Kōhei Oda

ORCID: 0000-0003-3243-6629
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About
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Research Areas
  • Enzyme Production and Characterization
  • Peptidase Inhibition and Analysis
  • Protein Hydrolysis and Bioactive Peptides
  • Biochemical and Structural Characterization
  • Advanced ceramic materials synthesis
  • Phytase and its Applications
  • Microbial Natural Products and Biosynthesis
  • Phytochemical compounds biological activities
  • Insect Resistance and Genetics
  • Fungal Biology and Applications
  • Microplastics and Plastic Pollution
  • Enzyme Catalysis and Immobilization
  • Protease and Inhibitor Mechanisms
  • Enzyme Structure and Function
  • Metal and Thin Film Mechanics
  • Radioactivity and Radon Measurements
  • Advanced materials and composites
  • Biopolymer Synthesis and Applications
  • biodegradable polymer synthesis and properties
  • Radioactive contamination and transfer
  • Amino Acid Enzymes and Metabolism
  • Recycling and utilization of industrial and municipal waste in materials production
  • Biochemical and Molecular Research
  • Semiconductor materials and devices
  • Glycosylation and Glycoproteins Research

Kyoto Institute of Technology
2012-2024

Kazusa DNA Research Institute
2022

Honda (Japan)
2022

Niigata University of Pharmacy and Medical and Life Sciences
2019

Seikei University
2019

Musashino Academia Musicae
2019

Wake Research
2016

Nagoya Institute of Technology
2013

Sophia University
2008-2012

Kyoto University
1994-2011

Some bacteria think plastic is fantastic Bacteria isolated from outside a bottle-recycling facility can break down and metabolize plastic. The proliferation of plastics in consumer products, bottles to clothing, has resulted the release countless tons into environment. Yoshida et al. show how biodegradation by specialized could be viable bioremediation strategy (see Perspective Bornscheuer). new species, Ideonella sakaiensis , breaks using two enzymes hydrolyze PET primary reaction...

10.1126/science.aad6359 article EN Science 2016-03-10

Most petroleum-derived plastics, as exemplified by poly(ethylene terephthalate) (PET), are chemically inactive and highly resistant to microbial attack. The accumulation of plastic waste results in environmental pollution threatens ecosystems, referred the "microplastic issue". Recently, PET hydrolytic enzymes (PHEs) have been identified we reported degradation a consortium its bacterial resident, Ideonella sakaiensis. Bioremediation may thus provide an alternative solution recycling waste....

10.1021/acscatal.8b05171 article EN ACS Catalysis 2019-04-08

A Gram-stain-negative, aerobic, non-spore-forming, rod-shaped bacterium, designed strain 201-F6T, was isolated from a microbial consortium that degrades poly(ethylene terephthalate) (PET) collected in Sakai city, Japan, and characterized on the basis of polyphasic taxonomic study. The cells were motile with polar flagellum. contained cytochrome oxidase catalase. It grew within pH range 5.5–9.0 (optimally at 7–7.5) 15–42 ºC 30–37 ºC). major isoprenoid quinone ubiquinone eight isoprene units...

10.1099/ijsem.0.001058 article EN INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY 2016-04-05

Enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process safer than conventional industrial approaches. Recently, a cationic PET hydrolase (PETase) was identified from Ideonella sakaiensis. Pre-incubation low-crystallinity film with anionic surfactants prior to initiating the reaction found improve PETase activity 120-fold. After 36 h at 30 °C, thickness decreased by 22 %. The binding makes surface anionic, thereby attracting PETase. Mutagenesis showed...

10.1002/cssc.201802096 article EN ChemSusChem 2018-10-06

Pollution by plastics such as polyethylene (PE), polypropylene (PP), polyvinyl chloride (PVC), polyurethane (PUR), polyamide (PA), polystyrene (PS), and poly(ethylene terephthalate) (PET) is now gaining worldwide attention a critical environmental issue, closely linked to climate change. Among them, PET particularly prone hydrolysis, breaking down into its constituents, ethylene glycol (EG) terephthalate (TPA). Biorecycling or bioupcycling stands out one of the most promising methods for...

10.1021/acs.biochem.3c00554 article EN Biochemistry 2024-01-29

Glutamate decarboxylase (GAD) [EC 4.1.1.15] was purified from a cell-free extract of Lactobadllus brevis TFO 12005 by chromatographies on Sephadex G-100, DEAE-Sepharose CL-6B, and Mono Q. About 9 mg GAD obtained 90.2 g wet cells. The preparation showed single protein band SDS-PAGE. molecular weights SDS-PAGE gel filtration Superdex 200 were 60,000 120,000, respectively, indicating that L. exists as dimer. N-terminal amino acid sequence the NH2-Met-Asn-Lys-Asn-Asp-Gln-Glu-Gln-Thr-. optimum pH...

10.1271/bbb.61.1168 article EN Bioscience Biotechnology and Biochemistry 1997-01-01

10.1007/bf01086464 article EN Journal of Materials Science 1987-08-01

The molecular structure of the pepstatin-insensitive carboxyl peptidase from Scytalidium lignicolum , formerly known as scytalidopepsin B, was solved by multiple isomorphous replacement phasing methods and refined to an R factor 0.230 ( free = 0.246) at 2.1-Å resolution. In addition unbound peptidase, a product complex cleaved angiotensin II bound in active site enzyme also determined. We propose name scytalidocarboxyl B (SCP-B) for this enzyme. On basis conserved, catalytic residues...

10.1073/pnas.0400246101 article EN Proceedings of the National Academy of Sciences 2004-03-01

In this study, the glutamate decarboxylase (GAD) gene from Lactobacillus brevis IFO12005 (Biosci. Biotechnol. Biochem., 61, 1168-1171 (1997)), was cloned and expressed. The deduced amino acid sequence showed 99.6% 53.1% identity with GAD of L. ATCC367 lactis respectively. His-tagged recombinant an optimum pH 4.5-5.0, 54 kDa on SDS-PAGE. activity stability significantly dependent ammonium sulfate concentration, as observed in authentic GAD. Gel filtration that inactive form a dimer. contrast,...

10.1271/bbb.70782 article EN Bioscience Biotechnology and Biochemistry 2008-05-23

Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features these a unique triad, Ser-Glu-Asp, as well presence an aspartic acid residue in oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, kumamolisin thermophilic bacterium, Bacillus novo MN-32....

10.18388/abp.2003_3716 article EN cc-by Acta Biochimica Polonica 2003-03-31

A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. purified 43-kDa proteinase produced by this showed optimal activity at 50 °C pH 9–10 in 20% NaCl. The of the enzyme enhanced about 2.5-fold addition 20–35% NaCl, highly stabilized It found to be a serine related either chymotrypsin or subtilisin. absolutely preferred Ile P2 position substrates. Thus, with unique substrate specificity.

10.1271/bbb.50658 article EN Bioscience Biotechnology and Biochemistry 2006-06-23

In order to find a unique proteinase, proteinase-producing bacteria were screened from fish sauce in Thailand. An isolated moderately halophilic bacterium was classified and named Filobacillus sp. RF2-5. The molecular weight of the purified enzyme estimated be 49 kDa. showed highest activity at 60 °C pH 10–11 under 10% NaCl, highly stable presence about 25% NaCl. strongly inhibited by phenylmethane sulfonyl fluoride (PMSF), chymostatin, α-microbial alkaline proteinase inhibitor (MAPI)....

10.1271/bbb.69.38 article EN Bioscience Biotechnology and Biochemistry 2005-01-01

The corrosion behavior and strength degradation of alumina ceramics with 99%, 99.9%, 99.99% Al 2 O 3 were studied in water at 300°C 8.6 MPa for 1 to 10 d. weight loss was mainly attributed the dissolution SiO Na grain‐boundary impurities. Intergranular proceeded by preferential attack grain boundaries. extent reduction corroded related impurity level ceramics.

10.1111/j.1151-2916.1997.tb03258.x article EN Journal of the American Ceramic Society 1997-12-01

Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number inhibitors, have been solved and refined at high- to atomic-level resolution. All these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, chymostatin, as well previously studied iodotyrostatin pseudo-iodotyrostatin) make covalent bonds active site Ser287 through their aldehyde moieties, while side chains occupy subsites S1−S4 enzyme. The mode binding is almost identical for P1...

10.1021/bi011817n article EN Biochemistry 2001-11-28
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