|Noriho Kamiya||Last modified date：2018.06.08|
Professor / Department of Applied Chemistry / Faculty of Engineering
|Noriho Kamiya||Last modified date：2018.06.08|
|1.||Uju, Agung Tri Wijayanta, Masahiro Goto, Noriho Kamiya, High yield hydrolysis of seaweed-waste biomass using peracetic acid and ionic liquid treatments, 3rd International Conference on Industrial Mechanical, Electrical, and Chemical Engineering, ICIMECE 2017, 2018.02, Seaweed is one of the most promising bioethanol feedstocks. This water plant has high carbohydrate content but low lignin content, as a result it will be easier to be hydrolysed. This paper described hydrolysis of seaweed-waste biomass from the carrageenan (SWBC) industry using enzymatic saccharification or ionic liquids-HCl hydrolysis. In the first work, SWBC pretreated by peracetic acid (PAA) followed by ionic liquid (IL) caused enhance the cellulose conversion of enzymatic saccharification. At 48h saccharification, the value conversion almost reached 100%. In addition, the untreated SWBC also produced the cellulose conversion 77%. In the second work, SWBC or Bagasse with or without pretreated by PAA was hydrolyzed using ILs-HCl hydrolysis. The ILs used were 1-buthyl-3-methylpyridium chloride, [Bmpy][Cl] and 1-butyl-3-metyl imidazolium chloride ([Bmim][Cl]). [Bmpy][Cl]-HCl hydrolysis produced higher cellulose conversion than [Bmim][Cl]-HCl hydrolysis. The phenomenon was clearly observed on the Bagasse, which without pretreated by PAA. Furthermore, SWBC hydrolyzed by both ILs in the presence low concentration of HCl produced cellulose conversion 70-98% at 60-90 min of hydrolysis time. High cellulose conversion of SWBC on the both hydrolysis was caused by SWBC had the low lignin (4%). Moreover, IL treatments caused lowering of cellulose hydrogen bonds or even changed the cellulose characteristics from cellulose I to cellulose II which easily to be hydrolyzed. In the case of [Bmpy][Cl], this IL may reduce the degree polymerization of celluloses..|
|2.||Noriho Kamiya, Enzyme-mediated fabrication of functional bioconjugates and biomaterials, IGER International Symposium on Cell Surface Structures and Functions 2017, 2017.11.|
|3.||Noriho Kamiya, Biocatalyst Engineering toward Biomedical Applications, ACB (Asian Congress on Biotechnology) 2017, 2017.07.|
|4.||Noriho Kamiya, Enzyme-mediated Design of Functional Bioconjugates and Biomaterials, 2017 BEST Conference, 2017.06.|
|5.||Noriho Kamiya, Mari Takahara, Rie Wakabayashi, Masahiro Goto, Design of novel biocatalysts by enzymatic biomolecular conjugation, The 9th AFOB Regional Symposium (ARS 2017), 2017.02.|
|6.||神谷 典穂, 南畑 孝介, Enzymatic Conjugation Strategy for the Design of Artificial Biomolecular Assemblies, 2016 AIChE Annual Meeting, 2016.11.|
|7.||神谷 典穂, Exploring biological strategies for sustainable utilization of lignocellulosic biomass, The e-ASIA Joint Research Program (e-ASIA JRP) Project Workshop, 2016.09.|
|8.||Rie Wakabayashi, Ayumi Suehiro, Masahiro Goto, Noriho Kamiya, Enzyme-mediated assembly of biomolecules on a designer scaffold based on self-assembled peptides, The 2015 International Chemical Congress of Pacific Basin Societies (Pacifichem), 2015.12.|
|9.||Mari Takahara, Yutaro Mori, Budinova Geisa A.L.G., Hikaru Nakazawa, Mitsuo Umezu, Noriho Kamiya, Design of an artificial cellulase with cellulose-binding DNA aptamer, The 2015 International Chemical Congress of Pacific Basin Societies (Pacifichem), 2015.12.|
|10.||神谷 典穂, One-dimensional assembly of functional proteins by avidin-biotin interaction, Asian Congress on Biotechnology (ACB) 2015, 2015.11.|
|11.||Ayumi Suehiro, Rie Wakabayashi, Masahiro Goto, Noriho Kamiya, Supramolecular Peptide Scaffold for an Enzymatic Assembly of Functional Molecules, The 28th International Symposium on Chemical Engineering (ISChE 2015), 2015.12.|
|12.||Takuji Kawanami, Rie Wakabayashi, Masahiro Goto, Noriho Kamiya, Enzymatic Strategy for Lipidization of Functional Proteins, The 28th International Symposium on Chemical Engineering (ISChE 2015), 2015.12.|
|13.||神谷 典穂, Design of biomolecular assemblies by enzymatic protein manipulation, NANO KOREA 2015, 2015.07.|
|14.||神谷 典穂, Molecular design of biocatalytic assemblies for sustainable biotechnological applications, ARS 2015, 2015.05.|
|15.||神谷 典穂, Potential use of oxidoreductases for the fabrication of biomaterials, Active Enzyme Molecule 2014, 2014.12.|
|16.||神谷 典穂, Enzyme as a Catalytic Tool for Fabrication of Biomaterials, The 13th CJK Symposium on Enzyme Engineering, 2014.11.|
|17.||神谷 典穂, Self-sacrificial display of an active protein on gold nanoparticles, YABEC 2014, 2014.11.|
|18.||神谷 典穂, ENZYMATIC APPROACHES FOR ACCELERATING CELLULOSIC BIOMASS HYDROLYSIS, 16th International Biotechnology Symposium and Exhibition - IBS 2014, 2014.09.|
|19.||神谷 典穂, Enzyme as a catalytic tool for designing new bioconjugates, 2014 BEST Conference, 2014.06, Proteins exhibit multiple roles in living systems. In particular, enzymes facilitate metabolic pathways by catalyzing the different types of chemical reactions to sustain our life. A variety of enzyme functions have been exploited in both biochemical studies and biotechnological applications, however, there has still been a room for applying biocatalysis for the design and creation of artificial biomaterials.
In natural biological systems, proteins often form well-organized higher-order structures that associate unique functions, which cannot be accessed by a single protein unit alone. Interestingly, enzymatic post-translational modification of protein building blocks plays an important role in the formation of multi-subunit macromolecular structures.
Inspired by nature’s strategy, we are interested in configuring biocatalysis for creating new functional biomaterials. Herein, I’ll introduce our strategies which will be exemplified by three different types of enzymes (microbial trasnglutaminase, horseradish peroxidase, and glycerol dehydrogenase) to create (nano)biomaterials with distinct functions in line with their possible applications..
|20.||神谷 典穂, Biomolecular Assembly by Enzymatic Conjugation and Scaffolding, 2013 KSBB Spring Meeting and International Symposium, 2014.04.|
|21.||神谷 典穂, Protein assembly design by enzymatic conjugation and scaffolding, 化学工学会第79年会（国際セッション）, 2014.03.|
|22.||神谷 典穂, Assembling enzymes on a DNA scaffold for Biotechnological Applications, Asian Congress on Biotechnology (ACB-2013), 2013.12.|
|23.||神谷 典穂, Substrate engineering for enzymatic site-specific and covalent modification of functional proteins, Enzyme Engineering XXII: Emerging Topics in Enzyme Engineering, 2013.09.|
|24.||神谷 典穂, Protein Supramolecular Complex Formation by Site-specific Protein Interactions and Scaffolding, IGER International Symposium on Cell Surface Structures and Functions, 2013.09, Proteins are biomacromolecules exhibiting multiple roles in living systems. A variety of protein functions have proven to be valuable in both biochemical studies and biotechnological applications. In natural biological systems, proteins often form well-organized higher-order structures that associate unique functions, which cannot be accessed by a sole protein unit. In the formation of multi-subunit protein polymers such as cell-surface pili in gram-positive bacteria, self-assembly of protein building blocks plays an important role, and interestingly, post-translational modification also facilitates the growth and stabilization of proteinaceous polymeric structures by introducing covalent bonds at specific sites of protein subunits.
Toward designer protein supramolecular complexes (PSCs), ordered protein assemblies have been designed by either site-specific ligand-receptor interaction or site-specific protein labeling onto a scaffold molecule based on a transglutaminase-catalyzed post-translational, site-specific protein modification technique with artificial substrates. For the former, strong and specific molecular interaction between a natural receptor protein, streptavidin (SA), and its small molecular ligand, biotin, was selected. By using a dimeric Escherichia coli alkaline phosphatase (AP) as a symmetric protein building block, we evaluated how the avidin-biotin interaction sites between protein units affect the formation of PSCs composed of AP and SA. For the latter, we have selected nucleic acid as a polymeric scaffold, and created novel DNA- and RNA-(enzyme)n conjugate, a nucleic acid-enzyme hybrid with 1:n stoichiometry. Our challenge for cellulosomal design with a nucleic acid scaffold will be also presented. .
|25.||神谷 典穂, Development of New Biomolecular Conjugation Techniques and Their Applications, YABEC 2013, 2013.08.|
|26.||森 裕太郎, Rie Wakabayashi, Masahiro Goto, 神谷 典穂, Fabrication of higher-order protein supramolecular complexes, IGER International Symposium on Cell Surface Structures and Functions, 2013.09.|
|27.||神谷 典穂, Manipulating biomolecules through enzymatic post-translational protein modification, 2013 KMB's 40th Anniversary International Symposium "Recent Breakthroughs in Microbial Biotechnology: From Bench to Industry", 2013.07, Site-specific modification of proteins with a variety of organic molecules represents a valuable approach to obtain biologically active and homogeneous protein formulations. In particular, site-specific and covalent protein manipulation catalyzed by enzymes that function in post-translational modifications is practical because enzymatic transformations offer high substrate specificity under protein-friendly conditions. Recombinant proteins tagged with a short peptide, which can be post-translationally modified by a specific enzyme, have been successfully employed for this purpose.
Our group has focused on the utility of microbial transglutaminase (MTG) from Streptomyces mobaraensis in biotechnology. Transglutaminase is an enzyme that catalyzes covalent bond formation between the side chains of specific Gln and Lys residues of target peptides and proteins in post-translational modification process. By combining simple chemistry and MTG-catalyzed reaction, we have demonstrated site-specific protein conjugation with genetically introduced substrate peptide tags, site-specific protein immobilization to solid surfaces and site-specific protein labeling with new chemical entities. The basic concept has recently been extended to enzymatic conjugation of functional proteins with oligonucleotides, DNA and RNA. We are also interested in the use of oxidoreductases for enzymatic manipulation of biomolecules. Our recent efforts on biofabrication of a range of unique proteinaceous materials will be presented. .
|28.||神谷 典穂, Momoko Kitaoka, Kounosuke Hayashi, A novel methodology for multiple enzyme labeling on nucleic acid scaffolds, 12th Japan-China-Korea Joint Symposium on Enzyme Engineering, 2012.05.|
|29.||神谷 典穂, Hiroki Abe, Masahiro Goto, Controlling protein localization by enzymatic protein lipidation, YABEC 2012, 2012.10.|
|30.||神谷 典穂, 中元亜耶, Uju, Masahiro Goto, Chiaki Ogino, Nobuhiro Ishida, Potential of pyridinium ionic liquids in a cellulosic biomass pretreatment process, 15th International Biotechnology Symposium and Exhibition, 2012.09.|
|31.||神谷 典穂, Designing biocatalysis for protein engineering through enzymatic post-translational modification
, The 2nd International Conference on Molecular and Functional Catalysis, 2012.07.
|32.||Nobuiro Ishida, Satoshi Katahira, Wataru Tokuhara, Yoshiyuki Noritake, Noriho Kamiya, Kazunori Nakashima, Chiaki Ogino, Akihiko Kondo, Development of ionic liquid-based consolidated bioprocessing (i-CBP) for bioethanol production, 2011 AIChE Annual Meeting, 11AIChE, 2011, Lignocellulose that is the primary polysaccharide of plant cell wall has been received considerable attention as a main feedstock for bio-refinery process such as bio-fuel production. The enzymatic hydrolysis of lignocellulose to soluble sugars is considered to be one of the environmental friendly processes for bio-ethanol production. But the spontaneous crystallization of cellulose due to the chemical uniformity of glucose and high degree of hydrogen bonding can form densely packed micro-fibrils which are inaccessible to cellulolytic enzymes. Therefore, efficient and cost-effective methods for the degradation and fermentation of lignocellulosic biomass to ethanol are required. In this study, for deconstruction of biomass, the ionic liquid was used as a pre-treatment medium, and the effective degradation and assimilation procedure was investigated. This effective process has been named as 'Ionic liquid-based Consolidated Bio-Processing (i-CBP)'. In this process, pretreated biomass by ionic liquids would be easily hydrolyzed to glucose and directly converted to ethanol by functional transgenic yeasts that were simultaneously displayed four kinds celluloses, endoglucase (EG), cellobiohydrolase (CBH I & II), and beta-glucosidase (BGL) on the cell surface. Research findings from these studies will be presented..|