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Volumn 2014, Issue , 2014, Pages

Manufacturing economics of plant-made biologics: Case studies in therapeutic and industrial enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CELLULASE; CHOLINESTERASE; INDUSTRIAL ENZYME; BIOFUEL; BIOLOGICAL PRODUCT; RECOMBINANT PROTEIN;

EID: 84902176028     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2014/256135     Document Type: Article
Times cited : (142)

References (51)
  • 4
    • 84892908874 scopus 로고    scopus 로고
    • Production of recombinant antigens and antibodies in Nicotiana benthamiana Using "magnifection" technology: GMP-compliant facilities for small- and large-scale manufacturing
    • Klimyuk V., Herz S., Butler J., Haydon H., Production of recombinant antigens and antibodies in Nicotiana benthamiana Using "Magnifection" technology: GMP-compliant facilities for small- and large-scale manufacturing. Current Topics in Microbiology and Immunology 2014 375 127 154
    • (2014) Current Topics in Microbiology and Immunology , vol.375 , pp. 127-154
    • Klimyuk, V.1    Herz, S.2    Butler, J.3    Haydon, H.4
  • 8
    • 77956440770 scopus 로고    scopus 로고
    • Commercialization of whole-plant systems for biomanufacturing of protein products: Evolution and prospects
    • 2-s2.0-77956440770 10.1111/j.1467-7652.2010.00550.x
    • Davies H. M., Commercialization of whole-plant systems for biomanufacturing of protein products: evolution and prospects. Plant Biotechnology Journal 2010 8 8 845 861 2-s2.0-77956440770 10.1111/j.1467-7652. 2010.00550.x
    • (2010) Plant Biotechnology Journal , vol.8 , Issue.8 , pp. 845-861
    • Davies, H.M.1
  • 9
    • 21644475978 scopus 로고    scopus 로고
    • Biopharming and the food system: Examining the potential benefits and risks
    • Elbehri A., Biopharming and the food system: Examining the potential benefits and risks. AgBioForum 2005 8 1 18 25 2-s2.0-21644475978 (Pubitemid 40935684)
    • (2005) AgBioForum , vol.8 , Issue.1 , pp. 18-25
    • Elbehri, A.1
  • 10
    • 33847613926 scopus 로고    scopus 로고
    • Process economics of industrial monoclonal antibody manufacture
    • DOI 10.1016/j.jchromb.2006.07.037, PII S1570023206006337
    • Farid S. S., Process economics of industrial monoclonal antibody manufacture. Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences 2007 848 1 8 18 2-s2.0-33847613926 10.1016/j.jchromb.2006.07.037 (Pubitemid 46367764)
    • (2007) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.848 , Issue.1 , pp. 8-18
    • Farid, S.S.1
  • 11
    • 0036901079 scopus 로고    scopus 로고
    • Monoclonal antibody manufacturing in transgenic plants - Myths and realities
    • DOI 10.1016/S0958-1669(02)00351-8
    • Hood E. E., Woodard S. L., Horn M. E., Monoclonal antibody manufacturing in transgenic plants: myths and realities. Current Opinion in Biotechnology 2002 13 6 630 635 2-s2.0-0036901079 10.1016/S0958-1669(02)00351-8 (Pubitemid 35448068)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.6 , pp. 630-635
    • Hood, E.E.1    Woodard, S.L.2    Horn, M.E.3
  • 12
    • 42549170120 scopus 로고    scopus 로고
    • Is the drought over for pharming
    • DOI 10.1126/science.320.5875.473
    • Kaiser J., Is the drought over for pharming. Science 2008 320 5875 473 475 2-s2.0-42549170120 10.1126/science.320.5875.473 (Pubitemid 351590625)
    • (2008) Science , vol.320 , Issue.5875 , pp. 473-475
    • Kaiser, J.1
  • 13
    • 28244473326 scopus 로고    scopus 로고
    • Plant-derived pharmaceuticals - The road forward
    • DOI 10.1016/j.tplants.2005.10.009, PII S1360138505002608
    • Ma J. K.-C., Chikwamba R., Sparrow P., Fischer R., Mahoney R., Twyman R. M., Plant-derived pharmaceuticals: the road forward. Trends in Plant Science 2005 10 12 580 585 2-s2.0-28244473326 10.1016/j.tplants.2005.10.009 (Pubitemid 41714013)
    • (2005) Trends in Plant Science , vol.10 , Issue.12 , pp. 580-585
    • Ma, J.K.-C.1    Chikwamba, R.2    Sparrow, P.3    Fischer, R.4    Mahoney, R.5    Twyman, R.M.6
  • 14
    • 0032127253 scopus 로고    scopus 로고
    • Process and economic evaluation of the extraction and purification of recombinant β-glucuronidase from transgenic corn
    • DOI 10.1021/bp980047c
    • Evangelista R. L., Kusnadi A. R., Howard J. A., Nikolov Z. L., Process and economic evaluation of the extraction and purification of recombinant β -glucuronidase from transgenic corn. Biotechnology Progress 1998 14 4 607 614 2-s2.0-0032127253 10.1021/bp980047c (Pubitemid 28382654)
    • (1998) Biotechnology Progress , vol.14 , Issue.4 , pp. 607-614
    • Evangelista, R.L.1    Kusnadi, A.R.2    Howard, J.A.3    Nikolov, Z.L.4
  • 15
    • 22144487779 scopus 로고    scopus 로고
    • Process development and economic evaluation of recombinant human lactoferrin expressed in rice grain
    • DOI 10.1007/s11248-004-8120-6
    • Nandi S., Yalda D., Lu S., Nikolov Z., Misaki R., Fujiyama K., Huang N., Process development and economic evaluation of recombinant human lactoferrin expressed in rice grain. Transgenic Research 2005 14 3 237 249 2-s2.0-22144487779 10.1007/s11248-004-8120-6 (Pubitemid 40982710)
    • (2005) Transgenic Research , vol.14 , Issue.3 , pp. 237-249
    • Nandi, S.1    Yalda, D.2    Lu, S.3    Nikolov, Z.4    Misaki, R.5    Fujiyama, K.6    Huang, N.7
  • 16
    • 84857441283 scopus 로고    scopus 로고
    • The challenge of enzyme cost in the production of lignocellulosic biofuels
    • 2-s2.0-84857441283 10.1002/bit.24370
    • Klein-Marcuschamer D., Oleskowicz-Popiel P., Simmons B. A., Blanch H. W., The challenge of enzyme cost in the production of lignocellulosic biofuels. Biotechnology and Bioengineering 2012 109 4 1083 1087 2-s2.0-84857441283 10.1002/bit.24370
    • (2012) Biotechnology and Bioengineering , vol.109 , Issue.4 , pp. 1083-1087
    • Klein-Marcuschamer, D.1    Oleskowicz-Popiel, P.2    Simmons, B.A.3    Blanch, H.W.4
  • 17
    • 1842339902 scopus 로고    scopus 로고
    • Process simulation for recombinant protein production: Cost estimation and sensitivity analysis for heparinase I expressed in Escherichia coli
    • DOI 10.1002/(SICI)1097-0290(19970320)53: 6<575::AID-BIT5>3.0.CO;2-J
    • Ernst S., Garro O. A., Winkler S., Venkataraman G., Langer R., Cooney C. L., Sasisekharan R., Process simulation for recombinant protein production: cost estimation and sensitivity analysis for heparinase I expressed in Escherichia coli. Biotechnology and Bioengineering 1997 53 6 575 582 (Pubitemid 27114320)
    • (1997) Biotechnology and Bioengineering , vol.53 , Issue.6 , pp. 575-582
    • Ernst, S.1    Garro, O.A.2    Winkler, S.3    Venkataraman, G.4    Langer, R.5    Cooney, C.L.6    Sasisekharan, R.7
  • 19
    • 0036031563 scopus 로고    scopus 로고
    • Making an ally from an enemy: Plant virology and the new agriculture
    • DOI 10.1146/annurev.phyto.40.021102.150133
    • Pogue G. P., Lindbo J. A., Garger S. J., Fitzmaurice W. P., Making an ally from an enemy: plant virology and the new agriculture. Annual Review of Phytopathology 2002 40 45 74 2-s2.0-0036031563 10.1146/annurev.phyto.40.021102. 150133 (Pubitemid 35235575)
    • (2002) Annual Review of Phytopathology , vol.40 , pp. 45-74
    • Pogue, G.P.1    Lindbo, J.A.2    Garger, S.J.3    Fitzmaurice, W.P.4
  • 20
    • 77953999126 scopus 로고    scopus 로고
    • Production of antibodies in plants: Status after twenty years
    • 2-s2.0-77953999126 10.1111/j.1467-7652.2009.00494.x
    • De Muynck B., Navarre C., Boutry M., Production of antibodies in plants: status after twenty years. Plant Biotechnology Journal 2010 8 5 529 563 2-s2.0-77953999126 10.1111/j.1467-7652.2009.00494.x
    • (2010) Plant Biotechnology Journal , vol.8 , Issue.5 , pp. 529-563
    • De Muynck, B.1    Navarre, C.2    Boutry, M.3
  • 21
    • 0038024485 scopus 로고    scopus 로고
    • Plant-based vaccines
    • DOI 10.1016/S0020-7519(03)00052-3
    • Streatfield S. J., Howard J. A., Plant-based vaccines. International Journal for Parasitology 2003 33 5-6 479 493 2-s2.0-0038024485 10.1016/S0020-7519(03)00052-3 (Pubitemid 36638531)
    • (2003) International Journal for Parasitology , vol.33 , Issue.5-6 , pp. 479-493
    • Streatfield, S.J.1    Howard, J.A.2
  • 24
    • 79953712649 scopus 로고    scopus 로고
    • Safety of plant-made pharmaceuticals: Product development and regulatory considerations based on case studies of two autologous human cancer vaccines
    • 2-s2.0-79953712649 10.4161/hv.7.3.14213
    • Tusé D., Safety of plant-made pharmaceuticals: product development and regulatory considerations based on case studies of two autologous human cancer vaccines. Human Vaccines 2011 7 3 322 330 2-s2.0-79953712649 10.4161/hv.7.3.14213
    • (2011) Human Vaccines , vol.7 , Issue.3 , pp. 322-330
    • Tusé, D.1
  • 25
    • 0023118832 scopus 로고
    • Complete amino acid sequence of human serum cholinesterase
    • Lockridge O., Bartels C. F., Vaughan T. A., Complete amino acid sequence of human serum cholinesterase. Journal of Biological Chemistry 1987 262 2 549 557 2-s2.0-0023118832 (Pubitemid 17005217)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.2 , pp. 549-557
    • Lockridge, O.1    Bartels, C.F.2    Vaughan, T.A.3
  • 28
    • 27544478065 scopus 로고    scopus 로고
    • Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys, a potential new therapeutic for protection against cocaine and nerve agent toxicity
    • nihms5095
    • Lockridge O., Schopfer L. M., Winger G., Woods J. H., Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys, a potential new therapeutic for protection against cocaine and nerve agent toxicity. Journal of Medical, Chemical, Biological, and Radiological Defense 2005 3 nihms5095
    • (2005) Journal of Medical, Chemical, Biological, and Radiological Defense , vol.3
    • Lockridge, O.1    Schopfer, L.M.2    Winger, G.3    Woods, J.H.4
  • 31
    • 18744437671 scopus 로고    scopus 로고
    • Association of tetramers of human butyrylcholinesterase is mediated by conserved aromatic residues of the carboxy terminus
    • DOI 10.1016/S0009-2797(99)00013-7, PII S0009279799000137
    • Altamirano C. V., Lockridge O., Association of tetramers of human butyrylcholinesterase is mediated by conserved aromatic residues of the carboxy terminus. Chemico-Biological Interactions 1999 119-120 53 60 2-s2.0-18744437671 10.1016/S0009-2797(99)00013-7 (Pubitemid 29278538)
    • (1999) Chemico-Biological Interactions , vol.119-120 , pp. 53-60
    • Altamirano, C.V.1    Lockridge, O.2
  • 32
    • 0028788139 scopus 로고
    • Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase
    • 2-s2.0-0028788139
    • Millard C. B., Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 1995 34 49 15925 15933 2-s2.0-0028788139
    • (1995) Biochemistry , vol.34 , Issue.49 , pp. 15925-15933
    • Millard, C.B.1
  • 35
    • 84902171821 scopus 로고    scopus 로고
    • Compositions and methods for the production and use of human cholinesterases
    • WO 2013040572 A2
    • Mor T., Kannan L., Larrimore K. E., Compositions and methods for the production and use of human cholinesterases. Patent Application 2012 WO 2013040572 A2
    • (2012) Patent Application
    • Mor, T.1    Kannan, L.2    Larrimore, K.E.3
  • 36
    • 84897094860 scopus 로고    scopus 로고
    • Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologue
    • 10.1002/biot.201300229
    • Schneider J. D., Castilho A., Neumann L., Altmann F., Loos A., Kannan L., Mor T. S., Steinkellner H., Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologue. Biotechnology Journal 2013 10.1002/biot.201300229
    • (2013) Biotechnology Journal
    • Schneider, J.D.1    Castilho, A.2    Neumann, L.3    Altmann, F.4    Loos, A.5    Kannan, L.6    Mor, T.S.7    Steinkellner, H.8
  • 38
    • 24944498904 scopus 로고    scopus 로고
    • Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants
    • DOI 10.1038/nbt1094
    • Marillonnet S., Thoeringer C., Kandzia R., Klimyuk V., Gleba Y., Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants. Nature Biotechnology 2005 23 6 718 723 2-s2.0-24944498904 10.1038/nbt1094 (Pubitemid 41716362)
    • (2005) Nature Biotechnology , vol.23 , Issue.6 , pp. 718-723
    • Marillonnet, S.1    Thoeringer, C.2    Kandzia, R.3    Klimyuk, V.4    Gleba, Y.5
  • 42
    • 68649119757 scopus 로고    scopus 로고
    • Commercial cellulosic ethanol: The role of plant-expressed enzymes
    • 2-s2.0-68649119757 10.1007/s11627-009-9210-1
    • Sainz M. B., Commercial cellulosic ethanol: The role of plant-expressed enzymes. In Vitro Cellular and Developmental Biology: Plant 2009 45 3 314 329 2-s2.0-68649119757 10.1007/s11627-009-9210-1
    • (2009) Vitro Cellular and Developmental Biology: Plant , vol.45 , Issue.3 , pp. 314-329
    • Sainz, M.B.1
  • 43
    • 84892940003 scopus 로고    scopus 로고
    • Production, storage and use of cell wall-degrading enzymes
    • EP2584042A1
    • Hahn S., Giritch A., Gleba Y., Production, storage and use of cell wall-degrading enzymes. Patent Application 2013 EP2584042A1
    • (2013) Patent Application
    • Hahn, S.1    Giritch, A.2    Gleba, Y.3
  • 44
    • 84902209448 scopus 로고    scopus 로고
    • Evaluation of float trays with high cell numbers on stand counts and yields in a close-grown tobacco production system
    • Mundell R., Chambers O., O'Daniel J. P., Davies H. M., Evaluation of float trays with high cell numbers on stand counts and yields in a close-grown tobacco production system. Tobacco Science 2012 49 4 7
    • (2012) Tobacco Science , vol.49 , pp. 4-7
    • Mundell, R.1    Chambers, O.2    O'Daniel, J.P.3    Davies, H.M.4
  • 46
    • 0002008580 scopus 로고
    • Biomass and chemical composition of tobacco plants under high density growth
    • Sheen S. J., Biomass and chemical composition of tobacco plants under high density growth. Beiträge Zur Tabakforschung International 1983 12 1 35 42
    • (1983) Beiträge Zur Tabakforschung International , vol.12 , Issue.1 , pp. 35-42
    • Sheen, S.J.1
  • 50
    • 79956093771 scopus 로고    scopus 로고
    • N-Glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans
    • 2-s2.0-79956093771 10.1093/glycob/cwr009
    • Castilho A., Gattinger P., Grass J., Jez J., Pabst M., Altmann F., Gorfer M., Strasser R., Steinkellner H., N-Glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans. Glycobiology 2011 21 6 813 823 2-s2.0-79956093771 10.1093/glycob/cwr009
    • (2011) Glycobiology , vol.21 , Issue.6 , pp. 813-823
    • Castilho, A.1    Gattinger, P.2    Grass, J.3    Jez, J.4    Pabst, M.5    Altmann, F.6    Gorfer, M.7    Strasser, R.8    Steinkellner, H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.