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Matsuzawa T.,Bioproduction Research Institute | Mitsuishi Y.,Bioproduction Research Institute | Kameyama A.,Japan National Institute of Advanced Industrial Science and Technology | Yaoi K.,Bioproduction Research Institute
Journal of Biological Chemistry | Year: 2016

Aspergillus oryzae produces a unique β-glucosidase, isoprimeverose-producing oligoxyloglucan hydrolase (IPase), that recognizes and releases isoprimeverose (α-D-xylopyranose-(1→6)-D-glucopyranose) units from the non-reducing ends of oligoxyloglucans. A gene encoding A oryzae IPase, termed ipeA, was identified and expressed in Pichiapastoris. With the exception of cellobiose, IpeA hydrolyzes a variety of oligoxyloglucans and is a member of the glycoside hydrolase family 3. Xylopyranosyl branching at the non-reducing ends was vital for IPase activity, and galactosylation at a α-1, 6-linked xylopyranosyl side chain completely abolished IpeA activity. Hepta-oligoxyloglucan saccharide (Xyl3Glc4) substrate was preferred over tri-(Xyl1Glc2) and tetra-(Xyl2Glc2) oligoxyloglucan saccharides substrates. IpeA transferred isoprimeverose units to other saccharides, indicating transglycosylation activity. The ipeA gene was expressed in xylose and xyloglucan media and was strongly induced in the presence of xyloglucan endo-xyloglucanase-hydrolyzed products. This is the first study to report the identification of a gene encoding IPase in eukaryotes. © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Ikegami M.,Bioproduction Research Institute | Mie Y.,Bioproduction Research Institute | Hirano Y.,Bioproduction Research Institute | Komatsu Y.,Bioproduction Research Institute
ECS Electrochemistry Letters | Year: 2013

Flavin-containing monooxygenases (FMOs) play an essential role in the detoxification of foreign compounds, similar to cytochrome P450. We present here the direct electrochemistry of human FMO1 or FMO3 microsomes immobilized on a naphthalenethiol (Np-S)-coated electrode. Both hFMO microsomes were successfully activated on an Np-S thin film and oxidized methyl p-tolyl sulfide through direct electron transfer. The Michaelis constants were comparable to those reported in solution phase experiments. This system, which requires no NADPH and no enzyme purification step, offers a potential method for constructing cost-effective sensors. © 2013 The Electrochemical Society.

Yoshimura Y.,Research Center for New Fuels and Vehicle Technology | Suzuki K.,Bioproduction Research Institute | Gotoh M.,Research Center for Medical Glycoscience
AIST Today (International Edition) | Year: 2014

AIST continues to make significant efforts to encourage Japanese research institutes to initiate better R&D activities by networking with overseas research institutes, penetrating global markets and conducting global business operations. AIST works jointly with Thailand's National Science and Technology Development Agency (NSTDA) and the Thailand Institute of Scientific and Technological Research (TISTR) to develop fundamental technology to produce transportation fuel from non-edible biomass as part of the Science and Technology Research Partnership for Sustainable Development (SATREPS) being implemented by the Japan Science and Technology Agency and the Japan International Cooperation Agency. AIST has also established a framework for international joint research by three parties, including AIST and Bridgestone Corporation to initiate such technology development activities.

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