| 1. |
Islam R, Nabila FH, Wakabayashi R, Kamiya N, Moniruzaman M, Goto M, Formulation, Characterization, and Evaluation of Ionic Liquid-Based Transdermal Patch for Enhanced Delivery of Sparingly Soluble Drug, IChES2024, 2024.03. |
| 2. |
Rizfi Fariz Pari, Uju, Wahyu Ramadhan, Safrina Dyah Hardiningtyas, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Amorphous Cellulose Nanofiber from Green Seaweed Ulva lactuca Prepared with Deep Eutectic Solvent Pretreatment, International Chemical Engineering Symposia 2024, 2024.03. |
| 3. |
Diah Anggraini Wulandari, Kyosuke Tsuru, Kosuke Minamihata, Rie Wakabayashi, Masahiro Goto, and Noriho Kamiya, A functional hydrogel bead-based high-throughput screening system for mammalian cells with enhanced secretion of therapeutic antibodies, International Chemical Engineering Symposia 2024, 2024.03. |
| 4. |
Ingram Tan, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Enhancing Cellular Uptake of Nucleic Acid Drug by Co-assembly of Peptide Amphiphile, 104th CSJ annual meeting, 2024.03. |
| 5. |
Noriho Kamiya, Biocatalysis for Biomolecular and Biomaterials engineering, The 9th International Symposium on Applied Chemistry & The 5th International Conference on Chemical & Material Engineering (ISAC-ICCME 2023), 2023.12. |
| 6. |
Rizfi Fariz Pari, Uju, Wahyu Ramadhan, Safrina Dyah Hardiningtyas3, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, The Effect of Deep Eutectic Solvent Pretreatment on Seaweed Cellulose for Cellulose Nanofiber Formation, The 9 th International Symposium on Applied Chemistry 2023, 2023.12. |
| 7. |
Kensei Orita, Yui Okawa, Ryota Tokuo, Kousuke Minamihata, Noriho Kamiya, Fluorescently stained hydrogel beads for construction of a high-throughput screening system of laccase, The 34th International Symposium on Chemical Engineering(ISChE 2023), 2023.12. |
| 8. |
西岡莉子、飯田龍哉、南畑孝介、佐藤崚、木村道夫、神谷典穂, Preparation of antibody-drug conjugates by protein crosslinking enzyme fused with an antibody-binding protein, The 34th International Symposium on Chemical Engineering, 2023.12. |
| 9. |
Noe INOMOTO, Masahiro Tominaga, Yoichiro Ito, Jun Ishii, Akihiko Kondo, Noriho Kamiya, Development of antibody binding protein-immobilized functional microhydrogels with cell sorting ability, The 34th International Symposium on Chemical Engineering (ISChE 2023)), 2023.12. |
| 10. |
Kazuki Uchida, Rie Wakabayashi, Masahiro Goto, Naofumi Shimokawa, Masahiro Takagi, Noriho Kamiya , Artificial lipidation of proteins controls protein dynamics on lipid membranes , The 34th International Symposium on Chemical Engineering, 2023.12. |
| 11. |
豊福淳大、若林里衣、神谷典穂、後藤雅宏, Non-invasive transdermal delivery of nucleic acid drugs with biocompatible ionic liquids, The 34th International Symposium on Chemical Engineering (ISChE 2023), 2023.12. |
| 12. |
Keisuke Tanaka, Kosuke Minamihata, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Development of a non-invasive malaria vaccine and analysis of the immune mechanism, ISChE2023, 2023.12. |
| 13. |
Ingram Tan, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Peptide Amphiphile Co-assembly Facilitated Direct Cellular Delivery of Antisense Oligonucleotides, international symposium on chemical engineering, 2023.12. |
| 14. |
東智大、豊福淳大、若林里衣、神谷典穂、後藤雅宏, Development of transdermal delivery technology for mRNA drugs using ionic liquids, International Symposium on Chemical Engineering, 2023.12. |
| 15. |
Yamaguchi Kyohei, Wakabayashi Rie, Kamiya Noriho, Goto Masahiro, Effect of hydrophobic portions of antigen-modified peptide assemblies on immune cell activation, ISChE2023, 2023.12. |
| 16. |
長谷彩沙、南畑孝介、若林里衣、後藤雅宏、神谷典穂, Hybrid protein crystal formation mediated by the interaction of positively charged peptide tags and oligo ssDNAs, The 34th International Symposium on Chemical Engineering, 2023.12. |
| 17. |
難波江友紀、樋口亜也斗、若林里衣、神谷典穂、後藤雅宏, Creation of Vaccine Adjuvants Using Antigenic Protein Modified Peptide Assemblies, The 34rd International Symposium on Chemical Engineering (ISChE 2023), 2023.12. |
| 18. |
豊福淳大、若林里衣、神谷典穂、後藤雅宏, Transdermal delivery of nucleic acid drugs using biocompatible ionic liquid, The 25th Joint Seminar of the Busan Branch of the Korean Chemical Society (KCS) and the Kyushu Branch of the Chemical Society of Japan (CSJ), 2023.11. |
| 19. |
Kazuki Uchida, Rie Wakabayashi, Masahiro Goto, Naofumi Shimokawa, Masahiro Takagi, Noriho Kamiya , Artificial protein lipidation and its dynamics on lipid membranes , The 16th Asian Congress on Biotechnology (ACB), 2023.10. |
| 20. |
Keisuke Tanaka, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Creation of a non-invasive malaria vaccine and elucidation of the immune mechanism, ACB2023, 2023.10. |
| 21. |
Noriho Kamiya, Ryutaro Ariyoshi, Takashi Matsuzaki, Ryo Sato, Kosuke Minamihata, Konosuke Hayashi, Rie Wakabayashi, Masahiro Goto, Design of engineered active zymogen of microbial transglutaminase, Enzyme Engineering XXVII, 2023.10. |
| 22. |
Noriho Kamiya, Riko Nishioka, Ryuya Iida, Kosuke Minamihata, Michio Kimura, Engineered Active Zymogen of Microbial Transglutaminase for Antibody-Drug Conjugation, The 16th Asian Congress on Biotechnology (ACB2023), 2023.10. |
| 23. |
Keisuke Tanaka, Kosuke Minamihata, Rie Wakabayashi, Noriho Kamiya, Masahiro Goto, Creation of transdermal malaria vaccine and analysis of immune response, YABEC 2023 Symposium, 2023.07. |
| 24. |
Kazuki Uchida, Rie Wakabayashi, Masahiro Goto, Naofumi Shimokawa, Masahiro Takagi, Noriho Kamiya, Lipid moieties affect the dynamics of lipid-modified proteins on lipid membranes , 2023 BEST Joint YABEC International Symposium, 2023.07. |
| 25. |
Noriho Kamiya, Hendra Saputra, Pugoh Santoso, Rie Wakabayashi, Toki Taira, Design of Lipid-based Bioconjugates with Antifungal Activity, Young Asian Biological Engineer’s Community (YABEC) 2023, 2023.07. |
| 26. |
Noriho Kamiya, Rie Wakabayashi, Toki Taira, Enzymatic Protein Lipidation for Biomolecular Engineering at Biointerfaces, The 14th AFOB Regional Symposium (ARS 2023), 2023.04. |
| 27. |
＠Noriho Kamiya, Wahyu Ramadhan, Kosuke Minamihata, Rie Wakabayashi, Uju and Masahiro Goto, Functional modulation of biopolymers by biocatalysts: from bioconjugation to sustainable bioproduction, The 15th Asian Congress on Biotechnology (ACB 2022), 2022.10. |
| 28. |
＠Noriho Kamiya, Artificial Lipidation for Biomolecular Engineering at Biointerfaces, 2022 KSBB (Korean Society for Biotechnology and Bioengineering) Fall Meeting and International Symposium, 2022.09. |
| 29. |
Pugoh Santoso, Kosuke Minamihata, Yugo Ishimine, Hiromasa Taniguchi, Ryo Sato, Masahiro Goto, Tomoya Takashima, Toki Taira, Noriho Kamiya, Synergistic antifungal activity by combining Amphotericin B with lipidated chitinase, APCChE 2022, 2022.08. |
| 30. |
＠Noriho Kamiya, Enzymatic Protein Lipidation for Biomolecular Engineering at Biointerfaces, The 13th AFOB Regional Symposium (ARS 2022) Taiwan series, 2022.06. |
| 31. |
＠Noriho Kamiya, Biomolecular engineering with microbial transglutaminase, European Society of Applied Biocatalysis (ESAB) Webinar ‘Enzyme Engineering’, 2022.02. |
| 32. |
＠Noriho Kamiya, Enzymatic manipulation of protein assemblies that function at biointerface, PacificChem2021, 2021.12. |
| 33. |
＃内田 和希、＃大林 洋貴、＠南畑 孝介、＠若林 里衣、＠後藤 雅宏、＠下川 直史、＠高木 昌宏、＠神谷 典穂, Selective Anchoring Behavior of Artificial Lipid-modified Proteins on Lipid Membrane Domains, The 26th Symposium of Young Asian Biological Engineers’ Community (YABEC2021), 2021.11. |
| 34. |
Noriho Kamiya, Design of Bioconjugates that Function at Biological Interface, The Korean Society for Biotechnology and Bioengineering (KSBB) 2021 International Symposium, 2021.04. |
| 35. |
Pugoh Santoso, Takuya Komada, Hiromasa Taniguchi, Yugo Ishimine, Ryo Sato, Kosuke Minamihata, Tomoya Takashima, Toki Taira, Noriho Kamiya, Synergistic Antifungal Action of Lipid-Modified Chitinase With Amphotericin-B, International Chemical Engineering Symposia 2021, 2021.03. |
| 36. |
D. Permana, K. Minamihata, R. Sato, R. Wakabayashi, M. Goto, N. Kamiya, Formation of Linear Protein Polymer by Controlling Enzymatic Cross-linking Reaction with a Tyrosine-containing Loop Peptide, The 12th Asian Federation of Biotechnology (AFOB) Regional Symposium 2020, 2020.02. |
| 37. |
W. Ramadhan, G. Kagawa, K. Moriyama, R. Wakabayashi, K. Minamihata, M. Goto and N. Kamiya., A ‘cellular furoshiki’ strategy for the construction of higher-order cellular architecture by using redox-responsive hydrogel, The 12th Asian Federation of Biotechnology (AFOB) Regional Symposium 2020, 2020.02. |
| 38. |
R. Sato, K. Minamihata, M. Goto, N. Kamiya, Single peptide-tag specific assembly of functional proteins by enzymatic crosslinking reaction, The 32nd International symposium on Chemical Engineering, 2019.12. |
| 39. |
Noriho Kamiya, Biomolecular engineering for sustainable production of designer functional proteins, The 10th Symposium on Innovative Bioproduction Taichung (iBioT2019), 2019.11. |
| 40. |
Noriho Kamiya*, Dani Permana, Wahyu Ramadhan, Kosuke Minamihata, Masahiro Goto, Biomolecular engineering by oxidative enzymatic manipulation, The 25th Young Asian Biological Engineer’s Community 2019, 2019.11. |
| 41. |
Noriho Kamiya, Biomolecular engineering by biocatalysis for designer bio-based functional materials, International Symposium of Innovative Bio-production Indonesia on Biotechnology & Bioengineering (ISIBio2019), 2019.10. |
| 42. |
T. KOMADA, M. Alif RAZI, M. TAKAHARA, R. WAKABAYASHI, M. GOTO, N. KAMIYA, Enzymatic preparation of lipid-modified proteins and their use for the decoration of liposome, 18th Asian Pacific Confederation of Chemical Engineering Congress (APCChE 2019), 2019.09. |
| 43. |
Y. Ohama, K. Minamihata, R. Wakabayashi, M. Goto, N. Kamiya, Cell-free protein synthesis inside liquid marbles toward molecular evolution, 18th Asian Pacific Confederation of Chemical Engineering Congress (APCChE 2019), 2019.09. |
| 44. |
Noriho Kamiya*, Kosuke Minamihata, Biomolecular engineering toward sustainable production of value-added functional proteins, 18th Asian Pacific Confederation of Chemical Engineering Congress (APCChE 2019), 2019.09. |
| 45. |
Noriho Kamiya, Enzymatic biomolecular engineering toward designer bioconjugates and biomaterials, The 14th Asian Congress on Biotechnology (ACB 2019), 2019.07. |
| 46. |
Rie Wakabayashi, Hiroki Obayashi, Noriho Kamiya, Masahiro Goto, Complemantary interaction with peptide amphiphiles guided the intracellular delivery of small molecular drugs, The 24th Symposium of Young Asian Biological Engineers' Community (YABEC2018), 2018.11. |
| 47. |
Noriho Kamiya, Takashi Matsuzaki, Ryo Sato, Kounosuke Hayashi, Rie Wakabayashi, Kosuke Minamihata, Engineered active zymogen of microbial transglutaminase, The 15th Japan-China-Korea Joint Symposium on Enzyme Engineering, 2018.07. |
| 48. |
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.. |
| 49. |
Noriho Kamiya, Enzyme-mediated fabrication of functional bioconjugates and biomaterials, IGER International Symposium on Cell Surface Structures and Functions 2017, 2017.11. |
| 50. |
Noriho Kamiya, Biocatalyst Engineering toward Biomedical Applications, ACB (Asian Congress on Biotechnology) 2017, 2017.07. |
| 51. |
Noriho Kamiya, Enzyme-mediated Design of Functional Bioconjugates and Biomaterials, 2017 BEST Conference, 2017.06. |
| 52. |
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. |
| 53. |
神谷 典穂, 南畑 孝介, Enzymatic Conjugation Strategy for the Design of Artificial Biomolecular Assemblies, 2016 AIChE Annual Meeting, 2016.11. |
| 54. |
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. |
| 55. |
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. |
| 56. |
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. |
| 57. |
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. |
| 58. |
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. |
| 59. |
神谷 典穂, One-dimensional assembly of functional proteins by avidin-biotin interaction, Asian Congress on Biotechnology (ACB) 2015, 2015.11. |
| 60. |
神谷 典穂, Design of biomolecular assemblies by enzymatic protein manipulation, NANO KOREA 2015, 2015.07. |
| 61. |
神谷 典穂, Molecular design of biocatalytic assemblies for sustainable biotechnological applications, ARS 2015, 2015.05. |
| 62. |
神谷 典穂, Potential use of oxidoreductases for the fabrication of biomaterials, Active Enzyme Molecule 2014, 2014.12. |
| 63. |
神谷 典穂, Enzyme as a Catalytic Tool for Fabrication of Biomaterials, The 13th CJK Symposium on Enzyme Engineering, 2014.11. |
| 64. |
神谷 典穂, Self-sacrificial display of an active protein on gold nanoparticles, YABEC 2014, 2014.11. |
| 65. |
神谷 典穂, ENZYMATIC APPROACHES FOR ACCELERATING CELLULOSIC BIOMASS HYDROLYSIS, 16th International Biotechnology Symposium and Exhibition - IBS 2014, 2014.09. |
| 66. |
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.. |
| 67. |
神谷 典穂, Biomolecular Assembly by Enzymatic Conjugation and Scaffolding, 2013 KSBB Spring Meeting and International Symposium, 2014.04. |
| 68. |
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. |
| 69. |
神谷 典穂, Assembling enzymes on a DNA scaffold for Biotechnological Applications, Asian Congress on Biotechnology (ACB-2013), 2013.12. |
| 70. |
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. |
| 71. |
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. |
| 72. |
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.[1] 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.[2] Our challenge for cellulosomal design with a nucleic acid scaffold will be also presented.[3] . |
| 73. |
神谷 典穂, Development of New Biomolecular Conjugation Techniques and Their Applications, YABEC 2013, 2013.08. |
| 74. |
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. . |
| 75. |
神谷 典穂, Hiroki Abe, Masahiro Goto, Controlling protein localization by enzymatic protein lipidation, YABEC 2012, 2012.10. |
| 76. |
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. |
| 77. |
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. |
| 78. |
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. |
| 79. |
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, 2011.11, 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.. |
