Kyushu University Academic Staff Educational and Research Activities Database
List of Papers
Noriho Kamiya Last modified date:2018.06.08

Professor / Department of Applied Chemistry / Faculty of Engineering


Papers
1. Patma, Kosuke Minamihata, T. Tatsuke, Jae Man Lee, Takahiro Kusakabe, Noriho Kamiya, Expression and Activation of Horseradish Peroxidase–Protein A/G Fusion Protein in Silkworm Larvae for Diagnostic Purposes, Biotechnology Journal, 10.1002/biot.201700624, 13, 1700624, 2018.06.
2. Akitsu Masuda, Jian Xu, Kosuke Minamihata, Genki Kagawa, Yusei Hamada, Yoshiki Morifuji, Takumi Yano, Masato Hino, Daisuke Morokuma, Noriko Karasaki, Hiroaki Mon, Noriho Kamiya, Takahiro Kusakabe, Jae Man Lee, Production of a biologically active human basic fibroblast growth factor using silkworm-baculovirus expression vector system, Journal of Asia-Pacific Entomology, https://doi.org/10.1016/j.aspen.2018.05.002, 21, 2, 716-720, 2018.06, As a therapeutic treatment, recombinant human basic fibroblast growth factor (rhbFGF) is usually employed in tissue regeneration, and as an essential component in culture medium for maintaining the induced pluripotent stem (iPS) cell and embryonic stem (ES) cell in an undifferentiated state. Therefore, a large amount of biologically active rhbFGF is required. In this study, silkworm-baculovirus expression vector system (silkworm-BEVS) is employed to achieve a high productivity of recombinant rhbFGF with two small affinity tags (His-tag and STREP-tag) at the N or C-terminus. It is observed that rhbFGF with 30 K signal peptide of silkworm were successfully expressed but are not sufficiently secreted into the culture medium of cultured insect cells. Then we purified the N- or C-tagged intracellular rhbFGF protein and obtained a yield of about 0.7 mg/larva and 1.2 mg/larva, respectively. Although the final yield of the C-tagged rhbFGF is higher than that of the N-tagged, rhbFGF with N-tag demonstrated promising and comparable biological activity, which is evaluated through a mammalian cell proliferation assay. Taken together, these results indicate that silkworm-BEVS could contribute to the mass-production of the biologically active rhbFGF for medical uses..
3. Safrina Dyah Hardiningtyas, Rie Wakabayashi, Momoko Kitaoka, Yoshiro Tahara, Kosuke Minamihata, Masahiro Goto, Noriho Kamiya, Mechanistic investigation of transcutaneous protein delivery using solid-in-oil nanodispersion
A case study with phycocyanin, European Journal of Pharmaceutics and Biopharmaceutics, https://doi.org/10.1016/j.ejpb.2018.01.020, 127, 44-50, 2018.06, Phycocyanin (PC), a water-soluble protein-chromophore complex composed of hexameric (αβ)6 subunits, has important biological functions in blue-green algae as well as pharmacological activities in biomedicine. We have previously developed a solid-in-oil (S/O) nanodispersion method to deliver biomacromolecules through the skin, although the transcutaneous mechanism has not yet been fully elucidated. To study the mechanism of transcutaneous protein delivery, we therefore enabled S/O nanodispersion by coating PC with hydrophobic surfactants and evaluated how the proteinaceous macromolecules formulated in an oil phase might permeate the skin. The extent of S/O nanodispersion of PC was dependent on the type of surfactant, suggesting that the selection of a suitable surfactant is crucial for encapsulating a large protein having a subunit structure. By measuring the intrinsic fluorescence of PC, we found that S/O nanodispersion facilitated the accumulation of PC in the stratum corneum (SC) of Yucatan micropig skin. Furthermore, after crossing the SC layer, the fluorescent recovery of PC was evident, indicating the release of the biologically active form of PC from the SC into the deeper skin layer..
4. Muhamad Alif Razi, Rie Wakabayashi, Yoshiro Tahara, Masahiro Goto, Noriho Kamiya, Genipin-stabilized caseinatehitosan nanoparticles for enhanced stability and anti-cancer activity of curcumin, Colloids and Surfaces B: Biointerfaces, https://doi.org/10.1016/j.colsurfb.2018.01.041, 164, 308-315, 2018.04, Nanoparticles formed by the assembly of protein and polysaccharides are of great interest for the delivery of hydrophobic molecules. Herein, the formation of genipin-crosslinked nanoparticles from caseinate (CS) and chitosan (CH) is reported for the delivery of curcumin, a polyphenolic compound from turmeric, to cells. Genipin-crosslinked CS-CH nanoparticles (G-CCNPs) having a diameter of ∼250 nm and a low polydispersity index showed excellent stability over a wide pH range, as indicated by dynamic light scattering and transmission electron microscopic measurements. Cellular uptake of curcumin loaded into G-CCNPs by HeLa cells was improved, as measured by confocal laser scanning microscopy (CLSM) and fluorescence-activated cell-sorting analysis. Cell proliferation assays indicated that G-CCNPs were nontoxic and that curcumin's anticancer activity in vitro was also improved by G-CCNPs. Stability of curcumin at neutral pH was enhanced by G-CCNPs. CLSM study revealed that G-CCNPs were poorly internalized by HeLa cells, possibly because of strong cell membrane interactions and a negative zeta potential. Overall, our results suggested that the enhanced curcumin cytotoxicity might be associated with the enhanced stability of curcumin by G-CCNPs and free curcumin released from G-CCNPs into the cell. These biocompatible NPs might be suitable carriers for enhancing curcumin's therapeutic potential..
5. Geisa A.L.G. Budinova, Yutaro Mori, Tsutomu Tanaka, Noriho Kamiya, Casein-based scaffold for artificial cellulosome design, Process Biochemistry, https://doi.org/10.1016/j.procbio.2017.12.013, 66, 140-145, 2018.03, Cellulosomal systems are known as highly efficient biocatalysts in the degradation of lignocellulosic biomass in nature, but they remain unsuitable for industrial applications. In seeking alternatives to natural cellulosomes, casein was chosen as a scaffold for cellulase clustering. Casein is recognized as an excellent substrate for microbial transglutaminase (MTG) because it contains naturally reactive glutamine and lysine residues. A substrate peptide containing an MTG-reactive lysine residue was inserted into the C-terminus of the endoglucanase Cel5A and Cel6A from Thermobifida fusca using genetic engineering. The engineered cellulases, EG(Cel5A) and EG(Cel6A), were conjugated onto casein in different ratios by an MTG-mediated site-specific protein crosslinking reaction. Overall, a more than two-fold increase was observed when EG(Cel5A) was conjugated onto N,N-dimethylcasein, but a small or no change was observed for EG(Cel6A)..
6. Rie Wakabayashi, Masato Sakuragi, Shuto Kozaka, Yoshiro Tahara, Noriho Kamiya, Masahiro Goto, Solid-in-Oil Peptide Nanocarriers for Transcutaneous Cancer Vaccine Delivery against Melanoma, Molecular Pharmaceutics, https://doi.org/10.1021/acs.molpharmaceut.7b00894, 15, 3, 955-961, 2018.03, Cancer vaccines represent a prophylactic or therapeutic method of suppressing cancer by activating the adaptive immune system. The immune response is initiated by the delivery of tumor antigens to antigen presenting cells (APCs). The use of peptides as vaccine antigens is advantageous, especially in the availability and productivity of pure and defined antigens. However, their limited immunogenicity remains a major drawback, and therefore, the utilization of nanocarriers as a means of delivering antigens to target cells and/or the addition of immune stimulants have been investigated as an efficient peptide-based cancer vaccine. We have developed a solid-in-oil (S/O) nanodispersion as a transcutaneous nanocarrier for hydrophilic molecules. This system has attractive features as a peptide nanocarrier for cancer vaccines, including transcutaneous targeting of professional APCs in the skin, high encapsulation efficacy of hydrophilic molecules, and capacity for coloading with a variety of immune stimulants such as adjuvants. We therefore sought to utilize the developed S/O nanodispersion for the delivery of the tyrosine-related protein 2 peptide, TRP-2180-188, as a peptide antigen against melanoma. Transcutaneous vaccination of the S/O nanodispersion coloaded with adjuvant R-848 was associated with a significant inhibition of melanoma growth and suppression of lung metastasis in tumor-bearing mice. Our findings indicate the potential of S/O nanodispersions as an endogenous peptide carrier for cancer vaccines..
7. Qingliang Kong, Momoko Kitaoka, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Transcutaneous immunotherapy of pollinosis using solid-in-oil nanodispersions loaded with T cell epitope peptides, International Journal of Pharmaceutics, https://doi.org/10.1016/j.ijpharm.2017.07.020, 529, 1-2, 401-409, 2017.08, Pollinosis, a typical seasonal allergy, is a serious public health problem. Limited numbers of patients receive curative immunotherapy instead of symptomatic therapy; however, there are still some concerns about the inconvenience and side effects of subcutaneous injections and sublingual administration caused by immunotherapy. Here, we propose a simple and safe transcutaneous immunotherapy using solid-in-oil (S/O) nanodispersions loaded with vaccine T cell epitope peptides derived from pollen allergen. S/O nanodispersions are oil-based dispersions of antigens coated with hydrophobic surfactants. They have a high potential to deliver biomolecules including peptides or proteins to immune cells in the skin, and to induce an immune response. The result of quantitative and qualitative analysis by in vitro permeation experiments demonstrated the effective permeation of T cell epitope peptides into the skin. Furthermore, in vivo experiments using a pollinosis mouse model indicated that the S/O nanodispersions loaded with T cell epitopes suppressed serum antibody IgE and cytokine production, and alleviated allergic symptoms to a similar therapeutic level to that observed for subcutaneous injection. These results indicate the potential of transcutaneous immunotherapy using S/O nanodispersions for the future treatment of pollinosis..
8. Mari Takahara, Rie Wakabayashi, Kosuke Minamihata, Masahiro Goto, Noriho Kamiya, Primary Amine-Clustered DNA Aptamer for DNA-Protein Conjugation Catalyzed by Microbial Transglutaminase, Bioconjugate Chemistry, https://doi.org/10.1021/acs.bioconjchem.7b00594, 28, 12, 2954-2961, 2017.12, DNA-protein conjugates are promising biomolecules for use in areas ranging from therapeutics to analysis because of the dual functionalities of DNA and protein. Conjugation requires site-specific and efficient covalent bond formation without impairing the activity of both biomolecules. Herein, we have focused on the use of a microbial transglutaminase (MTG) that catalyzes the cross-linking reaction between a glutamine residue and a primary amine. In a model bioconjugation, a highly MTG-reactive Gln (Q)-donor peptide (FYPLQMRG, FQ) was fused to enhanced green fluorescent protein (FQ-EGFP) and a primary amine-clustered DNA aptamer was enzymatically synthesized as a novel acyl-acceptor substrate of MTG, whose combination leads to efficient and convenient preparation of DNA-protein conjugates with high purity. Dual functionality of the obtained DNA-EGFP conjugate was evaluated by discrimination of cancer cells via c-Met receptor recognition ability of the DNA aptamer. The DNA aptamer-EGFP conjugate only showed fluorescence toward cells with c-Met overexpression, indicating the retention of the biochemical properties of the DNA and EGFP in the conjugated form..
9. Lili Jia, Kosuke Minamihata, Hirofumi Ichinose, Kouhei Tsumoto, Noriho Kamiya, Polymeric SpyCatcher Scaffold Enables Bioconjugation in a Ratio-Controllable Manner, Biotechnology Journal, https://doi.org/10.1002/biot.201700195, 12, 12, 2017.12, Conjugating enzymes into a large protein assembly often results in an enhancement of overall catalytic activity, especially when different types of enzymes that work cooperatively are assembled together. However, exploring the proper method to achieve protein assemblies with high stability and also to avoid loss of the function of each component for efficient enzyme clustering is remained challenging. Assembling proteins onto synthetic scaffolds through varied post-translational modification methods is particularly favored since the proteins can be site-specifically conjugated together with less activity loss. Here, a SpyCatcher polymer is prepared through catalytic reaction of horseradish peroxidase (HRP) and serves as a polymeric proteinaceous scaffold for construction of protein assemblies. Taking advantage of the favorable SpyCatcher–SpyTag interaction, SpyTagged proteins can be easily assembled onto the polymeric SpyCatcher scaffold with controllable binding ratio and site specificity. Firstly, the feasibility of construction of ratio-controllable binary artificial hemicellulosomes by assembling endoxylanase and arabinofuranosidase is explored. This construct achieves higher sugar conversion than that of the free enzymes when the proportion of arabinofuranosidase is high, because the close spatial proximity of the enzymes allows them to work in a synergistic manner. Another application for biosensing is developed by conjugating SpyTagged Nanoluc and protein G onto SpyCatcher polymer. Due to the protein clustering effect, an amplified luminescent intensity is achieved by the resulting conjugates than chimera protein of Nanoluc and protein G in ovalbumin detection in ELISA..
10. Rie Wakabayashi, Yahiro, Kensuke, Hayashi, Kounosuke, Masahiro Goto, Noriho Kamiya, Protein-Grafted Polymers Prepared Through a Site-Specific Conjugation by Microbial Transglutaminase for an Immunosorbent Assay, BIOMACROMOLECULES, 10.1021/acs.biomac.6b01538, 18, 2, 422-430, 2017.02.
11. Tatsukawa, Hideki, Liu, Hong Hong, Oba, Shota, Noriho Kamiya, Nakanishi, Yoichi, Hitomi, Kiyotaka, FRET-based detection of isozyme-specific activities of transglutaminases, AMINO ACIDS, 10.1007/s00726-016-2322-0, 49, 3, 615-623, 2017.03.
12. Hideki Tatsukawa, Hong Hong Liu, Shota Oba, Noriho Kamiya, Yoichi Nakanishi, Kiyotaka Hitomi, FRET-based detection of isozyme-specific activities of transglutaminases, Amino Acids, https://doi.org/10.1007/s00726-016-2322-0, 49, 3, 615-623, 2017, Transglutaminases (TGs) comprise a protein family in which the members catalyze the formation of isopeptide bonds between glutamine and lysine residues in various proteins. Expression studies on its three major members, FXIII, TG1, and TG2, have been performed in a relatively large number of mammalian tissues in comparison with those on the other isozymes. We previously identified a highly reactive substrate peptide, including glutamine, for each isozyme from a phage display library and developed a method for detecting isozyme-specific activities by incorporating a labeled substrate peptide into lysine residues of proteins. Here, we describe genetically encoded Förster resonance energy transfer (FRET)-based probes composed of each fluorescence protein (Cerulean and EVenus) fused with substrate peptides. The probe pairs, designated as Trac-MTG (His-CerΔ11-LQ/EV-K-His) containing linker and substrate peptide sequence for microbial TG (MTG), increased the EVenus:Cerulean fluorescence intensity ratio by more than 1.5-fold. Furthermore, we demonstrated that Trac-TG1 (His-CerΔ11-K5) and Trac-TG2 (His-CerΔ11-T26) containing substrate peptide sequence for mammalian TGs successfully detected the isozyme-specific activity of TG1 and TG2, respectively. In this study, we developed a rapid and convenient experimental system for measuring the isozyme-specific activity of TGs. The application of these probes for analyses in cells and tissues will be helpful for elucidating the physiological and pathological functions of TGs..
13. Hyung Joon Cha, Noriho Kamiya, Vikineswary Sabaratnam, Editorial
Asian Congress of Biotechnology 2015, Biotechnology Journal, https://doi.org/10.1002/biot.201600650, 11, 11, 1371-1372, 2016.11.
14. Ryosuke Yamada, Kazunori Nakashima, Nanami Asai-Nakashima, Wataru Tokuhara, Nobuhiro Ishida, Satoshi Katahira, Noriho Kamiya, Chiaki Ogino, Akihiko Kondo, Direct Ethanol Production from Ionic Liquid-Pretreated Lignocellulosic Biomass by Cellulase-Displaying Yeasts, Applied Biochemistry and Biotechnology, https://doi.org/10.1007/s12010-016-2322-2, 182, 1, 229-237, 2017, Among the many types of lignocellulosic biomass pretreatment methods, the use of ionic liquids (ILs) is regarded as one of the most promising strategies. In this study, the effects of four kinds of ILs for pretreatment of lignocellulosic biomass such as bagasse, eucalyptus, and cedar were evaluated. In direct ethanol fermentation from biomass incorporated with ILs by cellulase-displaying yeast, 1-butyl-3-methylimidazolium acetate ([Bmim][OAc]) was the most effective IL. The ethanol production and yield from [Bmim][OAc]-pretreated bagasse reached 0.81 g/L and 73.4% of the theoretical yield after fermentation for 96 h. The results prove the initial concept, in which the direct fermentation from lignocellulosic biomass effectively promoted by the pretreatment with IL..
15. Furukawa, Shin-ya, Hattori, Gaku, Sakai, Shinji, Kamiya, Noriho, Highly efficient and low toxic skin penetrants composed of amino acid ionic liquids, RSC Adv., 10.1039/C6RA16926K, 6, 87753-87755, 2016.09.
16. Kazunori Matsuura, Tomohiro Nakamura, Kenta Watanabe, Takanori Noguchi, Kosuke Minamihata, Kamiya, Noriho, Nobuo Kimizuka, Self-assembly of Ni-NTA-modified beta-annulus peptides into artificial viral capsids and encapsulation of His-tagged proteins, Org. Biomol. Chem., 10.1039/C6OB01227B, 14, 7869-7874, 2016.08.
17. Mori, Yutaro, Budinova, Geisa Aparecida Lopes Goncalves, Nakazawa, Hikaru, Umetsu, Mitsuo, Kamiya, Noriho, One-dimensional assembly of functional proteins: toward the design of an artificial cellulosome, Mol. Syst. Des. Eng., 10.1039/C6ME90005D, 1, 1, 66-73, 2016.04, In biological systems, proteins can form well-organized, higher-order structures with unique functions that would be difficult to achieve with a single protein. These proteinaceous supramolecular structures form by self-assembly, and the spatial arrangement of the protein building blocks in them is very important. In the present study, an artificial system was developed using recombinant proteins as building blocks, which were assembled in a one-dimensional manner. The assembly of these building blocks was based on the avidin-biotin interaction. A tetrameric biotin ligand unit was designed so that the 1:4 stoichiometry of the avidin-biotin interaction was altered to a 1:2 directional interaction between the streptavidin and tetrabiotinylated protein units. In a proof-of-concept study, site-specifically tetrabiotin-labeled endoglucanase and cellulose-binding module units were prepared, then these components were self-assembled by mixing with streptavidin to mimic a natural cellulosome. The formation of one-dimensional assemblies of the protein units depended on the stoichiometry of the avidin-biotin interaction sites in the system. Interestingly, the saccharification efficiency improved when the component ratio of protein units in the assemblies was changed..
18. Moriyama, Kousuke, Naito, Shono, Rie Wakabayashi, Masahiro Goto, Noriho Kamiya, Enzymatically prepared redox-responsive hydrogels as potent matrices for hepatocellular carcinoma cell spheroid formation, BIOTECHNOLOGY JOURNAL, 10.1002/biot.201600087, 11, 11, 1452-1460, 2016.11.
19. Takahara, Mari, Budinova, Geisa Aparecida Lopes Goncalves, Nakazawa, Hikaru, Mori, Yutaro, Umetsu, Mitsuo, Kamiya, Noriho, Salt-Switchable Artificial Cellulase Regulated by a DNA Aptamer, BIOMACROMOLECULES, 10.1021/acs.biomac.6b01141, 17, 10, 3356-3362, 2016.10.
20. Kitaoka, Momoko, Rie Wakabayashi, Masahiro Goto, Noriho Kamiya, Solid-in-oil nanodispersions for transdermal drug delivery systems, BIOTECHNOLOGY JOURNAL, 10.1002/biot.201600081, 11, 11, 1375-1385, 2016.11.
21. Uju, Masahiro Goto, Noriho Kamiya, Powerful peracetic acid-ionic liquid pretreatment process for the efficient chemical hydrolysis of lignocellulosic biomass, BIORESOURCE TECHNOLOGY, 10.1016/j.biortech.2016.04.121, 214, 487-495, 2016.08.
22. Akira Tsuchiya, Siti Norulhuda Hashim, Ise, Shoko, Furuhata, Takafumi, Rie Wakabayashi, Masahiro Goto, Kawai, Kiyohiko, Noriho Kamiya, Shinsuke Sando, BODIPY-labeled Fluorescent Aptamer Sensors for Turn-on Sensing of Interferon-gamma and Adenine Compounds on Cells, ANALYTICAL SCIENCES, 32, 5, 543-547, 2016.05.
23. Takahara, Mari, Hayashi, Kounosuke, Masahiro Goto, Kamiya, Noriho, Enzymatic conjugation of multiple proteins on a DNA aptamer in a tail-specific manner, BIOTECHNOLOGY JOURNAL, 10.1002/biot.201500560, 11, 6, 814-823, 2016.06.
24. Jia, Lili, Budinova, Geisa A. L. G., Takasugi, Yusaku, Noda, Shuhei, Tanaka, Tsutomu, Hirofumi Ichinose, Masahiro Goto, Kamiya, Noriho, Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase, BIOCHEMICAL ENGINEERING JOURNAL, 10.1016/j.bej.2016.07.013, 114, 271-278, 2016.10.
25. Hosomomi, Yukiho, F. Kubota, Rie Wakabayashi, Kamiya, Noriho, Masahiro Goto, Diglycolic amic acid-modified E. coli as a biosorbent for the recovery of rare earth elements, BIOCHEMICAL ENGINEERING JOURNAL, 10.1016/j.bej.2016.06.005, 113, 102-106, 2016.09.
26. Masato Hino, Takuji Kawanami, Noriho Kamiya, Tsuneyuki Tatsuke, Yutaka Banno, Takahiro Kusakabe, JAE MAN LEE, High-level expression and purification of biologically active human IL-2 using silkworm-baculovirus expression vector system, JOURNAL OF ASIA-PACIFIC ENTOMOLOGY, 10.1016/j.aspen.2016.03.014, 19, 2, 313-317, 2016.06.
27. Yukiho HOSOMOMI, Teppei NIIDE, Rie Wakabayashi, Masahiro Goto, Noriho Kamiya, Biocatalytic Formation of Gold Nanoparticles Decorated with Functional Proteins inside Recombinant Escherichia coli Cells, ANALYTICAL SCIENCES, 32, 3, 295-300, Cover page illustration, 2016.03.
28. Siti Norulhuda Hashim, Akira Tsuchiya, Noriho Kamiya, Shinsuke Sando, A Single Fluorophore-labeled Aptamer Sensor for the Detection of Interferon Gamma, Chem. Lett., 44, 12, 1670-1672, 2015.12.
29. Uju, Wijayanta, Agung Tri, Masahiro Goto, 神谷 典穂, Great potency of seaweed waste biomass from the carrageenan industry for bioethanol production by peracetic acid-ionic liquid pretreatment, BIOMASS & BIOENERGY, 10.1016/j.biombioe.2015.05.023, 81, 63-69, 2015.10.
30. Hayashi, Kounosuke, JAE MAN LEE, Tomozoe, Yusuke, takahiro kusakabe, 神谷 典穂, Heme precursor injection is effective for Arthromyces ramosus peroxidase fusion protein production by a silkworm expression system, JOURNAL OF BIOSCIENCE AND BIOENGINEERING, 10.1016/j.jbiosc.2015.02.013, 120, 4, 384-386, 2015.10.
31. Lili Jia, LOPES GONCALVES GEISA APARECIDA, Yusaku Takasugi, Yutaro Mori, Shuhei Noda, Tsutomu Tanaka, Hirofumi Ichinose, 神谷 典穂, Effect of pretreatment methods on the synergism of cellulase and xylanase during the hydrolysis of bagasse, BIORESOURCE TECHNOLOGY, 10.1016/j.biortech.2015.02.041, 185, 158-164, 2015.06.
32. LOPES GONCALVES GEISA APARECIDA, Yusaku Takasugi, Lili Jia, Yutaro Mori, Tsutomu Tanaka, Hirofumi Ichinose, 神谷 典穂, Synergistic effect and application of xylanases as accessory enzymes to enhance the hydrolysis of pretreated bagasse, ENZYME AND MICROBIAL TECHNOLOGY, 10.1016/j.enzmictec.2015.01.007, 72, 16-24, 2015.05.
33. Kousuke Moriyama, Rie Wakabayashi, Masahiro Goto, 神谷 典穂, Enzyme-mediated preparation of hydrogels composed of poly(ethylene glycol) and gelatin as cell culture platforms, RSC ADVANCES, 10.1039/c4ra12334d, 5, 4, 3070-3073, 2015.03.
34. Kosuke Minamihata, Masahiro Goto, 神谷 典穂, Site-specific conjugation of an antibody-binding protein catalyzed by horseradish peroxidase creates a multivalent protein conjugate with high affinity to IgG, BIOTECHNOLOGY JOURNAL, 10.1002/biot.201400512, 10, 1, 222-226, 2015.01.
35. Kousuke Moriyama, Rie Wakabayashi, Masahiro Goto, 神谷 典穂, Characterization of Enzymatically Gellable, Phenolated Linear Poly(Ethylene Glycol) with Different Molecular Weights for Encapsulating Living Cells, BIOCHEMICAL ENGINEERING JOURNAL, 93, 25-30, 2015.01.
36. Rie Wakabayashi, Ryutaro Ishiyama, 神谷 典穂, Masahiro Goto, A Novel Surface-Coated Nanocarrier for Efficient Encapsulation and Delivery of Camptothecin to Cells, MedChemComm, 5, 1515-1519, 2014.07.
37. Rie Wakabayashi, Yuko Abe, Masahiro Goto, 神谷 典穂, The Self-Assembly and Secondary Structure of Peptide Amphiphiles Determine the Membrane Permeation Activity, RSC Advances, 4, 30654-30657, 2014.07.
38. Kousuke Moriyama, Kosuke Minamihata, Rie Wakabayashi, Masahiro Goto, 神谷 典穂, Enzymatic preparation of a redox-responsive hydrogel for encapsulating and releasing living cells, CHEMICAL COMMUNICATIONS, 10.1039/c3cc49766f, 50, 44, 5895-5898, 2014.08, Horseradish peroxidase-mediated oxidative cross-linking of a thiolated poly(ethylene glycol) is promoted in the absence of exogenous hydrogen peroxide, by adding a small amount of phenolic compound under physiological conditions. The prepared hydrogel can encapsulate and release living mammalian cells..
39. Teppei Niide, Masahiro Goto, 神谷 典穂, Enzymatic self-sacrificial display of an active protein on gold nanoparticles, RSC ADVANCES, 10.1039/c3ra46384b, 4, 12, 5995-5998, 2014.04.
40. Jameson, Laramie P., Balaz, Milan, Dzyuba, Sergei V., 神谷 典穂, Conformational preference of a porphyrin rotor in confined environments, RSC ADVANCES, 10.1039/c3ra45668d, 4, 2, 705-708, 2014.01.
41. Kitaoka, Momoko, Imamura, Kana, Hirakawa, Yuya, Tahara, Yoshiro, 神谷 典穂, Masahiro Goto, Sucrose laurate-enhanced transcutaneous immunization with a solid-in-oil nanodispersion, MEDCHEMCOMM, 10.1039/c3md00164d, 5, 1, 20-24, 2014.01.
42. Baba, Yuzo, Fukiko Kubota, 神谷 典穂, Masahiro Goto, Development of Novel Extractants with Amino Acid Structure for Efficient Separation of Nickel and Cobalt from Manganese Ions, INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH, 10.1021/ie403524a, 53, 2, 812-818, 2014.01.
43. Kitaoka, Momoko, Imamura, Kana, Hirakawa, Yuya, Tahara, Yoshiro, 神谷 典穂, Masahiro Goto, Needle-free immunization using a solid-in-oil nanodispersion enhanced by a skin-permeable oligoarginine peptide, INTERNATIONAL JOURNAL OF PHARMACEUTICS, 10.1016/j.ijpharm.2013.10.006, 458, 2, 334-339, 2013.12.
44. Niide, Teppei, Shimojo, Kojiro, Rie Wakabayashi, Masahiro Goto, 神谷 典穂, Enzymatic Fabrication of Protein-Decorated Gold Nanoparticles by the Aid of Artificial Peptides with Gold-Binding Affinity, LANGMUIR, 10.1021/la401327h, 29, 50, 15596-15605, 2013.12.
45. Takahara, Mari, Hayashi, Kounosuke, Masahiro Goto, 神谷 典穂, Tailing DNA aptamers with a functional protein by two-step enzymatic reaction, JOURNAL OF BIOSCIENCE AND BIOENGINEERING, 10.1016/j.jbiosc.2013.05.025, 116, 6, 660-665, 2013.12.
46. Moriyama, Kousuke, Minamihata, Kosuke, Rie Wakabayashi, Masahiro Goto, 神谷 典穂, Enzymatic preparation of streptavidin-immobilized hydrogel using a phenolated linear poly(ethylene glycol), BIOCHEMICAL ENGINEERING JOURNAL, 10.1016/j.bej.2013.04.007, 76, 37-42, 2013.07.
47. Tatsuaya Okuda, Tahara, Yoshiro, 神谷 典穂, Masahiro Goto, Satoru Kidoaki, S/O-nanodispersion electrospun fiber mesh effective for sustained release of healthy plasmid DNA with the structural and functional integrity, JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION, 10.1080/09205063.2012.755600, 24, 10, 1277-1290, 2013.07.
48. Muraoka, Jin;, 神谷 典穂, Ito, Yuji, Preparation and evaluation of cellulose-dissolving magnetic ionic liquid, JOURNAL OF MOLECULAR LIQUIDS, 10.1016/j.molliq.2013.03.012, 182, 76-78, 2013.06.
49. Yang, Fan, Fukiko Kubota, Baba, Yuzo, 神谷 典穂, Masahiro Goto, Selective extraction and recovery of rare earth metals from phosphor powders in waste fluorescent lamps using an ionic liquid system, JOURNAL OF HAZARDOUS MATERIALS, 10.1016/j.jhazmat.2013.03.026, 254, 79-88, 2013.06.
50. Uju, Abe, Kojiro, Uemura, Nobuyuki, Oshima, Toyoji, Masahiro Goto, 神谷 典穂, Peracetic acid-ionic liquid pretreatment to enhance enzymatic saccharification of lignocellulosic biomass, BIORESOURCE TECHNOLOGY, 10.1016/j.biortech.2013.03.147, 138, 87-94, 2013.06.
51. Uju, Shoda, Yasuhiro, Masahiro Goto, Tokuhara, Wataru, Ishida, Nobuhiro, Ogino, Chiaki, 神谷 典穂, Low melting point pyridinium ionic liquid pretreatment for enhancing enzymatic saccharification of cellulosic biomass, BIORESOURCE TECHNOLOGY, 10.1016/j.biortech.2012.06.096, 135, 103-108, 2013.05.
52. Hiroki Abe, Rie Wakabayashi, Hiroaki Yonemura, Sunao Yamada, Masahiro Goto, Noriho Kamiya, Split Spy0128 as a Potent Scaffold for Protein Cross-Linking and Immobilization, BIOCONJUGATE CHEMISTRY, 10.1021/bc300606b, 24, 2, 242-250, 2013.02.
53. Shinya Furukawa, Kazuhiro Hasegawa, Ichino Fuke, Kkoji Kittaka, Terumitsu Nakakoba, Noriho Kamiya, Masahiro Goto, Enzymatic synthesis of Z-aspartame in liquefied amino acid substrates, BIOCHEMICAL ENGINEERING JOURNAL, 10.1016/j.bej.2012.10.002, 70, 84-87, 2013.01.
54. Kosuke Minamihata, Masahiro Goto, Noriho Kamiya, Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions, Biotechnol. Lett., 34, 2055-2060, 2012.08.
55. Fan Yang, Noriho Kamiya, Masahiro Goto, Transdermal delivery of the anti-rheumatic agent methotrexate using a solid-in-oil nanocarrier, EUROPEAN JOURNAL OF PHARMACEUTICS AND BIOPHARMACEUTICS, 10.1016/j.ejpb.2012.05.016, 82, 1, 158-163, 2012.09.
56. Yoshiro Tahara, Shota Honda, Noriho Kamiya, Masahiro Goto, Transdermal delivery of insulin using a solid-in-oil nanodispersion enhanced by arginine-rich peptides, MEDCHEMCOMM, 10.1039/c2md20059g, 3, 12, 1496-1499, 2012.12.
57. Yoshiro Tahara, Takeshi Kaneko, Riki Toita, Chiharu Yoshiyama, Takuya Kitaoka, Takuro Niidome, Yoshiki Katayama, Noriho Kamiya, Masahiro Goto, A novel double-coating carrier produced by solid-in-oil and solid-in-water nanodispersion technology for delivery of genes and proteins into cells, JOURNAL OF CONTROLLED RELEASE, 10.1016/j.jconrel.2012.05.001, 161, 3, 713-721, 2012.08.
58. Muhammad Moniruzzaman, Keishirou Ino, Noriho Kamiya, Masahiro Goto, Lipase incorporated ionic liquid polymers as active, stable and reusable biocatalysts, Org. Biomol. Chem., 14, 7707-7713, 2012.08.
59. Kosuke Minamihata, Masahiro Goto, Noriho Kamiya, Control of a Tyrosyl Radical Mediated Protein Cross-Linking Reaction by Electrostatic Interaction, BIOCONJUGATE CHEMISTRY, 10.1021/bc300137s, 23, 8, 1600-1609, 2012.08.
60. Noriho Kamiya, Momoko Kitaoka, Kounosuke Hayashi, Yoshiyuki HIraishi, Koji Nakano, Katsuyuki Miyawaki, Sumihare Noji, Masahiro Goto, Transglutaminase-Mediated in Situ Hybridization (TransISH) System: A New Methodology for Simplified mRNA Detection, ANALYTICAL CHEMISTRY, 10.1021/ac2034198, 84, 14, 5885-5891, 2012.07, In situハイブリダイゼーション法は遺伝子機能解明のための重要な基礎的技術となっているが、免疫染色技術を利用する一般的な方法では、煩雑で時間のかかる操作が必要とされる。本研究では、簡易な操作でターゲット核酸を検出するための新たなRNA―酵素複合体の調製方法を開発し、それを用いた組織切片上での高感度核酸検出を達成した。.
61. J.Shimada, T. Maruyama, M. Kitaoka, N. Kamiya, M. Goto, Microplate assay for aptamer-based thrombin detection using a DNA-enzyme conjugate based on His-tag chemistry, Anal. Biochem., 421, 541-546, 2012.02.
62. J.Shimada, T. Maruyama, M. Kitaoka, N. Kamiya, M. Goto, DNA-enzyme conjugate with a weak inhibitor that can specifically detect thrombin in a homogeneous medium, Anal. Biochem., 414, 103-108, 2011.09.
63. H. Piao, N. Kamiya, F. Cui, M. Goto, Preparation of a solid-in-oil nanosuspension containing l-ascorbic acid as a novel long-term stable topical formulation, Int. J. Pharm., 420, 156-160, 2011.10.
64. D. Pissuwan, K. Nose, R. Kurihara, K. Kaneko, Y. Tahara, N. Kamiya, M. Goto, Y. Katayama, T. Niidome, A solid-in-oil dispersion of gold nanorods can enhance trandermal protein delivery and skin vaccination, small, 7, 215-220, 2011.02.
65. T. Mouri, N. Kamiya,* M. Goto, New strategy to enhance catalytic performance of Escherichia coli whole cell biocatalysts harboring P450cam mutants, Biochem. Eng. J., 53, 229-233, 2011.01.
66. M. Sakono, K. Motomura, T. Maruyama, N. Kamiya, M. Goto, Alpha casein micelles show not only molecular chaperone-like aggregation inhibition properties but also protein refolding activity from the denatured state, Biochem. Biophys. Res. Commun., 404, 494-497, 2011.04.
67. K. Minamihata, M. Goto, N. Kamiya, Protein heteroconjugation by the peroxidase-catalyzed tyrosine coupling reaction, Bioconjugate Chem., 22, 2332-2338, 2011.12.
68. H. Abe, M. Goto, N. Kamiya, Protein lipidation catalyzed by microbial transglutaminase, Chem. Eur. J., 17, 14004-14008, 2011.12.
69. Y. Mori, K. Minamihata, H. Abe, M. Goto, N. Kamiya, Protein assemblies by site-specific avidin-biotin interactions, Org. Biomol. Chem., 9, 5641-5644, 2011.05.
70. Y. Mori, M. Goto, N. Kamiya, Transglutaminase-mediated internal protein labeling with a designed peptide loop, Biochem. Biophys. Res. Commun., 410, 829-833, 2011.05.
71. T. Niide, M. Goto, N. Kamiya, Biocatalytic synthesis of gold nanoparticles with cofactor regeneration in recombinant Escherichia coli cells, Chem. Commun., 47, 7350-7352, 2011.05.
72. K. Moriyama, K. Sung, M. Goto, N. Kamiya, Immobilization of alkaline phosphatase on magnetic particles by site-specific and covalent cross-linking catalyzed by microbial transglutaminase, J. Biosci. Bioeng., 111, 650-653, 2011.04.
73. K. Minamihata, M. Goto, N. Kamiya, Site-specific protein cross-linking by peroxidase-catalyzed activation of a tyrosine-containing peptide tag, Bioconjugate Chem., 22, 74-81, 2011.04.
74. M. Kitaoka, Y. Tsuruda, Y. Tanaka, M. Goto, M. Mitsumori, K. Hayashi, Y. Hiraishi, K. Miyawaki, S. Noji, N. Kamiya, Transglutaminase-mediated synthesis of a novel DNA-(enzyme)n probe for highly sensitive DNA detection, Chem. Eur. J., 19, 5387-5392, 2011.03, 生体内ではほとんどのタンパク質が何らかの翻訳後修飾を受けることに着目し、翻訳後修飾過程で働く酵素の基質特異性を利用すれば、狙った部位でタンパク質を修飾できると考えた。従来の有機化学的手法では、タンパク質の狙った部位を選択的に修飾するのは極めて困難であった。そこでラベル化したい有機分子内に基質となる部位(酵素の認識部位)を設計し、これを糊代として利用することで、糊代選択的な生体分子の連結・修飾法を確立した。
既往の方法ではDNAとタンパク質を1:1で連結することしかできなかったが、DNAを構成する分子を酵素の基質となるように設計し、DNA-(タンパク質)n型の新規ハイブリッド分子を高収率で得る技術を確立し、新たな遺伝子検出システムを提案した。.
75. K. Sung, N. Kamiya,* N. Kawata, S. Kamiya and M. Goto, Functional glass surface displaying a glutamyl donor substrate for transglutaminase-mediated protein immobilization, Biotechnol. J., 46, 456-462, 2010.06.
76. Yoshiro TAHARA, Kenichi NAMATSU, Noriho KAMIYA, Masayori HAGIMORI, Shinji KAMIYA, Masayuki ARAKAWA, Masahiro GOTO, Transcutaneous immunization by a solid-in-oil nanodispersion, Chem. Commun., 46, 9200-9202, 2010.06.
77. Hiroki Abe, Masahiro GOTO, Noriho KAMIYA, Enzymatic single-step preparation of multifunctional proteins, Chem. Commun., 46, 7160-7162, 2010.05.
78. M. Moniruzzaman, Y. Tahara, M. Tamura, N. Kamiya, M. Goto, Ionic liquid-assisted transdermal delivery of sparingly soluble drugs, Chem. Commun., 46, 1452-1454, 2010.01.
79. N. Kamiya,* H. Abe, M. Goto, Y. Tsuji, H. Jikuya, Fluorescent substrates for covalent protein labeling catalyzed by microbial transglutaminase, Org. Biomol. Chem., 7, 3407-3412, 2009.08.
80. K. Nakashima, N. Kamiya, D. Koda, T. Maruyama, M. Goto, Enzyme encapsulation in microparticles composed of polymerized ionic liquids for highly active and reusable biocatalysts, Org. Biomol. Chem., 7, 2353-2358, 2009.07.
81. N. Kamiya,* Y. Shiotari, M. Tokunaga, H. Matsunaga, H. Yamanouchi, K. Nakano, M. Goto, Stimuli-responsive nanoparticles composed of naturally occurring amphiphilic proteins, Chem. Commun., 5287-5289, 2009.08.
82. M.M.Zaman, N. Kamiya, M. Goto, Biocatalysis in Water-in-Ionic Liquid Microemulsions: A Case Study with Horseradish Peroxidase, Langmuir, 25, 977-982, 2009.04.
83. K. Minamihata, N. Kamiya,* S. Kiyoyama, H. Sakuraba, T. Ohshima, M. Goto, Development of a novel immobilization method for enzymes from hyperthermophiles, Biotechnol. Lett., 31, 1037-1041, 2009.07.
84. T. Mouri, T. Shimizu, N. Kamiya,* H. Ichinose, M. Goto*, Design of a cytochrome P450BM3 reaction system linked by two-step cofactor regeneration catalyzed by a soluble transhydrogenase and glycerol dehydrogenase, Biotechnol. Prog., 25, 1372-1378, 2009.10.
85. H. Yoshiura, M. Hashida, N. Kamiya, M. Goto, Factors affecting protein release behavior from surfactant-protein complexes under physiological conditions., Int. J. Pharm., 338, 174-179 (2007), 2007.07.
86. H. Piao, N. Kamiya, A. Hirata, T. Fujii, I. Shimizu, S. Ito, M. Goto, Reduction of gastric ulcerogenicity during multiple administration of diclofenac sodium by a novel solid-in-oil suspension., Pharm. Devel. Technol., vol.12, 321-325 (2007), 2008.07.
87. N. Kamiya, S. Doi, Y. Tanaka, H. Ichinose, M. Goto, Functional immobilization of recombinant alkaline phosphatases bearing a glutamyl donor substrate peptide of microbial transglutaminase, J. Biosci. Bioeng., 104, 195-199, 2007.09.
88. Y. Tanaka, Y. Tsuruda, M. Nishi, N. Kamiya, M. Goto, Exploring enzymatic catalysis at a solid surface: a case study with transglutaminase-mediated protein immobilization, Org. Biomol. Chem., 5, 1764-1770, 2007.05.
89. J. Tominaga, N. Kamiya, M. Goto, An enzyme-labeled protein polymer bearing pendant haptens, Bioconjugate Chem., 18, 860-865, 2007.03.
90. T. Maruyama, Y. Shimada, H. Matsushita, N. Kamiya, M. Goto, Proteins and protein-rich biomass as environmental-friendly adsorbents selective for precious metal ions, Env. Sci. Technol., 41, 1359-1364, 2007.02.
91. J. Tominaga, Y. Kemori, Y. Tanaka, T. Maruyama, N. Kamiya, M. Goto, An enzymatic method for site-specific labeling of recombinant proteins with oligonucleotides, Chem. Commun., 401-403, 2007.01.
92. K.Shimojo, K.Nakashima, N.Kamiya, M.Goto, Crown-ether mediated extraction and functional conversion of cytochrome c in ionic liquids, Biomacromolecules, vol.7, 2-5 (2006), 2006.10.
93. T.Mouri, J.Michizoe, H.Ichinose, N.Kamiya, M.Goto, A recombinant Escherichia coli whole cell biocatalyst harboring a cytochrome P450cam monooxygenase system coupled with enzymatic cofactor regeneration, Appl. Microbiol. Biotechnol., vol.72, 514-520 (2006), 2006.04.
94. T.Mouri, N.Kamiya, M.Goto, Increasing the catalytic performance of a whole cell biocatalyst harboring a cytochrome P450cam system by stabilization of an electron transfer component, Biotechnol. Lett., vol.28, 1509-1513 (2006), 2006.05.
95. T. Maruyama, T. Shinohara, T. Hosogi, H. Ichinose, N. Kamiya, M. Goto, Masking oligonucleotides improve sensitivity of mutation detection based on guanine quenching, Anal. Biochem., vol.354, 8-14 (2006), 2006.07.
96. K. Shimojo, N. Kamiya, F. Tani, H. Naganawa, Y. Naruta, M. Goto, Extractive Solubilization, Structural Change and Functional Conversion of Cytochrome c in Ionic Liquids via Crown Ether Complexation, Anal. Chem., vol.78, 7735-7742 (2006), 2006.10.
97. H. Piao, N. Kamiya, J. Watanabe, H. Yokoyama, A. Hirata, T. Fujii, I. Shimizu, S. Ito, M. Goto, Oral delivery of diclofenac sodium using a novel solid-in-oil suspension, Int. J. Pharm., vol.313, 159-162 (2006) , 2006.11.
98. K. Nakashima, T. Maruyama, N. Kamiya, M. Goto, Homogeneous Enzymatic Reaction in Ionic Liquids with Poly(ethylene glycol)-Modified Subtilisin, Org. Biomol. Chem., vol.4, 3462-3467 (2006), 2006.10.
99. K. Nakashima, T. Maruyama, N. Kamiya, M. Goto, Activation of lipase in ionic liquids by modification with comb-shaped poly(ethylene glycol), Sci. Technol. Adv. Mater., vol.7, 692-698 (2006), 2007.01.
100. J. Tominaga, N. Kamiya, S. Doi, H. Ichinose, T. Maruyama, M. Goto, Design of a specific peptide tag that affords covalent and site-specific enzyme immobilization catalyzed by microbial transglutaminase, Biomacromolecules, 10.1021/bm050193o, 6, 4, 2299-2304, vol.6, 2299 -2304 (2005), 2005.01.
101. N.Kamiya, S.Doi, J.Tominaga, H.Ichinose, M.Goto, Transglutaminase-mediated protein immobilization to casein nanolayers created on a plastic surface, Biomacromolecules, 10.1021/bm0494895, 6, 1, 35-38, 6, 35-38 (2005), 2005.01.
102. T.Tanaka, N. Kamiya, T.Nagamune, N-terminal glycine-specific protein conjugation catalyzed by microbial transglutaminase, FEBS Letter, 10.1016/j.febslet.2005.02.064, 579, 10, 2092-2096, vol.579, 2092-2096 (2005), 2005.01.
103. H.Ichinose, J.Michizoe, T.Maruyama, N.Kamiya, M.Goto, Electron transfer reaction and functionalization of P450cam system in reverse micelles, Langmuir, 10.1021/la049752n, 20, 13, 5564-5568, vol.20, 5564-5568 (2004), 2004.01.