業大学, 生命理工学研究科, 助教 (90334531)
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Project Period (FY) |
2011-04-28 – 2015-03-31
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Project Status |
Completed (Fiscal Year 2014)
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Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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Keywords | 耐塩化酵素 / 超臨界二酸化炭素 / オリゴ糖合成 / 高度好塩性古細菌 / キチナーゼ / キチンオリゴ糖合成 / 国際情報交換 / 国際情報交流 |
Outline of Final Research Achievements |
Genome sequencing of extremely halophilic archaeon Halobacterium salinarum NRC-1 was completed, and a chitinase-homolog (ChiN1) was found. The gene encoding ChiN1 was expressed in extremely halophilic archaeon Haloarcula japonica. The recombinant ChiN1 was most active at 1.0 M NaCl. Supercritical carbon dioxide (scCO2) is attracting as an environmentally friendly solvent since CO2 is an abundant resource. The scCO2 has been used as a solvent for enzyme-catalyzed organic synthesis. However, many enzymes are unstable in scCO2. In this study, some ChiN1 mutants with less lysines on its protein surface were prepared and characterized to find a category of enzymes with high tolerance toward CO2 pressurization. On the basis of the 3D structure model of ChiN1, more solvent-accessible lysines were replaced by alanines. The Ha. japonica-produced mutants were prepared and assayed for chitinase activity in scCO2. Two mutants showed higher activity than wild-type ChiN1 in 10 MPa scCO2 for 1 h.
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Report
(5 results)
Research Products
(52 results)
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[Journal Article] Identification of carotenoids from the extremely halophilic archaeon Haloarcula japonica2014
Author(s)
R. Yatsunami, A. Ando, Y. Yang, S. Takaichi, M. Kohno, Y. Matsumura, H. Ikeda, T. Fukui, K. Nakasone, N. Fujita, M. Sekine, T. Takashina, S. Nakamura
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Journal Title
Frontiers in Microbiology
Volume: 100
Pages: 1-5
DOI
Related Report
Peer Reviewed
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[Journal Article] Gene Analysis, Expression, and Characterization of an Intracellular α-Amylase from the Extremely Halophilic Archaeon <i>Haloarcula japonica</i>2013
Author(s)
M. Onodera, R. Yatsunami, W. Tsukimura, T. Fukui, K. Nakasone, T. Takashina and S. Nakamura
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Journal Title
Bioscience, Biotechnology, and Biochemistry
Volume: 77
Issue: 2
Pages: 281-288
DOI
NAID
ISSN
0916-8451, 1347-6947
Related Report
Peer Reviewed
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[Presentation] Characterization of crtI homologs and antioxidant capacity of carotenoids from extremely halophilic archaeon Haloarcula japonica2013
Author(s)
Rie Yatsunami, Ai Ando, Ying Yang, Shinichi Takaichi, Masahiro Kohno, Yuriko Matsumura, Toshiaki Fukui, Kaoru Nakasone,Nobuyuki Fujita, Mitsuo Sekine, Tomonori Takashina, Satoshi Nakamura
Organizer
2013 Halophiles Conference
Place of Presentation
コネチカット州、アメリカ
Related Report
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[Presentation] Characterization of a haloarchaeal chitinase: Effect of aspartates, glutamates and lysines on its protein surface2013
Author(s)
Kinuka Toyama, Koichi Sakagami, Zang Yang, An Ran, Motoaki Sato, Keita Orishimo1, Yoshinobu Hatori, Rie Yatsunami, Tomonori Takashina, Toshiaki Fukui, Satoshi Nakamura
Organizer
27th Japanese Chitin & Chitosan Symposiun/10th Asia-Pacific Chitin &Chitosan Symposiun
Place of Presentation
米子、日本
Related Report
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[Presentation] Physiological function and some properties of possible aerotaxis transducer Htr8 from extremely halophilic archaeon Haloarcula japonica2012
Author(s)
T. Matsubara, T. Tadikara, Y. Kubota, T. Kosaka, T. Ozawa, R. Yatsunami, T. Fukui, K. Nakasone, N. Fujita, M. Sekine, T. Takashina, S. Nakamura
Organizer
The First International Symposium on Biofunctional Chemistry (ISBC2012)
Place of Presentation
東工大蔵前会館(東京)
Related Report
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