Staff

KONDO HidemasaVisiting Associate Professor

Laboratory
Laboratory of Biomolecular Adaptation Science
Research Theme
Characterization and improvement of industrial proteins
Research Keywords

structural biology, antifreeze protein, industrial protein, industrial enzyme

Overview of Research

A main focus of my research is to elucidate the structural principle for the biological activities of functional proteins, especially which can be utilized for bioproduction and bioprocessing of the novel biomaterials. By using X-ray crystallography, we have analyzed the 3D structures of functional proteins including various antifreeze proteins and industrial enzymes. Based on detailed insights of the 3D structure of functional proteins, combined with other biochemical and molecular biological study, we have clarified the molecular mechanism of their function to product modified proteins with advanced properties.

Charge

  • School of Science:
    No
  • Graduate School of Life Science:
    Division of Life Science, Transdisciplinary Life Science Course, Biomolecular Adaptation Science (Inter-field Cooperation with AIST)

Message

X-ray crystallography is one of the most powerful tools to determine the 3D structure of the biological molecules. I would like to contribute to bring up young scientists and engineers through our researches including the structure determination, presentation and publication.

Representative Publications

Rahman, A.T., Arai, T., Yamauchi, A., Miura, A., Kondo, H., Ohyama, Y., and Tsuda, S., Ice recrystallization is strongly inhibited when antifreeze proteins bind to multiple ice planes. Sci. Rep., 9, 2212 (2019).

Arai, T., Fukami, D., Hoshino, T., Kondo, H., and Tsuda, S., Ice-binding proteins from the fungus Antarctomyces psychrotrophicus possibly originate from two different bacteria through horizontal gene transfer. FEBS J., 286, 946-962 (2019).

Kondo, H., Mochizuki, K., and Bayer-Giraldi, M., Multiple binding modes of a moderate ice-binding protein from a polar microalga. Phys. Chem. Chem. Phys., 20, 25295-25303 (2018).

Mahatabuddin, S., Fukami, D., Arai, T., Nishimiya, Y., Shimizu, R., Shibazaki, C., Kondo, H., Adachi, M., and Tsuda, S., Polypentagonal ice-like water networks emerge solely in an activity-improved variant of ice-binding protein. Proc. Natl. Acad. Sci. USA, 115, 5456-5461 (2018).

Mahatabuddin, S., Hanada, Y., Nishimiya, Y., Miura, A., Kondo, H., Davies P.L., and Tsuda, S. Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive. Sci. Rep., 7, 42501 (2017).

Cheng, J., Hanada, Y., Miura, A., Tsuda, S., and Kondo, H. Hydrophobic ice-binding sites confer hyperactivity of an antifreeze protein from a snow mold fungus. Biochem. J., 473, 4011-4026 (2016).

Note

<Office Hour>
– Time: Anytime during the lecture period
– Place: Science Bldg. No.2, 8F, #2-804
Please contact in advance by E-mail.
E-mail: h.kondo[at]aist.go.jp

Affiliation

  • National Institute of Advanced Industrial Science and Technology (AIST) Hokkaido