Updated on 2025/09/30

写真a

 
YATSUNAMI RIE
 
Organization
School of Life Science and Technology Associate Professor
Title
Associate Professor
Homepage
http://www.nakamura.bio.titech.ac.jp
External link

Degree

  • Doctor of Engineering ( Tokyo Institute of Technology )

Research Interests

  • Extrephile

  • Molecular Biology

  • Protein Engineering

  • metabolic engineering

  • Extremozyme

Research Areas

  • Manufacturing Technology (Mechanical Engineering, Electrical and Electronic Engineering, Chemical Engineering) / Biofunction and bioprocess engineering

  • Life Science / Applied microbiology

  • Life Science / Molecular biology

Education

  • Tokyo Institute of Technology   Bioscience and Biotechnology

    1997.4 - 2000.3

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    Country： Japan

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  • Nagasaki University   Graduate school of Engineering

    1993.4 - 1995.3

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  • Nagasaki University   Faculty of Engineering

    1989.4 - 1993.3

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    Country： Japan

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Research History

  • Tokyo Institute of Technology   School of Life Science and Technology   Associate Professor

    2016.4

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  • Tokyo Institute of Technology   Graduate School of Bioscience and Biotechnology Department of Bioengineering   Associate Professor

    2015.11 - 2016.3

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  • Tokyo Institute of Technology   Graduate School of Bioscience and Biotechnology Department of Bioengineering   Assistant Professor

    2007.4 - 2015.10

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  • Tokyo Institute of Technology   Graduate School of Bioscience and Biotechnology Department of Bioengineering

    2001.4 - 2007.3

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  • Japan Advanced Institute of Science and Technology

    2000.4 - 2001.3

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  • Tokyo Institute of Technology   School of Bioscience and Biotechnology

    1997.4 - 2000.3

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  • Tokyo Institute of Technology   School of Bioscience and Biotechnology

    1996.10 - 1997.3

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  • 艶金興業株式会社

    1995.4 - 1996.9

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Professional Memberships

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Committee Memberships

  • 日本農芸化学会   ダイバーシティー推進委員会委員  

    2021   

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  • Microbes & Environments   associate editor  

    2019   

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  • 酵素工学研究会   幹事  

    2017   

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    Committee type：Academic society

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  • 日本農芸化学会   和文誌編集委員  

    2017 - 2020   

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    Committee type：Academic society

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  • 極限環境生物学会   学術幹事  

    2013   

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    Committee type：Academic society

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Papers

  • Characterization of a xylanase belonging to the glycoside hydrolase family 5 subfamily 35 from Paenibacillus sp. H2C. Reviewed International journal

    Yusuke Hagiwara, Tomohiro Okeda, Keiko Okuda, Rie Yatsunami, Satoshi Nakamura

    Bioscience, biotechnology, and biochemistry   87 ( 1 )   54 - 62   2022.12

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    Language：English   Publishing type：Research paper (scientific journal)  

    Corn xylan is resistant to enzymatic hydrolysis due to its complex structure. We characterized PsXyn5A, an enzyme highly active for corn xylan, isolated from Paenibacillus sp. H2C. PsXyn5A is a modular xylanase with a catalytic domain belonging to the glycoside hydrolase family 5 subfamily 35 (GH5_35) and a carbohydrate-binding module family 13 (CBM13) domain. The substrate recognition mechanism of GH5_35 xylanase has not been reported. Analysis of the hydrolysate from rye arabinoxylan (RAX) has shown that the GH5_35 catalytic domain of PsXyn5A recognizes an arabinofuranosyl (Araf) side residue and cleaves the reducing terminal side of Araf-linked xylopyranose. This cleavage specificity is the same as reported for the GH5_34 xylanase from Hungateiclostridium thermocellum (HtXyl5A). Unlike HtXyl5A, PsXyn5A produced Araf-xylopyranose from RAX and did not hydrolyze 33-α-l-Araf-xylotetraose. Deletion of the CBM13 domain significantly decreased the activity toward insoluble corn xylan, indicating that CBM13 plays an essential role in hydrolyzing corn xylan.

    DOI： 10.1093/bbb/zbac175

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  • Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica. Reviewed International journal

    Shintaro Nagaoka, Noriko Sugiyama, Rie Yatsunami, Satoshi Nakamura

    Bioscience, biotechnology, and biochemistry   85 ( 9 )   1986 - 1994   2021.8

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    3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 m KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH.

    DOI： 10.1093/bbb/zbab122

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  • The mutation of Thr315 to Asn of GH10 xylanase XynR increases the alkaliphily but decreases the alkaline resistance. Reviewed International journal

    Kohei Kuwata, Manami Suzuki, Teisuke Takita, Rie Yatsunami, Satoshi Nakamura, Kiyoshi Yasukawa

    Bioscience, biotechnology, and biochemistry   85 ( 8 )   1853 - 1860   2021.7

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    XynR is a thermophilic and alkaline GH10 xylanase, identified in the culture broth of alkaliphilic and thermophilic Bacillus sp. strain TAR-1. We previously selected S92E as a thermostable variant from a site saturation mutagenesis library. Here, we attempted to select the alkaliphilic XynR variant from the library and isolated T315N. In the hydrolysis of beechwood xylan, T315N and S92E/T315N exhibited a broader bell-shaped pH-dependent activity than the wild-type (WT) XynR and S92E. The optimal pH values of T315N and S92E/T315N were 6.5-9.5 while those of WT and S92E were 6.5-8.5. On the other hand, T315N and S92E/T315N exhibited a narrower bell-shaped pH dependence of stability: the pHs at which the activity was stable after the incubation at 37 °C for 24 h were 6.0-8.5 for T315N and S92E/T315N, but 6.0-10.0 for WT and S92E. These results indicated that the mutation of Thr315 to Asn increased the alkaliphily but decreased the alkaline resistance.

    DOI： 10.1093/bbb/zbab102

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  • Characterization of a GlgC homolog from extremely halophilic archaeon Haloarcula japonica. Reviewed International journal

    Rin Sueda, Kento Yoshida, Masahiko Onodera, Toshiaki Fukui, Rie Yatsunami, Satoshi Nakamura

    Bioscience, biotechnology, and biochemistry   85 ( 6 )   1441 - 1447   2021.5

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    Glycogen synthesis in bacteria is mainly organized by the products of glgB, glgC, and glgA genes comprising the widely known glg operon. On the genome of extremely halophilic archaeon Haloarcula japonica, there was a gene cluster analogous to the bacterial glg operon. In this study, we focused on a GlgC homolog of Ha. japonica, and its recombinant enzyme was prepared and characterized. The enzyme showed highest activity toward GTP and glucose-1-phosphate as substrates in the presence of 2.6 m KCl and predicted to be work as "GDP-glucose pyrophosphorylase" in Ha. japonica.

    DOI： 10.1093/bbb/zbab050

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  • Functional expression of the reverse transcriptase αβ heterodimer from avian myeloblastosis virus in Escherichia coli. Reviewed International journal

    Yuriko Makino, Hiroshi Sato, Atsushi Noguchi, Teruhiko Ide, Rie Yatsunami, Satoshi Nakamura

    Bioscience, biotechnology, and biochemistry   85 ( 6 )   1464 - 1467   2021.5

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    The α subunit of avian myeloblastosis virus reverse transcriptase (AMV-RT) is generated from the β-subunit by proteolysis, and the αβ heterodimer represents the active form. The codon-optimized gene was expressed in Escherichia coli, and an active αβ heterodimer was generated. The RNA amplification activity of the purified recombinant AMV-RT αβ heterodimer was similar to that of the native one.

    DOI： 10.1093/bbb/zbab057

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  • Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E. Reviewed International journal

    Manami Suzuki, Teisuke Takita, Kohei Kuwata, Kota Nakatani, Tongyang Li, Yuta Katano, Kenji Kojima, Kimihiko Mizutani, Bunzo Mikami, Rie Yatsunami, Satoshi Nakamura, Kiyoshi Yasukawa

    Bioscience, biotechnology, and biochemistry   85 ( 2 )   386 - 390   2021.2

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    The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95.

    DOI： 10.1093/bbb/zbaa003

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  • Isolation of four xylanases capable of hydrolyzing corn fiber xylan from Paenibacillus sp. H2C. Reviewed International journal

    Yusuke Hagiwara, Yasuhiro Mihara, Koichi Sakagami, Ryuta Sagara, Undramaa Bat-Erdene, Rie Yatsunami, Satoshi Nakamura

    Bioscience, biotechnology, and biochemistry   84 ( 3 )   640 - 650   2020.3

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    Corn fibre xylan (CX) shows high resistance to enzymatic hydrolysis due to its densely decorated side chains. To find enzymes capable of hydrolyzing CX, we isolated a bacterial strain (named H2C) from soil, by enrichment culture using non-starch polysaccharides of corn as the sole carbon source. Analysis based on the 16S rRNA sequence placed strain H2C within genus Paenibacillus. Enzymes were purified from supernatant of culture broth of strain H2C based on solubilizing activities toward CX. Four enzymes, Xyn5A, Xyn10B, Xyn11A, and Xyn30A, were successfully identified, which belong to glycoside hydrolase (GH) families, 5, 10, 11, and 30, respectively. Phylogenetic analysis classified Xyn5A in subfamily 35 of GH family 5, a subfamily of unknown function. Their activities toward beechwood xylan and/or wheat arabinoxylan indicated that these enzymes are β-1,4-xylanases. They showed high solubilizing activities toward a feed material, corn dried distiller's grains with solubles, compared to five previously characterized xylanases.Abbreviations : CX: corn fibre xylan; DDGS: corn dried distiller's grains with solubles.

    DOI： 10.1080/09168451.2019.1693253

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  • Characterization of novel arabinofuranosidases from Paenibacillus sp. strain H2C Reviewed

    K. Okuda, K. Ito, Y. Hagiwara, T. Okeda, R. Yatsunami, T. Fukui, S. Nakamura

    J. Jpn. Soc. Extremophiles   16   37 - 45   2020

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  • The novel potent TEAD inhibitor, K-975, inhibits YAP1/TAZ-TEAD protein-protein interactions and exerts an anti-tumor effect on malignant pleural mesothelioma. Reviewed International journal

    Ayumi Kaneda, Toshihiro Seike, Tomohiro Danjo, Takahiro Nakajima, Nobumasa Otsubo, Daisuke Yamaguchi, Yoshiro Tsuji, Kaori Hamaguchi, Mai Yasunaga, Yoichi Nishiya, Michihiko Suzuki, Jun-Ichi Saito, Rie Yatsunami, Satoshi Nakamura, Yoshitaka Sekido, Kiyotoshi Mori

    American journal of cancer research   10 ( 12 )   4399 - 4415   2020

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    The Hippo signaling pathway regulates cell fate and organ development. In the Hippo pathway, transcriptional enhanced associate domain (TEAD) which is a transcription factor is activated by forming a complex with yes-associated protein 1 (YAP1) or transcriptional coactivator with PDZ-binding motif (TAZ, also called WWTR1). Hyper-activation of YAP1/TAZ, leading to the activation of TEAD, has been reported in many cancers, including malignant pleural mesothelioma (MPM). Therefore, the YAP1/TAZ-TEAD complex is considered a novel therapeutic target for cancer treatment. However, few reports have described YAP1/TAZ-TEAD inhibitors, and their efficacy and selectivity are poor. In this study, we performed a high-throughput screening of a neurofibromin 2 (NF2)-deficient MPM cell line and a large tumor suppressor kinase 1/2 (LATS1/2)-deficient non-small-cell lung cancer cell line using a transcriptional reporter assay. After screening and optimization, K-975 was successfully identified as a potent inhibitor of YAP1/TAZ-TEAD signaling. X-ray crystallography revealed that K-975 was covalently bound to an internal cysteine residue located in the palmitate-binding pocket of TEAD. K-975 had a strong inhibitory effect against protein-protein interactions between YAP1/TAZ and TEAD in cell-free and cell-based assays. Furthermore, K-975 potently inhibited the proliferation of NF2-non-expressing MPM cell lines compared with NF2-expressing MPM cell lines. K-975 also suppressed tumor growth and provided significant survival benefit in MPM xenograft models. These findings indicate that K-975 is a strong and selective TEAD inhibitor with the potential to become an effective drug candidate for MPM therapy.

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  • Increase in the thermostability of GH11 xylanase XynJ from Bacillus sp. strain 41M-1 using site saturation mutagenesis. Reviewed International journal

    Teisuke Takita, Kota Nakatani, Yuta Katano, Manami Suzuki, Kenji Kojima, Naoki Saka, Bunzo Mikami, Rie Yatsunami, Satoshi Nakamura, Kiyoshi Yasukawa

    Enzyme and microbial technology   130   109363 - 109363   2019.11

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    GH11 xylanase XynJ from Bacillus sp. strain 41M-1 has a β-jellyroll fold composed of eight β strands with a deep active-site cleft. We hypothesized that the thermostability of XynJ will increase if the flexibility of the β strands in the jellyroll structure is decreased without impairing activity. To verify this hypothesis, we introduced random mutations into Tyr13-Arg104 and Gly169-Tyr194, both of which are located in the β-jellyroll fold of XynJ, to construct a site saturation mutagenesis library. By screening 576 clones followed by site saturation mutation analysis of Thr82, T82A was selected as the most thermostable variant. In the hydrolysis of beechwood xylan at pH 7.8, the temperatures required to reduce initial activity by 50% in 15 min were 61 °C for the wild-type XynJ (WT) and 65 °C for T82A. The optimum hydrolysis temperatures were 60 °C for WT and 65 °C for T82A. There was little difference in the kcat and Km values and the pH dependence of activity between WT and T82A. Crystallographic analysis of WT and T82A revealed that thermostabilization by the T82A mutation might result from the removal of unfavorable van der Waals interactions. Thus, a highly thermostable XynJ variant was generated without impairing activity using this mutation strategy.

    DOI： 10.1016/j.enzmictec.2019.109363

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  • Increase in the thermostability of Bacillus sp. strain TAR-1 xylanase using a site saturation mutagenesis library. Reviewed International journal

    Kota Nakatani, Yuta Katano, Kenji Kojima, Teisuke Takita, Rie Yatsunami, Satoshi Nakamura, Kiyoshi Yasukawa

    Bioscience, biotechnology, and biochemistry   82 ( 10 )   1715 - 1723   2018.10

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    UNLABELLED: Site saturation mutagenesis library is a recently developed technique, in which any one out of all amino acid residues in a target region is substituted into other 19 amino acid residues. In this study, we used this technique to increase the thermostability of a GH10 xylanase, XynR, from Bacillus sp. strain TAR-1. We hypothesized that the substrate binding region of XynR is flexible, and that the thermostability of XynR will increase if the flexibility of the substrate binding region is decreased without impairing the substrate binding ability. Site saturation mutagenesis libraries of amino acid residues Tyr43-Lys115 and Ala300-Asn325 of XynR were constructed. By screening 480 clones, S92E was selected as the most thermostable one, exhibiting the residual activity of 80% after heat treatment at 80°C for 15 min in the hydrolysis of Remazol Brilliant Blue-xylan. Our results suggest that this strategy is effective for stabilization of GH10 xylanase. ABBREVIATIONS: DNS: 3,5-dinitrosalicylic acid; RBB-xylan: Remazol Brilliant Blue-xylan.

    DOI： 10.1080/09168451.2018.1495550

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  • Complete Biosynthetic Pathway of the C-50 Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica Reviewed International journal

    Ying Yang, Rie Yatsunami, Ai Ando, Nobuhiro Miyoko, Toshiaki Fukui, Shinichi Takaichi, Satoshi Nakamura

    JOURNAL OF BACTERIOLOGY   197 ( 9 )   1614 - 1623   2015.5

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    Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1128/JB.02523-14

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  • Identification of carotenoids from the extremely halophilic archaeon Haloarcula japonica Reviewed International journal

    Rie Yatsunami, Ai Ando, Ying Yang, Shinichi Takaichi, Masahiro Kohno, Yuriko Matsumura, Hiroshi Ikeda, Toshiaki Fukui, Kaoru Nakasone, Nobuyuki Fujita, Mitsuo Sekine, Tomonori Takashina, Satoshi Nakamura

    FRONTIERS IN MICROBIOLOGY   5 ( 5 )   100 - 104   2014.3

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    Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.3389/fmicb.2014.00100

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  • Combination of site-directed mutagenesis and calcium ion addition for enhanced production of thermostable MBP-fused heparinase I in recombinant Escherichia coli. Reviewed International journal

    Shuo Chen, Ziliang Huang, Jingjun Wu, Yin Chen, Fengchun Ye, Chong Zhang, Rie Yatsunami, Satoshi Nakamura, Xin-Hui Xing

    Applied microbiology and biotechnology   97 ( 7 )   2907 - 16   2013.4

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    Heparinase I (HepI), which specifically cleaves heparin and heparan sulfate, is one of the most extensively studied glycosaminoglycan lyases. Low productivity of HepI has largely hindered its industrial and pharmaceutical applications. Loss of bacterial HepI enzyme activity through poor thermostability during its expression and purification process in production can be an important issue. In this study, using a thermostabilization strategy combining site-directed mutagenesis and calcium ion addition during its production markedly improved the yield of maltose-binding protein-fused HepI (MBP-HepI) from recombinant Escherichia coli. Substitution of Cys297 to serine in MBP-HepI offered a 30.6% increase in the recovered total enzyme activity due to a mutation-induced thermostabilizing effect. Furthermore, upon addition of Ca2+ as a stabilizer at optimized concentrations throughout its expression, extraction, and purification process, purified mutant MBP-HepI showed a specific activity of 56.3 IU/mg, 206% higher than that of the wild type obtained without Ca2+ addition, along with a 177% increase in the recovered total enzyme activity. The enzyme obtained through this novel approach also exhibited significantly enhanced thermostability, as indicated by both experimental data and the kinetic modeling. High-yield production of thermostable MBP-HepI using the present system will facilitate its applications in laboratory-scale heparin analysis as well as industrial-scale production of low molecular weight heparin as an improved anticoagulant substitute.

    DOI： 10.1007/s00253-012-4145-6

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  • Gene Analysis, Expression, and Characterization of an Intracellular alpha-Amylase from the Extremely Halophilic Archaeon Haloarcula japonica Reviewed International journal

    Masahiko Onodera, Rie Yatsunami, Wataru Tsukimura, Toshiaki Fukui, Kaoru Nakasone, Tomonori Takashina, Satoshi Nakamura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   77 ( 2 )   281 - 288   2013.2

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    DOI： 10.1271/bbb.120693

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  • Gene expression and characterization of aerotaxis transducer HemAT from extremely halohilic archaeon Haloarcula japonica TR-1 Reviewed

    T. Tadikara, T. Matsubara, Y. Kubota, T. Kosaka, T. Ozawa, W. Tsukimura, R. Yatsunami, T. Fukui, K. Nakasone, T. Takashina, S. Nakamura

    J. Jpn. Soc. Extremophiles   12   29 - 32   2013

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  • Mutational Analysis of a CBM Family 5 Chitin-Binding Domain of an Alkaline Chitinase from Bacillus sp J813 Reviewed International journal

    Fumiya Uni, Sunmi Lee, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   76 ( 3 )   530 - 535   2012.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1271/bbb.110835

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  • Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: implications for a comprehensive thermostabilization strategy. Reviewed International journal

    Shuo Chen, Fengchun Ye, Yang Chen, Yu Chen, Hongxin Zhao, Rie Yatsunami, Satoshi Nakamura, Fumio Arisaka, Xin-Hui Xing

    Biotechnology and bioengineering   108 ( 8 )   1841 - 51   2011.8

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    Enzymatic degradation of heparin by heparin lyases has not only largely facilitated heparin structural analysis and contamination detection, but also showed great potential to be a green and cost-effective way to produce low molecular weight heparin (LMWH). However, the commercial use of heparinase I (HepI), one of the most studied heparin lyases, has been largely hampered by its low productivity and extremely poor thermostability. Here we report the thermal inactivation mechanism and strategic thermal stabilization of maltose-binding protein (MBP)-HepI, a fusion HepI produced in E. coli with high yield, solubility and activity. Biochemical studies demonstrated that the thermal inactivation of MBP-HepI involves an unfolding step that is temperature-dependently reversible, followed by an irreversible dimerization step induced by intermolecular disulfide bonds. A good consistency between the kinetic modeling and experimental data of the inactivation was obtained within a wide range of temperature and enzyme concentration, confirming the adequacy of the proposed inactivation model. Based on the inactivation mechanism, a comprehensive strategy was proposed for the thermal stabilization of MBP-HepI, in which Ca(2+) and Tween 80 were used to inhibit unfolding while site mutation at Cys297 and DTT were employed to suppress dimerization. The engineered enzyme exhibits remarkably improved storage and operational thermostability, for example, 16-fold increase in half-life at its optimum temperature of 30 °C and 8-fold increase in remaining activity of 95% after 1-week storage at 4 °C, and therefore shows great potential as a commercial biocatalyst for heparin degradation in the pharmaceutical industry.

    DOI： 10.1002/bit.23144

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  • A Calcium-Dependent Xylan-Binding Domain of Alkaline Xylanase from Alkaliphilic Bacillus sp Strain 41M-1 Reviewed International journal

    Risa Yazawa, Jun Takakura, Tomoko Sakata, Ihsanawati, Rie Yatsunami, Toshiaki Fukui, Takashi Kumasaka, Nobuo Tanaka, Satoshi Nakamura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   75 ( 2 )   379 - 381   2011.2

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    DOI： 10.1271/bbb.100730

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  • Expression and characterization of a novel glucoamylase from extremely halophilic archaeon Haloarcula japonica

    Kiyohara Mie, Onodera Masahiko, Yatsunami Rie, Fukui Toshiaki, Nakasone Kaoru, Fujita Nobuyuki, Sekine Mitsuo, Takashina Tomonori, Nakamura Satoshi

    Journal of Applied Glycoscience Supplement   2010   38 - 38   2010

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    Language：Japanese   Publisher：The Japanese Society of Applied Glycoscience  

    DOI： 10.11541/jsag.2010.0.38.0

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  • Characterization of a Haloarchaeal GH family 18 Chitinase with Additional Acidic Amino Acids on Its Protein Surface Reviewed

    Y. Zhang, R. An, R. Yatsunami, M. Sato, K. Orishimo, Y. Hatori, T. Fukui, S. Nakamura

    J. Jpn. Soc. Extremophiles   9   72 - 74   2010

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  • Genetic analysis and characterization of an intracellular α-amylase from extremely halophilic archaeon Haloarcula japonica

    Onodera Masahiko, Yatsunami Rie, Fukui Toshiaki, Nakasone Kaoru, Fujita Nobuyuki, Sekine Mitsuo, Takashina Tomonori, Nakamura Satoshi

    Journal of Applied Glycoscience Supplement   2010   37 - 37   2010

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    Language：Japanese   Publisher：The Japanese Society of Applied Glycoscience  

    DOI： 10.11541/jsag.2010.0.37.0

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  • Gene expression and characterization of a novel GH family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum NRC-1 Reviewed

    Yatsunami R, Sato M, Orishimo K, Hatori Y, Zhang Y, Takashina T, Fukui T, Nakamura S

    Journal of Japanese Society for Extremophiles   9 ( 1 )   19 - 24   2010

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    Language：English   Publisher：THE JAPANESE SOCIETY FOR EXTREMOPHILES  

    An open reading frame encoding a chitinase homolog (ChiN1) was found in the genome of extremely halophilic archaeon Halobacterium salinarum NRC-1. ChiN1 is a multidomain enzyme consisting of a chitin-binding domain, a polycystic kidney disease domain and a catalytic domain belonging to glycoside hydrolase family 18. chiN1 gene was successfully expressed in extremely halophilic archaeon Haloarcula japonica TR-1 by employing the promoter sequence of its cell surface glycoprotein gene. A large amount of recombinant ChiN1 was secreted into the culture supernatant. The Ha. japonica-produced ChiN1 was purified and characterized. The optimal pH and temperature of ChiN1 are pH 4.5 and 55°C, respectively. ChiN1 was most active at 1.0 M NaCl and stable over a wide range of NaCl concentration from 1.0 to 4.5 M. This is the first report on a chitinase from extremely halophilic archaeon.

    DOI： 10.3118/jjse.9.19

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    Other Link： https://jlc.jst.go.jp/DN/JALC/00357868582?from=CiNii

  • Additional Carbohydrate-Binding Modules Enhance the Insoluble Substrate-Hydrolytic Activity of beta-1,3-Glucanase from Alkaliphilic Nocardiopsis sp F96 Reviewed International journal

    Naoya Koizumi, Sumiko Masuda, Kiyoe Maeda, Yuya Isoda, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   73 ( 5 )   1078 - 1082   2009.5

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    DOI： 10.1271/bbb.80846

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  • Improvement of Alkaliphily of Bacillus Alkaline Xylanase by Introducing Amino Acid Substitutions Both on Catalytic Cleft and Protein Surface Reviewed International journal

    Hirohito Umemoto, Ihsanawati, Mayuko Inami, Rie Yatsunami, Toshiaki Fukui, Takashi Kumasaka, Nobuo Tanaka, Satoshi Nakamura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   73 ( 4 )   965 - 967   2009.4

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    DOI： 10.1271/bbb.80869

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  • Role of exposed aromatic residues in substrate-binding of CBM family 5 chitin-binding domain of alkaline chitinase. International journal

    Fumiya Uni, Sunmi Lee, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)   ( 53 )   311 - 2   2009

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    Chitinase J (ChiJ) from alkaliphilic Bacillus sp. strain J813 has a multidomain structure containing a catalytic domain (CatD), a fibronectin type III like domain (FnIIID) and a chitin-binding domain (ChBD). It has been shown that the ChBD binds to an insoluble chitin and enhances its degradation by the CatD. Further binding study of the ChBD was performed with a glutathione-S-transferase fusion protein. This fusion protein showed binding abilities to insoluble chitin and chitosan. Two surface-exposed aromatic residues (Trp541 and Trp542) were found in the tertiary-structure model of ChBD and targeted for mutational analysis. Single and double mutations of the two aromatic residues decreased the chitin- and chitosan-binding abilities. It was revealed that these residues would be important for substrate-binding of the ChBD.

    DOI： 10.1093/nass/nrp156

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  • Contribution of salt bridges to alkaliphily of Bacillus alkaline xylanase. International journal

    Hirohito Umemoto, Ihsanawati, Mayuko Inami, Rie Yatsunami, Toshiaki Fukui, Takashi Kumasaka, Nobuo Tanaka, Satoshi Nakamura

    Nucleic acids symposium series (2004)   ( 51 )   461 - 2   2007

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    Xylanase J (XynJ) from alkaliphilic Bacillussp. strain 41M-1 is an alkaline xylanase. Structure comparison indicated that there were several specific salt bridges in the catalytic cleft of XynJ compared with neutral xylanases. Mutant enzymes were prepared by substituting several amino acids comprising the salt bridges. Some mutants exhibited acidophilic shift in optimum pH, whereas another showed alkaliphilic shift. These results suggested that the characteristic salt bridges could contribute to the alkaliphily of XynJ.

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  • Characterization of Nocardiopsis beta-1,3-glucanase with additional carbohydrate-binding domains. International journal

    Naoya Koizumi, Yuya Isoda, Kiyoe Maeda, Sumiko Masuda, Gunter Fibriansah, Takashi Kumasaka, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)   ( 51 )   459 - 60   2007

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    beta-1,3-Glucanase F (BglF) from alkaliphilic Nocardiopsis sp. F96 is a single domain enzyme composed of only a catalytic domain. Chimeric BglFs with some carbohydrate-binding domains were constructed and characterized. By connecting the C-terminal additional domain of beta-1,3-glucanase H from Bacillus circulans IAM1165 and the chitin-binding domain of chitinase J from alkaliphilic Bacillus sp. J813, binding ability and hydrolyzing activity toward insoluble beta-1,3-glucans were both improved.

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  • Functional Improvement of Xylanase by Introducing Mutated Xylan-binding Domain

    Sakata Tomoko, Miyakubo Hiroyuki, Osada Yuko, Wada Rieko, Takahashi Hidenori, Yatsunami Rie, Fukui Toshiaki, Nakamura Satoshi

    Journal of Applied Glycoscience   53 ( 2 )   131 - 136   2006.4

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    Alkaliphilic Bacillus sp. strain 41M-1 secretes a xylanase (termed xylanase J) that has an alkaline pH optimum. Xylanase J is a multidomain enzyme and consists of two functional domains: a glycoside hydrolase family 11 catalytic domain and an additional domain of unknown function. Protein engineering study of xylanase J indicated that the functionally unknown domain should be a xylan-binding domain (XBD) belonging to carbohydrate binding module family 36. The XBD bound to insoluble xylan and enhanced hydrolyzing activity of the adjacent catalytic domain. The XBD was successfully displayed on the surface of filamentous phage. Random mutations were introduced into the XBD gene and the repertoire was cloned for display on phage. Sequencing analysis of the xylan-binding activity-deficient mutants revealed that Phe284, Asp286, Asp313, Trp317 and Asp318 might contribute to the xylan-binding activity of XBD. The mutant XBD with amino acid substitution T316I (Thr317 was replaced by Ile) showed higher xylan-binding activity compared to the wild-type XBD. Furthermore, hydrolyzing activity of xylanase J toward insoluble xylan was improved by introducing mutation T316I.

    DOI： 10.5458/jag.53.131

    DOI： 10.1271/bbb.100730_references_DOI_Yq8iGTz6ThCLdBu4SgY2etvWhvd

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  • Improvement of binding activity of xylan-binding domain by amino acid substitution. International journal

    Tomoko Sakata, Jun Takakura, Hiroyuki Miyakubo, Yuko Osada, Rieko Wada, Hidenori Takahashi, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)   ( 50 )   253 - 4   2006

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    Xylanase J (XynJ) of alkaliphilic Bacillus sp. strain 41M-1 is a multi-domain enzyme and consists of a glycoside hydrolase (GH) family 11 catalytic domain and an additional xylan-binding domain (XBD) belonging to carbohydrate-binding module (CBM) family 36. Random mutations were introduced into the XBD gene and the repertoire was cloned for display on the surface of filamentous phage. The mutant XBD with amino acid substitution T316I (Thr317 was replaced by Ile) showed higher xylan-binding activity compared to the wild-type XBD. Furthermore, hydrolyzing activity of XynJ toward insoluble xylan was also improved by introducing the mutation T316I.

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  • Molecular identification of a novel beta-1,3-glucanase from alkaliphilic Nocardiopsis sp. strain F96. Reviewed International journal

    Sumiko Masuda, Kimiko Endo, Naoya Koizumi, Tokusuke Hayami, Tetsuya Fukazawa, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Extremophiles : life under extreme conditions   10 ( 3 )   251 - 255   2006

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    DOI： 10.1007/s00792-006-0514-3

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  • Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8. Reviewed International journal

    Ihsanawati, Takashi Kumasaka, Tomonori Kaneko, Chihiro Morokuma, Rie Yatsunami, Takao Sato, Satoshi Nakamura, Nobuo Tanaka

    Proteins   61 ( 4 )   999 - 1009   2005.12

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    The crystal structure of xylanase 10B from Thermotoga maritima MSB8 (TmxB), a hyperthermostable xylanase, has been solved in its native form and in complex with xylobiose or xylotriose at 1.8 A resolution. In order to gain insight into the substrate subsite and the molecular features for thermal stability, we compared TmxB with family 10 xylanase structures from nine microorganisms. As expected, TmxB folds into a (beta/alpha)8-barrel structure, which is common among the glycoside hydrolase family 10. The enzyme active site and the environment surrounding the xylooligosaccharide of TmxB are highly similar to those of family 10 xylanases. However, only two xylose moieties were found in its binding pocket from the TmxB-xylotriose complex structure. This finding suggests that TmxB could be a potential biocatalyst for the large-scale production of xylobiose. The result of structural analyses also indicated that TmxB possesses some additional features that account for its thermostability. In particular, clusters of aromatic residues together with a lack of exposed hydrophobic residues are characteristic of the TmxB structure. TmxB has also a significant number of ion pairs on the protein surface that are not found in other thermophilic family 10 xylanases.

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  • Gene cloning, expression and partial characterization of cell division protein FtsZ1 from extremely halophilic archaeon Haloarcula japonica strain TR-1 Reviewed International journal

    K Ozawa, T Harashina, R Yatsunami, S Nakamura

    EXTREMOPHILES   9 ( 4 )   281 - 288   2005.8

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    DOI： 10.1007/s00792-005-0443-6

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  • Molecular cloning of transducer gene hjtB from extremely halophilic archaeon Haloarcula japonica. International journal

    Takayuki Kosaka, Takatoshi Ozawa, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)   ( 49 )   315 - 6   2005

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    A transducer gene, hjtB, was cloned from genomic DNA of extremely halophilic archaeon Haloarcula japonica. The structural gene consisted of an open reading frame of 984 nucleotides encoding 328 amino acids. RT-PCR analysis revealed that this gene was transcribed in Ha. japonica.

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  • Role of an N-terminal domain found in the ferredoxin from extremely halophilic archaeon Haloarcula japonica Reviewed

    N. Hirota, T. Matsuo, A. Ikeda, R. Yatsunami, T. Fukui, S. Nakamura

    J. Jpn. Soc. Extremophiles   4   14 - 24   2005

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  • Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp K17 Reviewed International journal

    W Adachi, Y Sakihama, S Shimizu, T Sunami, T Fukazawa, M Suzuki, R Yatsunami, S Nakamura, A Takenaka

    JOURNAL OF MOLECULAR BIOLOGY   343 ( 3 )   785 - 795   2004.10

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    DOI： 10.1016/j.jmb.2004.08.028

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  • Crystallizations and Preliminary X-ray Analyses of the Active and the Inactive Forms of Family GH-8 Chitosanase with Subclass II Specificity from Bacillus sp. Strain K17 Reviewed International journal

    Y. Sakihama, W. Adachi, S. Shimizu, T. Sunami, T. Fukazawa, M. Suzuki, R. Yatsunami, S. Nakamura, A. Takenaka

    Acta Cryst.,   D60 ( Pt 11 )   2081 - 2083   2004

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    DOI： 10.1107/S0907444902042668

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  • A novel bacteriorhodopsin-like protein from Haloarcula japonica strain TR-1: Gene cloning, squencing and transcript analysis Reviewed

    R. Yatsunami, T. Kawakami, H. Ohtani, S. Nakamura

    Extremophiles   4   109-144 - 144   2000

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Books

  • ビギナーのための微生物実験ラボガイド : microbiological experiment

    中村, 聡, 中島, 春紫, 伊藤, 政博, 道久, 則之, 八波, 利恵

    講談社  2019.5  （ ISBN:9784065135990 ）

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  • 好塩菌に備わった分子ポンプ

    化学装置  2003 

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  • 生体分子と自己修復

    化学と教育  2001 

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  • クジラ DNA に刻まれた生命の起源

    化学と工業  1998 

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  • SINE 配列に学ぶ生命の進化

    化学と生物  1998 

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MISC

  • 高度好塩性古細菌Haloarcula japonica由来走気性トランスデューサーの親株における発現と機能解析—Expression and Functional Analysis of Aerotaxis Transducers from Extremely Halophilic Archaeon Haloarcula japonica

    田力 鉄平, 松原 惇高, 久保田 芳弘, 小坂 貴幸, 小澤 孝俊, 八波 利恵, 福居 俊昭, 中村 聡

    沼津工業高等専門学校研究報告 National Institute of Technology Numazu College research annual   ( 56 )   1 - 6   2022.2

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  • 好アルカリ性Bacillus sp. J813株由来アルカリキチナーゼの指向性進化による比活性の向上—Improvement of Specific Activity of an Alkaline Chitinase from Alkaliphilic Bacillus sp. J813 by Directed Evolution

    齋藤 圭祐, 宇仁 文哉, 渡部 俊樹, 深沢 徹也, 長尾 由里, 三瓶 全次郎, 大竹 潤, 八波 利恵, 福居 俊昭, 中村 聡

    沼津工業高等専門学校研究報告 National Institute of Technology Numazu College research annual   ( 55 )   1 - 5   2021.1

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  • Characterization of GH family 18 chitinases ChiF1 and ChiF3 from alkaliphilic actinomycete Nocardiopsis sp. F96

    遠山絹華, 三須大樹, 梶谷嶺, 遠藤きみ子, 深沢徹也, 八波利恵, 伊藤武彦, 福居俊昭, 中村聡

    キチン・キトサン研究   22 ( 2 )   2016

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  • 古細菌のカロテノイド生合成経路

    93 ( 7 )   394 - 396   2015

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  • 極限環境微生物が合成するカロテノイド : バクテリオルベリン(バイオミディア)

    八波,利恵

    生物工学会誌 : Seibutsu-kogaku Kaishi   90 ( 11 )   738   2012.11

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  • Directed evolution of a GH family 18 alkaline chitinase : establishment of high-throughput screening system and characterization of mutant enzymes

    SAITO K., UNI F., ZHU Leilei, YATSUNAMI R., FUKUI T., SCHWANEBERG Ulrich, NAKAMURA S.

    18 ( 2 )   136 - 137   2012.7

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  • 極限環境微生物学会研究奨励賞受賞研究 高度好塩性古細菌に由来する機能性タンパク質の解析—Analysis of Functional Proteins from Extremely Halophilic Archaea

    八波 利恵

    極限環境生物学会誌 = Journal of Japanese Society for Extremophiles   10 ( 1 )   17 - 22   2011.9

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  • Transglycosylation activity of intracellular starch-active enzyme MalA from extremely halophilic archaeon Haloarcula japonica

    Onodera Masahiko, Yatsunami Rie, Fukui Toshiaki, Nakasone Kaoru, Fujita Nobuyuki, Sekine Mitsuo, Takashina Tomonori, Nakamura Satoshi

    Journal of Applied Glycoscience Supplement   2011   56 - 56   2011

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    Language：Japanese   Publisher：The Japanese Society of Applied Glycoscience  

    DOI： 10.11541/jsag.2011.0.56.0

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  • キチン質分解酵素の抗真菌活性に及ぼすキチン結合ドメイン付加の効果

    山本公隆, 前田聖恵, 小泉直也, 中峯由香子, 崎濱由梨, 深沢徹也, 八波利恵, 福居俊昭, 中村聡

    日本農芸化学会関東支部講演要旨集   2011 ( Oct )   2011

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  • Characterization of CBM family 5 chitin-binding domain mutants

    UNI Fumiya, LEE Sunmi, YATSUNAMI Rie, FUKUI Toshiaki, NAKAMURA Satoshi

    16 ( 2 )   200 - 200   2010.6

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  • Substrate specificity of loop-modified mutants of GH family 8 chitosanase from Bacillus sp. K17

    NAKAMINE Yukako, SAKIHAMA Yuri, SUZUKI Mamie, FUKAZAWA Tetsuya, YATSUNAMI Rie, FUKUI Toshiaki, TAKENAKA Akio, NAKAMURA Satoshi

    キチン・キトサン研究   16 ( 2 )   172 - 173   2010.6

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  • Analysis of Functional Domains and Improvement of Alkaliphily of an Alkaline Xylanase on the Basis of Its Three-dimensional Structure

    Umemoto Hirohito, Yazawa Risa, Takakura Jun, Yatsunami Rie, Fukui Toshiaki, Nakamura Satoshi

    Journal of Applied Glycoscience   57 ( 2 )   145 - 150   2010

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    Language：English   Publisher：The Japanese Society of Applied Glycoscience  

    Xylanase J (XynJ) from alkaliphilic Bacillus sp. strain 41M-1 is a multi-domain enzyme consisting of a glycoside hydrolase (GH) family 11 catalytic domain and a carbohydrate-binding module family 36 xylan-binding domain (XBD). Structural comparison of the GH family 11 catalytic domains indicated that there were several specific salt bridges in the catalytic cleft of XynJ. Mutant enzymes were prepared by substituting several amino acid residues responsible for the characteristic salt bridges. Elimination of the salt bridges caused an acidophilic shift in optimum pH, suggesting that the characteristic salt bridges contributed to the alkaliphily of XynJ. On the other hand, reinforcing one of the characteristic salt bridges in the catalytic domain shifted the optimum pH of XynJ from 8.5 to 9.0. Furthermore, introducing excess Arg residues on the protein surface was also effective to improve the alkaliphily of XynJ. Xylan-binding properties of various XBD mutants were investigated as fusion proteins with glutathione-S-transferase. Furthermore, the same substitutions were introduced into the XBD region of XynJ and insoluble xylan-hydrolyzing activity was measured. The results indicated that some Asp, Trp and Tyr residues were important for xylan-binding activity of the XBD, and that xylan-hydrolyzing activity of XynJ was closely correlated to xylan-binding activity of the XBD region.

    DOI： 10.5458/jag.57.145

    DOI： 10.5458/jag.jag.jag-2011_001_references_DOI_GDe00KHSKuS7qpbDxmR6q3DIDpR

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  • Extracellular secretion mechanism in Escherichia coli of a recombinant GH family 18 chitinase from alkaliphilic Nocardiopsis sp. F96 : role of signal peptide and mature polypeptide region

    ISHIDA Shunsei, KANG Fei, MATSUSHIMA Junya, ENDO Kimiko, MORIGUCHI Manabu, FUKAZAWA Tetsuya, YATSUNAMI Rie, FUKUI Toshiaki, KUMASAKA Takashi, TANAKA Nobuo, NAKAMURA Satoshi

    15 ( 2 )   110 - 111   2009.7

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  • Role of surface amino acids on halotolerancy of GH family 18 chitinase from Halobacterium salinarum NRC-1

    YATSUNAMI R., ZHANG Y., HATORI Y., SATO M., ORISHIMO K., FUKUI T., NAKAMURA S.

    15 ( 2 )   108 - 109   2009.7

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  • バシラス属細菌由来キトサナーゼのループ領域改変に基づく基質特異性の変換

    中峯由香子, 崎濱由梨, 鈴木麻美絵, 深沢徹也, 八波利恵, 福居俊昭, 竹中章郎, 中村聡

    触媒討論会討論会A予稿集   104th   2009

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  • Characterization of Nocardiopsis GH Family 18 Chitinase with Additional CBM Family 5 Chitin-binding Domains

    MAEDA K., KOIZUMI N., ENDO K., FUKAZAWA T., YATSUNAMI R., FUKUI T., NAKAMURA S.

    14 ( 2 )   231 - 231   2008.7

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  • Surface Charge Alteration of Family 8/subclass II Chitosanase from Bacillus sp. Strain K17

    NAKAMINE Y., ZHANG Y., SAKIHAMA Y., SUZUKI M., FUKAZAWA T., ADACHI W., YATSUNAMI R., FUKUI T., TAKENAKA A., NAKAMURA S.

    キチン・キトサン研究   14 ( 2 )   232   2008.7

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  • バシラス属細菌由来キトサナーゼの活性に及ぼす表面電荷の改変および基質結合ドメイン付加の影響

    中峯由香子, 前田聖恵, 小泉直也, 張楊, 崎濱由梨, 深沢徹也, 八波利恵, 福居俊昭, 中村聡

    触媒討論会討論会A予稿集   102nd   2008

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  • Characterization of Nocardiopsis family 18 chitinase with additional chitin-binding domain

    MAEDA K., KOIZUMI N., ENDO K., FUKAZAWA T., YATSUNAMI R., FUKUI T., NAKAMURA S.

    13 ( 2 )   194 - 194   2007.8

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  • Identification of subsites in family 8/subclass II chitosanase from Bacillus sp. strain K17

    NAKAMINE Y., SAKIHAMA Y., SUZUKI M., FUKAZAWA T., ADACHI W., YATSUNAMI R., FUKUI T., TAKENAKA A., NAKAMURA S.

    キチン・キトサン研究   13 ( 2 )   192   2007.8

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  • Influence of organic solvents on transglycosylation activity of Haloarchaeal chitinase

    YATSUNAMI R., HATORI Y., ZHANG Y., SATO M., ORISHIMO K., FUKUI T., NAKAMURA S.

    13 ( 2 )   154 - 155   2007.8

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  • Creation of a tissue culture matrix using functional domains of chitinase

    FUKAGAWA Satoko, SAMPEI Zenjiro, NAGAO Yuri, MATSUO Takatoshi, FUKAZAWA Tetsuya, ENDO Kimiko, YATSUNAMI Rie, FUKUI Toshiaki, NAKAMURA Satoshi

    12 ( 2 )   106 - 107   2006.7

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  • Characterization of Chimeric Family 18 Chitinase from Alkaliphilic Bacillus sp. Strain J813 by Domain Shuffling

    OTAKE H., SAMPEI Z., NAGAO Y., SAKIHAMA Y., FUKAZAWA T., FUKAGAWA S., ENDO K., YATSUNAMI R., FUKUI T., NAKAMURA S.

    キチン・キトサン研究   12 ( 2 )   202   2006.7

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  • Characterization of Recombinant Family 18 Chitinase from Extremely Halophilic Archaeon Halobacterium salinarum Strain NRC-1

    HATORI Y., SATO M., ORISHIMO K., YATSUNAMI R., ENDO K., FUKUI T., NAKAMURA S.

    12 ( 2 )   201 - 201   2006.7

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  • Functional analysis of the signal peptide of chitinase F1 from alkaliphilic Nocardiopsis sp. strain F96

    YATSUNAMI Rie, MATSUSHIMA Junya, ENDO Kimiko, MORIGUCHI Manabu, FUKAZAWA Tetsuya, FUKUI Toshiaki, MATSUI Tsutomu, SATO Takao, KUMASAKA Takashi, TANAKA Nobuo, NAKAMURA Satoshi

    12 ( 2 )   108 - 109   2006.7

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  • 好アルカリ性バシラス属細菌キチナーゼのドメインシャフリングと変異型酵素の性質検討

    大竹潤, 三瓶全次郎, 長尾由里, 崎濱由梨, 深沢徹也, 深川聡子, 遠藤きみ子, 八波利恵, 福居俊昭, 中村聡

    酵素工学研究会講演会講演要旨集   56th   2006

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  • Functional Analysis of a Family 8/Subclass II Chitosanase from Bacillus sp. Strain K17

    SAKIHAMA Y., SUZUKI M., FUKAZAWA T., ENDO K., YATSUNAMI R., FUKUI T., ADACHI W., SHIMIZU S., SUNAMI T., TSUNODA M., TAKENAKA A., NAKAMURA S.

    11 ( 2 )   102 - 103   2005.7

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  • Application of Chitin-Binding Domain of Chitinase J from Alkaliphilic Bacillus sp. Strain J813 to Tissue Culture Matrix

    FUKAGAWA S., SAMPEI Z., NAGAO Y., MATSUO T., FUKAZAWA T., ENDO K., YATSUNAMI R., FUKUI T., NAKAMURA S.

    11 ( 2 )   217 - 217   2005.7

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  • Catalytic Mechanism of Family 18 Chitinase from Alkaliphilic Nocardiopsis sp. Strain F96 and Its Extracellular Secretion in Escherichia coli

    MATSUSHIMA J., ENDO K., MORIGUCHI M., FUKAZAWA T., YATSUNAMI R., FUKUI T., MATSUI T., SATO T., KUMASAKA T., TANAKA N., NAKAMURA S.

    11 ( 2 )   218 - 218   2005.7

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  • Mutational Analysis of a Family 18 Chitinase from Alkaliphilic Bacillus sp. J813 : Characterization of Mutant with Additional Acidic Amino Acids

    OTAKE H., SAMPEI Z., NAGAO Y., SAKIHAMA Y., FUKAZAWA T., FUKAGAWA S., ENDO K., YATSUNAMI R., FUKUI T., NAKAMURA S.

    11 ( 2 )   219 - 219   2005.7

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  • Analysis of Functional Domains of a Family 18 Chitinase from Extremely Halophilic Archaeon Halobacterium sp. Strain NRC-1

    HATORI Y., SATO M., ORISHIMO K., YATSUNAMI R., ENDO K., FUKUI T., NAKAMURA S.

    11 ( 2 )   220 - 220   2005.7

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  • Analysis of Functional Domains of Chitinase J from Alkaliphilic Bacillus sp. Strain J813

    SAMPEI Z., NAGAO Y., FUKAZAWA T., FUKAGAWA S., MATSUO T., ENDO K., YATSUNAMI R., NAKAMURA S.

    10 ( 2 )   114 - 115   2004.7

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  • Characterization of Haloarchaeal Chitinase from Halobacterium sp. NRC-1 Produced by Haloacrula japonica

    YATSUNAMI R., SATO M., ORISHIMO K., ENDO K., NAKAMURA S.

    10 ( 2 )   108 - 109   2004.7

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  • Gene Cloning and Deletion Analysis of Chitinase J from Alkaliphilic Bacillus sp. Strain J813 International journal

    Rie Yatsunami

    Nucleic Acids Symp. Ser.,   48 ( 48 )   167 - 168   2004

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    Alkaliphilic Bacillus sp. strain J813 produces a novel chitinase (chitinase J). The gene encoding chitinase J (chij) was cloned and sequenced. Deduced amino acid sequence revealed that Chij contained a family 18 catalytic domain, a fibronectin type III-like domain and a chitin-binding domain. Analysis of deletion derivatives indicated that the chitin-binding domain was important for binding to chitin and it enhanced the hydrolysis of insoluble chitin. The subsites existing in the catalytic domain of Chij was thought to bind to insoluble chitosan, although Chij did not hydrolyze chitosan. Some amino acid-substituted mutants were prepared and characterized, suggesting that Glu198 should be the catalytic residue of Chij.

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  • Molecular cloning of a chitinase gene from newly isolated alkaliphilic Nocardiopsis sp. strain F96

    Kimiko Endo, Tetsuya Fukazawa Rie Yatsunami, Satoshi Nakamura

    Extremophiles   2004

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  • Various Chitosanase Developed from Different Structural Kingdoms

    Rie Yatsunami

    Chitin Chitosan Res.,   2004

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  • Isolation of crtI Homolog from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    R. Yatsunami, S. Takaichi, S. Nakamura

    Nucleic Acids Symp. Ser.,   48   193 - 194   2004

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  • Molecular Cloning of Transducer Genes hjtA and hjtC from Extremely Halophilic Archaeon <I>Haloarcula japonica<I>

    Rie Yatsunami

    Nucleic Acids Symp. Ser.,   48   169 - 170   2004

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  • Gene Cloning and Deletion Analysis of Chitinase J from Alkaliphilic Bacillus sp. Strain J813

    Rie Yatsunami

    Nucleic Acids Symp. Ser.,   48   167 - 168   2004

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  • Various Chitosanase Developed from Different Structural Kingdoms

    Rie Yatsunami

    Chitin Chitosan Res.,   2004

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  • Isolation of crtI Homolog from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1 International journal

    R. Yatsunami, S. Takaichi, S. Nakamura

    Nucleic Acids Symp. Ser.,   48 ( 48 )   193 - 194   2004

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    Halobacterium sp. strain NRC-1 possesses phytoene dehydrogenase genes (crtIs). A crtI2 homolog was cloned from Haloarcula japonica strain TR-1. Nucleotide sequencing analysis of the possible crtI2 revealed that the structural gene consisted of an open reading frame of 1,521 nucleotides encoding 507 amino acids. Transcription of crtI2 in Ha. japonica was confirmed by RT-PCR.

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  • Molecular Cloning of Transducer Genes hjtA and hjtC from Extremely Halophilic Archaeon <I>Haloarcula japonica<I> International journal

    Rie Yatsunami

    Nucleic Acids Symp. Ser.,   48 ( 48 )   169 - 170   2004

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    Language：English  

    The genes encoding putative taxis transducers hjtA and hjtC were cloned from triangular disc-shaped extremely halophilic archaeon Haloarcula japonica strain TR-1. Nucleotide sequencing analysis revealed that HjtA and HjtC consisted of 438 and 630 amino acids, respectively. HjtA and HjtC have the highly conserved sequence which is commonly found in signaling domains of bacterial and archaeal transducers.

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  • Molecular cloning of a family 18 chitinase gene from alkaliphilic Nocardiopsis sp. strain F96

    ENDO Kimiko, FUKAZAWA Tetsuya, YATSUNAMI Rie, NAKAMURA Satoshi

    Extremophiles   9 ( 2 )   150 - 151   2003.6

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  • 好塩菌に備わった分子ポンプ—特集1 バイオと化学産業の接点 ; 第2章 バイオマテリアル

    八波 利恵, 中村 聡

    化学装置   45 ( 4 )   66 - 68   2003.4

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  • Directed evolution of xylanase J from alkaliphilic Bacillus sp. strain 41M-1: restore of alkaliphiliy of a mutant with an acidic pH optimum International journal

    M. Inami, C. Morokuma, A. Sugio, H. Tamanoi, R, Yatsunami, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   315 - 316   2003

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    Alkaliphilic Bacillus sp. strain 41M-1 produces an alkaliphilic xylanase (xylanase J). The newly constructed mutant E177Q deltaJC had an acidic pH optimum and showed almost no activity at pH 8.0. The alkaliphily of the enzyme was restored by directed evolution. The evolved mutants, Y176S/E177Q deltaJC and G32V/Y176D/E177Q deltaJC, retained about 30% and 43% activity of their maximal activities at pH 6.0, respectively.

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  • Cloning and expression of bglF gene from alkaliphilic Nocardiopsis sp. strain F96 International journal

    S. Masuda, K. Endo T, Hayami T, Fukazawa R, Yatsunami, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   317 - 318   2003

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    The gene encoding a novel beta-1,3-glucanase was cloned from alkaliphilic Nocardiopsis sp. F96 and sequenced. The gene contained an open reading frame of 936 bp. The deduced amino acid sequence of the beta-1,3-glucanase exhibited highest homology to those of family 16 glucanases, suggesting that the enzyme belonged to family 16. The beta-1,3-glucanase gene was functionally expressed in Escherichia coli.

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  • A brp homolog of Haloarcula japonica : gene cloning and transcriptional analysis

    R. Yatsunami, M. Iwamoto, S. Ito, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   267 - 268   2003

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  • Gene cloning of ftsZ homolog from extremely halophilic archaeon Haloarcula japonica

    K. Ozawa, R, Yatsunami, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   313 - 314   2003

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  • Directed evolution of xylanase J from alkaliphilic Bacillus sp. strain 41M-1: restore of alkaliphiliy of a mutant with an acidic pH optimum

    M. Inami, C. Morokuma, A. Sugio, H. Tamanoi, R, Yatsunami, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   315 - 316   2003

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  • Cloning and expression of bglF gene from alkaliphilic Nocardiopsis sp. strain F96

    S. Masuda, K. Endo T, Hayami T, Fukazawa R, Yatsunami, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   317 - 318   2003

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  • A brp homolog of Haloarcula japonica : gene cloning and transcriptional analysis International journal

    R. Yatsunami, M. Iwamoto, S. Ito, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   267 - 268   2003

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    The gene encoding a homolog of Halobacterium salinarum bacterioopsin-related protein (Brp) was cloned from Haloarcula japonica strain TR-1. Nucleotide sequencing analysis of the possible brp gene revealed that the structural gene consisted of an open reading frame of 1,062 nucleotides encoding 354 amino acids. Transcription of the brp homolog in Ha. japonica was confirmed by RT-PCR.

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  • Gene cloning of ftsZ homolog from extremely halophilic archaeon Haloarcula japonica International journal

    K. Ozawa, R, Yatsunami, S. Nakamura

    Nucleic Acid Res. Suppl.   ( 3 )   313 - 314   2003

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    The gene encoding FtsZ1 was cloned from triangular disc-shaped extremely halophilic archaeon Haloarcula japonica strain TR-1. Nucleotide sequencing analysis of the possible ftsZ1 gene revealed that the structural gene consisted of an open reading frame of 1,038 nucleotides encoding 346 amino acids. Transcription of the ftsZ1 gene in Ha. japonica was confirmed by RT-PCR.

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  • A Novel Chitosanase from Bacillus sp. Strain K17: Gene Cloning and Expression in Escherichia coil. International journal

    R. Yatsunami, Y. Sakihama, M, Suzuki T. Fukazawa, S. Shimizu, T. Sunami, K. Endo, A. Takenaka, S. Nakamura

    Nucleic Acids Res. Suppl   2 ( 2 )   227 - 228   2002

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    The gene encoding a novel chitosanase from Bacillus sp. strain K17 was cloned and sequenced. The nucleotide sequence of the gene contained an open reading frame corresponded to a protein of 453 amino acids. The deduced amino acid sequence of the K17 chitosanase exhibited the highest homology to those of family 8 glycanases, suggesting that the enzyme belonged to family 8.

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  • A novel chitosanase from Bacillus sp. strain K17: gene cloning and expression in Escherichia coli. International journal

    Rie Yatsunami, Yuri Sakihama, Mamie Suzuki, Tetsuya Fukazawa, Shinji Shimizu, Tomoko Sunami, Kimiko Endo, Akio Takénaka, Satoshi Nakamura

    Nucleic acids research. Supplement (2001)   2 ( 2 )   227 - 228   2002

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    The gene encoding a novel chitosanase from Bacillus sp. strain K17 was cloned and sequenced. The nucleotide sequence of the gene contained an open reading frame corresponded to a protein of 453 amino acids. The deduced amino acid sequence of the K17 chitosanase exhibited the highest homology to those of family 8 glycanases, suggesting that the enzyme belonged to family 8.

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  • Cloning and sequencing of a chitosanase gene from Bacillus sp. strain K17

    SUZUKI Mamie, FUKAZAWA Tetsuya, YATSUNAMI Rie, NAGATOMO Kentaro, ENDO Kimiko, NAKAMURA Satoshi

    7 ( 2 )   156 - 157   2001.7

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  • 生体内分子と自己修復

    YATSUNAMI Rie, NAKAMURA Satoshi

    CHEMISTRY & EDUCATION   49 ( 3 )   122 - 125   2001

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    Language：Japanese   Publisher：The Chemical Society of Japan  

    DOI： 10.20665/kakyoshi.49.3_122

    CiNii Books

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  • Gene Clusters Encoding ATP synthase of Haloarcula japonica Strain TR-1

    R. Yatsunami, M. Iwamoto, K. Ihara, S. Nakamura

    Nucleic Acids Res. Suppl   1   51 - 52   2001

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  • Gene Clusters Encoding ATP synthase of Haloarcula japonica Strain TR-1

    R. Yatsunami, M. Iwamoto, K. Ihara, S. Nakamura

    Nucleic Acids Res. Suppl   1   51 - 52   2001

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  • The Gene Encoding a Novel Halorhodopsin-like Protein of Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    R. Yatsunami, S. Aono, S. Nakamura

    Nucleic Acids Symp. Ser.   44   1 - 2   2000

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  • A Novel Bacterio-Rhodopsin like Protein from Haloarcula japonica Strain TR-1: Gene Cloning, Sequencing and Transcript Analysis

    R. Yatsunami, T. Kawakami, H. Ohtani, S. Nakamura

    Extremophiles   4 ( 2 )   109 - 114   2000

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  • Cloning and Sequencing of ftsZ Homolog from Extermely Halophilic Archaeon Haloarcula japonica Strain TR-1

    Rie Yatsunami

    Nucleic Acids Symp. Ser.   44   155 - 156   2000

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  • The Gene Encoding a Novel Halorhodopsin-like Protein of Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    R. Yatsunami, S. Aono, S. Nakamura

    Nucleic Acids Symp. Ser.   44   1 - 2   2000

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  • Cloning and Sequencing of ftsZ Homolog from Extermely Halophilic Archaeon Haloarcula japonica Strain TR-1

    Rie Yatsunami

    Nucleic Acids Symp. Ser.   44   155 - 156   2000

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  • Molocular Cloning of A1-ATPase Gene from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    Rie Yatsunami

    Nucleic Acids Symp. Ser.   42   75 - 76   1999

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  • Transcriptional Regulation of Cruxrhodopsin Gene from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    R. Yatsunami, T. Kawakami, H. Ohtani, S. Nakamura

    Nucleic Acids Symp. Ser.   42   73 - 74   1999

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  • Molocular Cloning of A1-ATPase Gene from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    Rie Yatsunami

    Nucleic Acids Symp. Ser.   42   75 - 76   1999

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  • Transcriptional Regulation of Cruxrhodopsin Gene from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    R. Yatsunami, T. Kawakami, H. Ohtani, S. Nakamura

    Nucleic Acids Symp. Ser.   42   73 - 74   1999

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  • クジラDNAに刻まれた生命の起源

    八波 利恵

    化学と工業 = Chemistry and chemical industry   51 ( 6 )   918   1998.6

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  • Evolution of life learned from the SINE sequence.

    KAGAKU TO SEIBUTSU   36 ( 8 )   523 - 524   1998

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    Language：Japanese   Publisher：Japan Society for Bioscience, Biotechnology, and Agrochemistry  

    DOI： 10.1271/kagakutoseibutsu1962.36.523

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  • Primary Structure of the Novel Bacterial Rhodopsin from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    Rie Yatsunami

    Nucleic Acids Symp. Ser.   37   111 - 112   1997

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  • Primary Structure of the Novel Bacterial Rhodopsin from Extremely Halophilic Archaeon Haloarcula japonica Strain TR-1

    Rie Yatsunami

    Nucleic Acids Symp. Ser.   37   111 - 112   1997

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Presentations

  • Genetic analysis and characterization of an intracellular α-amylase from extremely halophilic archaeon Haloarcula japonica

    Onodera Masahiko, Yatsunami Rie, Fukui Toshiaki, Nakasone Kaoru, Fujita Nobuyuki, Sekine Mitsuo, Takashina Tomonori, Nakamura Satoshi

    Journal of Applied Glycoscience Supplement  2010  The Japanese Society of Applied Glycoscience

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    Event date： 2010

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  • Role of exposed aromatic residues in substrate-binding of CBM family 5 chitin-binding domain of alkaline chitinase.

    Fumiya Uni, Sunmi Lee, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)  2009 

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    Event date： 2009

    Language：English  

    Chitinase J (ChiJ) from alkaliphilic Bacillus sp. strain J813 has a multidomain structure containing a catalytic domain (CatD), a fibronectin type III like domain (FnIIID) and a chitin-binding domain (ChBD). It has been shown that the ChBD binds to an insoluble chitin and enhances its degradation by the CatD. Further binding study of the ChBD was performed with a glutathione-S-transferase fusion protein. This fusion protein showed binding abilities to insoluble chitin and chitosan. Two surface-exposed aromatic residues (Trp541 and Trp542) were found in the tertiary-structure model of ChBD and targeted for mutational analysis. Single and double mutations of the two aromatic residues decreased the chitin- and chitosan-binding abilities. It was revealed that these residues would be important for substrate-binding of the ChBD.

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  • Analysis of functional domains and improvement of alkaliphily of an alkaline xylanase on the basis of its three-dimensional structure

    Umemoto Hirohito, Yazawa Risa, Takakura Jun, Yatsunami Rie, Fukui Toshiaki, Nakamura Satoshi

    Journal of Applied Glycoscience Supplement  2009  The Japanese Society of Applied Glycoscience

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    Event date： 2009

    Language：Japanese  

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  • Improvement of alkaliphily of GH family 11 xylanase by modifying electrorical charge of protein surface

    Umemoto Hirohito, Yatsunami Rie, Fukui Toshiaki, Nakamura Satoshi

    Proceeding of Annual/Fall Meetings of the Japan Petroleum Institute  2009  The Japan Petroleum Institute

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    Event date： 2009

    Language：Japanese  

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  • Characterization of Nocardiopsis beta-1,3-glucanase with additional carbohydrate-binding domains.

    Naoya Koizumi, Yuya Isoda, Kiyoe Maeda, Sumiko Masuda, Gunter Fibriansah, Takashi Kumasaka, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)  2007 

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    Event date： 2007

    Language：English  

    beta-1,3-Glucanase F (BglF) from alkaliphilic Nocardiopsis sp. F96 is a single domain enzyme composed of only a catalytic domain. Chimeric BglFs with some carbohydrate-binding domains were constructed and characterized. By connecting the C-terminal additional domain of beta-1,3-glucanase H from Bacillus circulans IAM1165 and the chitin-binding domain of chitinase J from alkaliphilic Bacillus sp. J813, binding ability and hydrolyzing activity toward insoluble beta-1,3-glucans were both improved.

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  • Characterization of domain-shuffled and/or amino-acid-substituted beta-1,3-glucanase from alkaliphilic actinomycete

    Koizumi Naoya, Maeda Kiyoe, Isoda Yuya, Masuda Sumiko, Fibriansah Guntur, Kumasaka Takashi, Yatsunami Rie, Fukui Toshiaki, Nakamura Satoshi

    Proceeding of Annual/Fall Meetings of the Japan Petroleum Institute  2007  The Japan Petroleum Institute

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    Event date： 2007

    Language：Japanese  

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  • Contribution of salt bridges to alkaliphily of Bacillus alkaline xylanase.

    Hirohito Umemoto, Ihsanawati, Mayuko Inami, Rie Yatsunami, Toshiaki Fukui, Takashi Kumasaka, Nobuo Tanaka, Satoshi Nakamura

    Nucleic acids symposium series (2004)  2007 

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    Event date： 2007

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    Xylanase J (XynJ) from alkaliphilic Bacillussp. strain 41M-1 is an alkaline xylanase. Structure comparison indicated that there were several specific salt bridges in the catalytic cleft of XynJ compared with neutral xylanases. Mutant enzymes were prepared by substituting several amino acids comprising the salt bridges. Some mutants exhibited acidophilic shift in optimum pH, whereas another showed alkaliphilic shift. These results suggested that the characteristic salt bridges could contribute to the alkaliphily of XynJ.

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  • Improvement of binding activity of xylan-binding domain by amino acid substitution.

    Tomoko Sakata, Jun Takakura, Hiroyuki Miyakubo, Yuko Osada, Rieko Wada, Hidenori Takahashi, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)  2006 

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    Event date： 2006

    Language：English  

    Xylanase J (XynJ) of alkaliphilic Bacillus sp. strain 41M-1 is a multi-domain enzyme and consists of a glycoside hydrolase (GH) family 11 catalytic domain and an additional xylan-binding domain (XBD) belonging to carbohydrate-binding module (CBM) family 36. Random mutations were introduced into the XBD gene and the repertoire was cloned for display on the surface of filamentous phage. The mutant XBD with amino acid substitution T316I (Thr317 was replaced by Ile) showed higher xylan-binding activity compared to the wild-type XBD. Furthermore, hydrolyzing activity of XynJ toward insoluble xylan was also improved by introducing the mutation T316I.

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  • Molecular cloning of transducer gene hjtB from extremely halophilic archaeon Haloarcula japonica.

    Takayuki Kosaka, Takatoshi Ozawa, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

    Nucleic acids symposium series (2004)  2005 

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    Event date： 2005

    Language：English  

    A transducer gene, hjtB, was cloned from genomic DNA of extremely halophilic archaeon Haloarcula japonica. The structural gene consisted of an open reading frame of 984 nucleotides encoding 328 amino acids. RT-PCR analysis revealed that this gene was transcribed in Ha. japonica.

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Awards

  • 2023年度農芸化学女性研究者賞

    2023.3   日本農芸化学会   極限環境微生物が生産する極限酵素の機能解明とその応用

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  • 極限環境生物学会研究奨励賞

    2010.11   極限環境生物学会   高度好塩性古細菌に由来する機能性タンパク質の解析

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  • 優秀講演賞

    2009.9   日本化学会第3回関東支部大会優秀講演賞   高度好塩性古細菌由来キチナーゼの酸性アミノ酸分布と耐塩性との相関

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  • 手島記念研究賞博士論文賞

    2001.3   東京工業大学   高度好塩性古細菌 Haloarcula japonicaに由来するクルックスロドプシン

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    Country：Japan

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  • 鎌田泉博士論文賞

    2000.3   東京工業大学   高度好塩性古細菌 Haloarcula japonicaに由来するクルックスロドプシン

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    Country：Japan

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Research Projects

  • Tag-based reinforcement of proteins and enzymes

    Grant number：24K21231  2024.6 - 2027.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Challenging Research (Pioneering)

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    Grant amount：\25870000 （ Direct Cost: \19900000 、 Indirect Cost：\5970000 ）

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  • 海洋漂着プラスチックをエコフレンドリーな方法で分解する新技術の開発

    Grant number：24K08678  2024.4 - 2027.3

    日本学術振興会  科学研究費助成事業  基盤研究(C)

    八波 利恵

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    Grant amount：\4550000 （ Direct Cost: \3500000 、 Indirect Cost：\1050000 ）

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  • Design of carotenoid production plant: Large scale synthesis of various carotenoids by extremely halophilic archaea

    Grant number：16K06868  2016.4 - 2020.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    Yatsunami Rie

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    Grant amount：\4810000 （ Direct Cost: \3700000 、 Indirect Cost：\1110000 ）

    The purpose of this study was to synthesize a large amount of a novel carotenoid with high antioxidant activity by extremely halophilic archaeon Haloarcula japonica.
    In order to synthesize carotenoids with more antioxidant activity, we aimed to synthesize tetradehydrolycopene with 15 conjugated double bonds. For its synthesis, carotenoid desaturase (CrtD) was mutated by the directed evolution. Analysis of the mutated CrtD gene library revealed amino acid residues important for lycopene synthesis.

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  • Producing of supercritical carbon dioxide-tolerant enzyme based on halo-tolerant enzyme and syntheses of chitin oligosaccharide

    Grant number：23550177  2011.4 - 2015.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    YATSUNAMI Rie

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    Grant amount：\5070000 （ Direct Cost: \3900000 、 Indirect Cost：\1170000 ）

    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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  • 高度好塩性古細菌キチナーゼの耐塩機構の解明と有機溶媒中での新規オリゴ糖創製

    Grant number：16760630  2004 - 2005

    日本学術振興会  科学研究費助成事業  若手研究(B)

    八波 利恵

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    Grant amount：\3600000 （ Direct Cost: \3600000 ）

    既にゲノム解析により、高度好塩性古細菌Halobacterium sp. NRC-1株にはキチナーゼホモログをコードする遺伝子が存在することが報告されているが、タンパク質としての実態は明らかにされていない。本研究ではNRC-1株キチナーゼの酵素学的性質、耐塩機構の解明および工学応用を目指した研究を行った。以下1および2に実績の概要を示す。
    1.Haloarcula japonicaにおけるキチナーゼ遺伝子の発現と組換え型キチナーゼの精製
    高度好塩性古細菌用キチナーゼ遺伝子発現型プラスミドを構築し、発現型プラスミドを導入したH.japonica形質転換体より、培養上清を回収した。次に限外ろ過濃縮した後、ヒドロキシアパタイト・カラムクロマトグラフィーを行い、組換え型キチナーゼの精製を実施した。その結果、分子質量約70kDaの位置に単一バンドを示す精製標品が得られた。
    2.組換え型キチナーゼの性質検討
    組換え型キチナーゼ精製標品用いて、37℃における反応pH依存性およびpH6.0における反応温度依存性を調べた。その結果、本酵素はpH4.5付近に反応の至適を有し、至適温度は55℃であることがわかった。またpH6.0、37℃において、キチナーゼ活性のNaCl濃度依存性を調べたところ、組換え型キチナーゼは1M付近に反応の至適を有することが明らかとなった。.また、NaClが0M付近の活性は最大活性40%程度であり、活性発現に塩を必要とすることがわかった。

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  • 高度好塩性古細菌に由来する新規古細菌型ロドプシンに関する研究

    Grant number：00J04716  2000

    日本学術振興会  科学研究費助成事業  特別研究員奨励費

    八波 利恵

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    Grant amount：\1200000 （ Direct Cost: \1200000 ）

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  • Proteins Produced by Extremophiles

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    Grant type：Competitive

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  • 極限環境微生物が生産する機能性タンパク質

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    Grant type：Competitive

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