메뉴 건너뛰기




Volumn 47, Issue , 2016, Pages 51-63

Biopharmaceuticals from microorganisms: from production to purification

Author keywords

Biopharmaceuticals; Biotechnology; Downstream process; Fermentation process; Upstream process

Indexed keywords

BIOLOGICAL PRODUCT; BIOSIMILAR AGENT; DRUG; RECOMBINANT PROTEIN;

EID: 85003794105     PISSN: 15178382     EISSN: 16784405     Source Type: Journal    
DOI: 10.1016/j.bjm.2016.10.007     Document Type: Review
Times cited : (114)

References (82)
  • 1
    • 84859813803 scopus 로고    scopus 로고
    • An engineered eukaryotic protein glycosylation pathway in Escherichia coli
    • 1 Valderrama-Rincon, J.D., Fisher, A.C., Merritt, J.H., et al. An engineered eukaryotic protein glycosylation pathway in Escherichia coli. Nat Chem Biol 8:5 (2012), 434–436.
    • (2012) Nat Chem Biol , vol.8 , Issue.5 , pp. 434-436
    • Valderrama-Rincon, J.D.1    Fisher, A.C.2    Merritt, J.H.3
  • 2
    • 84900540654 scopus 로고    scopus 로고
    • Design and implementation of a high yield production system for recombinant expression of peptides
    • 2 Rodríguez, V., Asenjo, J.A., Andrews, B.A., Design and implementation of a high yield production system for recombinant expression of peptides. Microb Cell Fact 13 (2014), 1–10.
    • (2014) Microb Cell Fact , vol.13 , pp. 1-10
    • Rodríguez, V.1    Asenjo, J.A.2    Andrews, B.A.3
  • 3
    • 77956260809 scopus 로고    scopus 로고
    • Biopharmaceuticals: an overview
    • 3 Sekhon, B.S., Biopharmaceuticals: an overview. Thai J Pharm Sci 34 (2010), 1–19.
    • (2010) Thai J Pharm Sci , vol.34 , pp. 1-19
    • Sekhon, B.S.1
  • 4
    • 85003795656 scopus 로고    scopus 로고
    • Tufts CSDD assessment of cost to develop and win marketing approval for a new drug now published. Available from: [Accessed 12.07.16].
    • 4 Tufts Center for the Study of Drug Development. Tufts CSDD assessment of cost to develop and win marketing approval for a new drug now published. Available from: http://csdd.tufts.edu/news/complete_story/tufts_csdd_rd_cost_study_now_published [Accessed 12.07.16].
  • 5
  • 6
    • 84923106217 scopus 로고    scopus 로고
    • Therapeutic genome editing: prospects and challenges
    • 6 Cox, D.B.T., Platt, R.J., Zhang, F., Therapeutic genome editing: prospects and challenges. Nat Med 21:2 (2015), 121–131.
    • (2015) Nat Med , vol.21 , Issue.2 , pp. 121-131
    • Cox, D.B.T.1    Platt, R.J.2    Zhang, F.3
  • 7
    • 84929266411 scopus 로고    scopus 로고
    • Current recommendations for the Japanese encephalitis vaccine
    • 7 Chen, H.L., Chang, J.K., Tang, R.B., Current recommendations for the Japanese encephalitis vaccine. J Chin Med Assoc 78:5 (2015), 271–275.
    • (2015) J Chin Med Assoc , vol.78 , Issue.5 , pp. 271-275
    • Chen, H.L.1    Chang, J.K.2    Tang, R.B.3
  • 8
    • 84893909299 scopus 로고    scopus 로고
    • Therapeutic potentials of gene silencing by RNA interference: principles, challenges, and new strategies
    • 8 Deng, Y., Wang, C.C., Choy, K.W., et al. Therapeutic potentials of gene silencing by RNA interference: principles, challenges, and new strategies. Gene 538:2 (2014), 217–227.
    • (2014) Gene , vol.538 , Issue.2 , pp. 217-227
    • Deng, Y.1    Wang, C.C.2    Choy, K.W.3
  • 9
    • 84934307590 scopus 로고    scopus 로고
    • Knocking down disease: a progress report on siRNA therapeutics
    • 9 Wittrup, A., Lieberman, J., Knocking down disease: a progress report on siRNA therapeutics. Nat Rev Genet 16:9 (2015), 543–552.
    • (2015) Nat Rev Genet , vol.16 , Issue.9 , pp. 543-552
    • Wittrup, A.1    Lieberman, J.2
  • 10
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: a summary and pharmacological classification
    • 10 Leader, B., Baca, Q.J., Golan, D.E., Protein therapeutics: a summary and pharmacological classification. Nat Rev Drug Discov 7:1 (2008), 21–39.
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.1 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 11
    • 84859428492 scopus 로고    scopus 로고
    • A discussion of molecular biology methods for protein engineering
    • 11 Zawaira, A., Pooran, A., Barichievy, S., Chopera, D., A discussion of molecular biology methods for protein engineering. Mol Biotechnol 51:1 (2012), 67–102.
    • (2012) Mol Biotechnol , vol.51 , Issue.1 , pp. 67-102
    • Zawaira, A.1    Pooran, A.2    Barichievy, S.3    Chopera, D.4
  • 12
    • 79952715351 scopus 로고    scopus 로고
    • Biobetter and next generation therapeutic antibodies
    • 12 Beck, A., Biosimilar, Biobetter and next generation therapeutic antibodies. MAbs 3:2 (2011), 107–110.
    • (2011) MAbs , vol.3 , Issue.2 , pp. 107-110
    • Beck, A.1    Biosimilar2
  • 13
    • 84941423766 scopus 로고    scopus 로고
    • Fusion proteins for half-life extension of biologics as a strategy to make biobetters
    • 13 Strohl, W.R., Fusion proteins for half-life extension of biologics as a strategy to make biobetters. BioDrugs 29:4 (2015), 215–239.
    • (2015) BioDrugs , vol.29 , Issue.4 , pp. 215-239
    • Strohl, W.R.1
  • 14
    • 85003800505 scopus 로고    scopus 로고
    • Biobetters: the better biologics and their regulatory overview
    • 14 Sandeep, V., Parveen, J., Chauhan, P., Biobetters: the better biologics and their regulatory overview. Int J Drug Regul Aff 4:1 (2016), 13–20.
    • (2016) Int J Drug Regul Aff , vol.4 , Issue.1 , pp. 13-20
    • Sandeep, V.1    Parveen, J.2    Chauhan, P.3
  • 15
    • 84908299353 scopus 로고    scopus 로고
    • Overcoming the challenges in administering biopharmaceuticals: formulation and delivery strategies
    • 15 Mitragotri, S., Burke, P.A., Langer, R., Overcoming the challenges in administering biopharmaceuticals: formulation and delivery strategies. Nat Rev Drug Discov 13:9 (2014), 655–672.
    • (2014) Nat Rev Drug Discov , vol.13 , Issue.9 , pp. 655-672
    • Mitragotri, S.1    Burke, P.A.2    Langer, R.3
  • 16
    • 85003910130 scopus 로고    scopus 로고
    • This is a list of new full FDA approvals for biopharmaceutical products (unless otherwise noted). Available from: [Accessed 12.07.16].
    • 16 BIOPHARMA: Biopharmaceutical Products in the U.S. and European Markets. This is a list of new full FDA approvals for biopharmaceutical products (unless otherwise noted). Available from: http://www.biopharma.com/approvals.html [Accessed 12.07.16].
  • 17
    • 85019787919 scopus 로고    scopus 로고
    • EMA greenlights second gene therapy
    • 17 Mullard, A., EMA greenlights second gene therapy. Nat Rev Drug Discov, 15(5), 2016, 299.
    • (2016) Nat Rev Drug Discov , vol.15 , Issue.5 , pp. 299
    • Mullard, A.1
  • 18
    • 84974577177 scopus 로고    scopus 로고
    • Gene therapies: the challenge of super-high-cost treatments and how to pay for them
    • 18 Carr, D.R., Bradshaw, S.E., Gene therapies: the challenge of super-high-cost treatments and how to pay for them. Regen Med 11:4 (2016), 381–393.
    • (2016) Regen Med , vol.11 , Issue.4 , pp. 381-393
    • Carr, D.R.1    Bradshaw, S.E.2
  • 19
    • 79955666020 scopus 로고    scopus 로고
    • Introduction to current and future protein therapeutics: a protein engineering perspective
    • 19 Carter, P.J., Introduction to current and future protein therapeutics: a protein engineering perspective. Exp Cell Res 317:9 (2011), 1261–1269.
    • (2011) Exp Cell Res , vol.317 , Issue.9 , pp. 1261-1269
    • Carter, P.J.1
  • 20
    • 84947036849 scopus 로고    scopus 로고
    • Rational design of biobetters with enhanced stability
    • 20 Courtois, F., Schneider, C.P., Agrawal, N.J., Trout, B.L., Rational design of biobetters with enhanced stability. J Pharm Sci 104:8 (2015), 2433–2440.
    • (2015) J Pharm Sci , vol.104 , Issue.8 , pp. 2433-2440
    • Courtois, F.1    Schneider, C.P.2    Agrawal, N.J.3    Trout, B.L.4
  • 21
    • 0842304936 scopus 로고    scopus 로고
    • Minimizing the immunogenicity of protein therapeutics
    • 21 Chirino, A.J., Ary, M.L., Marshall, S., Minimizing the immunogenicity of protein therapeutics. Drug Discov Today 9:2 (2004), 82–90.
    • (2004) Drug Discov Today , vol.9 , Issue.2 , pp. 82-90
    • Chirino, A.J.1    Ary, M.L.2    Marshall, S.3
  • 22
    • 76649110785 scopus 로고    scopus 로고
    • The three-dimensional structure of protein
    • 1st ed. John Wiley & Sons West Sussex, England
    • 22 Whitford, D., The three-dimensional structure of protein. Proteins: Structure and Function, 1st ed., 2005, John Wiley & Sons, West Sussex, England, 39–83.
    • (2005) Proteins: Structure and Function , pp. 39-83
    • Whitford, D.1
  • 23
    • 84964556388 scopus 로고    scopus 로고
    • Rational design of therapeutic mAbs against aggregation through protein engineering and incorporation of glycosylation motifs applied to bevacizumab
    • 23 Courtois, F., Agrawal, N.J., Lauer, T.M., Trout, B.L., Rational design of therapeutic mAbs against aggregation through protein engineering and incorporation of glycosylation motifs applied to bevacizumab. MAbs 8:1 (2016), 99–112.
    • (2016) MAbs , vol.8 , Issue.1 , pp. 99-112
    • Courtois, F.1    Agrawal, N.J.2    Lauer, T.M.3    Trout, B.L.4
  • 24
    • 84946546463 scopus 로고    scopus 로고
    • Structural asymmetry of phosphodiesterase-9a and a unique pocket for selective binding of a potent enantiomeric inhibitor
    • 24 Huang, M., Shao, Y., Hou, J., et al. Structural asymmetry of phosphodiesterase-9a and a unique pocket for selective binding of a potent enantiomeric inhibitor. Mol Pharmacol 88:5 (2015), 836–845.
    • (2015) Mol Pharmacol , vol.88 , Issue.5 , pp. 836-845
    • Huang, M.1    Shao, Y.2    Hou, J.3
  • 25
    • 84939617820 scopus 로고    scopus 로고
    • A rational design strategy for the selective activity enhancement of a molecular chaperone toward a target substrate
    • 25 Aprile, F.A., Sormanni, P., Vendruscolo, M., A rational design strategy for the selective activity enhancement of a molecular chaperone toward a target substrate. Biochemistry 54:32 (2015), 5103–5112.
    • (2015) Biochemistry , vol.54 , Issue.32 , pp. 5103-5112
    • Aprile, F.A.1    Sormanni, P.2    Vendruscolo, M.3
  • 26
    • 0022751283 scopus 로고
    • Site-directed mutagenesis
    • 26 Carter, P., Site-directed mutagenesis. Biochem J 237 (1986), 1–7.
    • (1986) Biochem J , vol.237 , pp. 1-7
    • Carter, P.1
  • 27
    • 84934439066 scopus 로고    scopus 로고
    • Protein engineering: single or multiple site-directed mutagenesis
    • 27 Hsieh, P., Vaisvila, R., Protein engineering: single or multiple site-directed mutagenesis. Methods Mol Biol 978 (2013), 173–186.
    • (2013) Methods Mol Biol , vol.978 , pp. 173-186
    • Hsieh, P.1    Vaisvila, R.2
  • 28
    • 84946098489 scopus 로고    scopus 로고
    • Rapid fine conformational epitope mapping using comprehensive mutagenesis and deep sequencing
    • 28 Kowalsky, C.A., Faber, M.S., Nath, A., et al. Rapid fine conformational epitope mapping using comprehensive mutagenesis and deep sequencing. J Biol Chem 290:44 (2015), 26457–26470.
    • (2015) J Biol Chem , vol.290 , Issue.44 , pp. 26457-26470
    • Kowalsky, C.A.1    Faber, M.S.2    Nath, A.3
  • 29
    • 84926228359 scopus 로고    scopus 로고
    • Trends in upstream and downstream process development for antibody manufacturing
    • 29 Gronemeyer, P., Ditz, R., Strube, J., Trends in upstream and downstream process development for antibody manufacturing. Bioengineering 1:4 (2014), 188–212.
    • (2014) Bioengineering , vol.1 , Issue.4 , pp. 188-212
    • Gronemeyer, P.1    Ditz, R.2    Strube, J.3
  • 31
    • 84903174199 scopus 로고
    • The relation of the toxicity of diphtheria toxin to its neutralizing value upon antitoxin at different stages in the growth of culture
    • 31 Park, W.H., Atkinson, J.P., The relation of the toxicity of diphtheria toxin to its neutralizing value upon antitoxin at different stages in the growth of culture. J Exp Med 3:4–5 (1898), 513–532.
    • (1898) J Exp Med , vol.3 , Issue.4-5 , pp. 513-532
    • Park, W.H.1    Atkinson, J.P.2
  • 32
    • 35549010987 scopus 로고    scopus 로고
    • The origin and application of experimental autoimmune encephalomyelitis
    • 32 Baxter, A.G., The origin and application of experimental autoimmune encephalomyelitis. Nat Rev Immunol 7:11 (2007), 904–912.
    • (2007) Nat Rev Immunol , vol.7 , Issue.11 , pp. 904-912
    • Baxter, A.G.1
  • 33
    • 84883205070 scopus 로고    scopus 로고
    • The history of the idea of allergy
    • 33 Igea, J.M., The history of the idea of allergy. Allergy 68:8 (2013), 966–973.
    • (2013) Allergy , vol.68 , Issue.8 , pp. 966-973
    • Igea, J.M.1
  • 34
    • 0032883446 scopus 로고    scopus 로고
    • Pharmacokinetic and glucodynamic comparisons of recombinant and animal-source glucagon after IV, IM, and SC injection in healthy volunteers
    • 34 Graf, C.J., Woodworth, J.R., Seger, M.E., Holcombe, J.H., Bowsher, R.R., Lynch, R., Pharmacokinetic and glucodynamic comparisons of recombinant and animal-source glucagon after IV, IM, and SC injection in healthy volunteers. J Pharm Sci 88:10 (1999), 991–995.
    • (1999) J Pharm Sci , vol.88 , Issue.10 , pp. 991-995
    • Graf, C.J.1    Woodworth, J.R.2    Seger, M.E.3    Holcombe, J.H.4    Bowsher, R.R.5    Lynch, R.6
  • 35
    • 84951292119 scopus 로고    scopus 로고
    • Therapeutic L-asparaginase: upstream, downstream and beyond
    • [Epub ahead of print]
    • 35 Lopes, A.M., Oliveira-Nascimento, L., Ribeiro, A., et al. Therapeutic L-asparaginase: upstream, downstream and beyond. Crit Rev Biotechnol 23 (2015), 1–18 [Epub ahead of print].
    • (2015) Crit Rev Biotechnol , vol.23 , pp. 1-18
    • Lopes, A.M.1    Oliveira-Nascimento, L.2    Ribeiro, A.3
  • 36
    • 84937732919 scopus 로고    scopus 로고
    • Exenatide extended-release: an updated review of its use in type 2 diabetes mellitus
    • 36 Syed, Y.Y., McCormack, P.L., Exenatide extended-release: an updated review of its use in type 2 diabetes mellitus. Drugs 75:10 (2015), 1141–1152.
    • (2015) Drugs , vol.75 , Issue.10 , pp. 1141-1152
    • Syed, Y.Y.1    McCormack, P.L.2
  • 38
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms
    • 38 Demain, A.L., Vaishnav, P., Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 27:3 (2009), 297–306.
    • (2009) Biotechnol Adv , vol.27 , Issue.3 , pp. 297-306
    • Demain, A.L.1    Vaishnav, P.2
  • 39
    • 0036885616 scopus 로고    scopus 로고
    • Insulin: discovery and controversy
    • 39 Rosenfeld, L., Insulin: discovery and controversy. Clin Chem 48:12 (2002), 2270–2288.
    • (2002) Clin Chem , vol.48 , Issue.12 , pp. 2270-2288
    • Rosenfeld, L.1
  • 40
    • 57649213405 scopus 로고    scopus 로고
    • Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity
    • 40 Lim, J.C., Choi, H.-I., Park, Y.S., et al. Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity. J Biol Chem 283:43 (2008), 28873–28880.
    • (2008) J Biol Chem , vol.283 , Issue.43 , pp. 28873-28880
    • Lim, J.C.1    Choi, H.-I.2    Park, Y.S.3
  • 41
    • 70349128489 scopus 로고    scopus 로고
    • Aspergillus niger var. taxi, a new species variant of taxol-producing fungus isolated from Taxus cuspidata in China
    • 41 Zhao, K., Ping, W., Li, Q., et al. Aspergillus niger var. taxi, a new species variant of taxol-producing fungus isolated from Taxus cuspidata in China. J Appl Microbiol 107:4 (2009), 1202–1207.
    • (2009) J Appl Microbiol , vol.107 , Issue.4 , pp. 1202-1207
    • Zhao, K.1    Ping, W.2    Li, Q.3
  • 42
    • 50049083383 scopus 로고    scopus 로고
    • Application relevant studies of fungal beta-galactosidases with potential application in the alleviation of lactose intolerance
    • 42 O'Connell, S., Walsh, G., Application relevant studies of fungal beta-galactosidases with potential application in the alleviation of lactose intolerance. Appl Biochem Biotechnol 149:2 (2008), 129–138.
    • (2008) Appl Biochem Biotechnol , vol.149 , Issue.2 , pp. 129-138
    • O'Connell, S.1    Walsh, G.2
  • 43
    • 80053439614 scopus 로고    scopus 로고
    • Recombinant microbial systems for improved β-galactosidase production and biotechnological applications
    • 43 Oliveira, C., Guimarães, P.M.R., Domingues, L., Recombinant microbial systems for improved β-galactosidase production and biotechnological applications. Biotechnol Adv 29:6 (2011), 600–609.
    • (2011) Biotechnol Adv , vol.29 , Issue.6 , pp. 600-609
    • Oliveira, C.1    Guimarães, P.M.R.2    Domingues, L.3
  • 44
    • 84871756769 scopus 로고    scopus 로고
    • Presence of mono-, di- and galactooligosaccharides in commercial lactose-free UHT dairy products
    • 44 Ruiz-Matute, A.I., Corzo-Martínez, M., Montilla, A., Olano, A., Copovi, P., Corzo, N., Presence of mono-, di- and galactooligosaccharides in commercial lactose-free UHT dairy products. J Food Compos Anal 28:2 (2012), 164–169.
    • (2012) J Food Compos Anal , vol.28 , Issue.2 , pp. 164-169
    • Ruiz-Matute, A.I.1    Corzo-Martínez, M.2    Montilla, A.3    Olano, A.4    Copovi, P.5    Corzo, N.6
  • 46
    • 84940196750 scopus 로고    scopus 로고
    • Isolation, purification, and structural identification of an antifungal compound from a trichoderma strain
    • 46 Li, C.-W., Song, R.-Q., Yang, L.-B., Deng, X., Isolation, purification, and structural identification of an antifungal compound from a trichoderma strain. J Microbiol Biotechnol 25:8 (2015), 1257–1264.
    • (2015) J Microbiol Biotechnol , vol.25 , Issue.8 , pp. 1257-1264
    • Li, C.-W.1    Song, R.-Q.2    Yang, L.-B.3    Deng, X.4
  • 47
    • 84962625613 scopus 로고    scopus 로고
    • Penicillium nalgiovense Laxa isolated from Antarctica is a new source of the antifungal metabolite amphotericin B
    • 47 Svahn, K.S., Chryssanthou, E., Olsen, B., Bohlin, L., Göransson, U., Penicillium nalgiovense Laxa isolated from Antarctica is a new source of the antifungal metabolite amphotericin B. Fungal Biol Biotechnol 2:1 (2015), 2–8.
    • (2015) Fungal Biol Biotechnol , vol.2 , Issue.1 , pp. 2-8
    • Svahn, K.S.1    Chryssanthou, E.2    Olsen, B.3    Bohlin, L.4    Göransson, U.5
  • 48
    • 1242292972 scopus 로고    scopus 로고
    • Collagenolytic proteases from bacteria
    • 48 Watanabe, K., Collagenolytic proteases from bacteria. Appl Microbiol Biotechnol 63:5 (2004), 520–526.
    • (2004) Appl Microbiol Biotechnol , vol.63 , Issue.5 , pp. 520-526
    • Watanabe, K.1
  • 49
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: from a bioindustrial viewpoint
    • 49 Kumar, C.G., Takagi, H., Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnol Adv 17:7 (1999), 561–594.
    • (1999) Biotechnol Adv , vol.17 , Issue.7 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 50
    • 0025244017 scopus 로고
    • Heterologous gene expression by filamentous fungi: secretion of human interleukin-6 by Aspergillus nidulans
    • 50 Carrez, D., Janssens, W., Degrave, P., et al. Heterologous gene expression by filamentous fungi: secretion of human interleukin-6 by Aspergillus nidulans. Gene 94:2 (1990), 147–154.
    • (1990) Gene , vol.94 , Issue.2 , pp. 147-154
    • Carrez, D.1    Janssens, W.2    Degrave, P.3
  • 51
    • 0030063032 scopus 로고    scopus 로고
    • Effect of culture conditions and induction strategies on production of human interleukin-6 by a recombinant Aspergillus nidulans strain
    • 51 Yadwad, V.B., Wilson, S., Ward, O.P., Effect of culture conditions and induction strategies on production of human interleukin-6 by a recombinant Aspergillus nidulans strain. Mycol Res 100:3 (1996), 356–360.
    • (1996) Mycol Res , vol.100 , Issue.3 , pp. 356-360
    • Yadwad, V.B.1    Wilson, S.2    Ward, O.P.3
  • 52
    • 0002596901 scopus 로고    scopus 로고
    • Filamentous fungi as production organisms for glycoproteins of bio-medical interest
    • 52 Maras, M., van Die, I., Contreras, R., van den Hondel, C.A., Filamentous fungi as production organisms for glycoproteins of bio-medical interest. Glycoconj J 16:2 (1999), 99–107.
    • (1999) Glycoconj J , vol.16 , Issue.2 , pp. 99-107
    • Maras, M.1    van Die, I.2    Contreras, R.3    van den Hondel, C.A.4
  • 53
    • 62549139648 scopus 로고    scopus 로고
    • Chromatography-free recovery of biopharmaceuticals through aqueous two-phase processing
    • 53 Azevedo, A.M., Rosa, P.A.J., Ferreira, I.F., Aires-Barros, M.R., Chromatography-free recovery of biopharmaceuticals through aqueous two-phase processing. Trends Biotechnol 27:4 (2009), 240–247.
    • (2009) Trends Biotechnol , vol.27 , Issue.4 , pp. 240-247
    • Azevedo, A.M.1    Rosa, P.A.J.2    Ferreira, I.F.3    Aires-Barros, M.R.4
  • 54
    • 84920914665 scopus 로고    scopus 로고
    • Application of process analytical technology for downstream purification of biotherapeutics
    • 54 Rathore, A.S., Kapoor, G., Application of process analytical technology for downstream purification of biotherapeutics. J Chem Technol Biotechnol 90:2 (2015), 228–236.
    • (2015) J Chem Technol Biotechnol , vol.90 , Issue.2 , pp. 228-236
    • Rathore, A.S.1    Kapoor, G.2
  • 55
    • 77950101404 scopus 로고    scopus 로고
    • Aqueous two-phase systems: a viable platform in the manufacturing of biopharmaceuticals
    • 55 Rosa, P.A.J., Ferreira, I.F., Azevedo, A.M., Aires-Barros, M.R., Aqueous two-phase systems: a viable platform in the manufacturing of biopharmaceuticals. J Chromatogr A 1217:16 (2010), 2296–2305.
    • (2010) J Chromatogr A , vol.1217 , Issue.16 , pp. 2296-2305
    • Rosa, P.A.J.1    Ferreira, I.F.2    Azevedo, A.M.3    Aires-Barros, M.R.4
  • 56
    • 84947997846 scopus 로고    scopus 로고
    • Advances in affinity ligand-functionalized nanomaterials for biomagnetic separation
    • 56 Fields, C., Li, P., O'Mahony, J.J., Lee, G.U., Advances in affinity ligand-functionalized nanomaterials for biomagnetic separation. Biotechnol Bioeng 113:1 (2016), 11–25.
    • (2016) Biotechnol Bioeng , vol.113 , Issue.1 , pp. 11-25
    • Fields, C.1    Li, P.2    O'Mahony, J.J.3    Lee, G.U.4
  • 58
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: production and purification
    • 58 Roque, A.C.A., Lowe, C.R., Taipa, M.A., Antibodies and genetically engineered related molecules: production and purification. Biotechnol Prog 20:3 (2004), 639–654.
    • (2004) Biotechnol Prog , vol.20 , Issue.3 , pp. 639-654
    • Roque, A.C.A.1    Lowe, C.R.2    Taipa, M.A.3
  • 59
    • 84960480192 scopus 로고    scopus 로고
    • Instrumental aspects of simulated moving bed chromatography
    • 59 Faria, R.P.V., Rodrigues, A.E., Instrumental aspects of simulated moving bed chromatography. J Chromatogr A 1421 (2015), 82–102.
    • (2015) J Chromatogr A , vol.1421 , pp. 82-102
    • Faria, R.P.V.1    Rodrigues, A.E.2
  • 60
    • 84893733256 scopus 로고    scopus 로고
    • Preparative purification of recombinant proteins: current status and future trends
    • 60 Saraswat, M., Musante, L., Ravidá, A., Shortt, B., Byrne, B., Holthofer, H., Preparative purification of recombinant proteins: current status and future trends. Biomed Res Int 2013 (2013), 1–18.
    • (2013) Biomed Res Int , vol.2013 , pp. 1-18
    • Saraswat, M.1    Musante, L.2    Ravidá, A.3    Shortt, B.4    Byrne, B.5    Holthofer, H.6
  • 61
    • 0035359193 scopus 로고    scopus 로고
    • Combinatorial approaches to affinity chromatography
    • 61 Lowe, C.R., Combinatorial approaches to affinity chromatography. Curr Opin Chem Biol 5:3 (2001), 248–256.
    • (2001) Curr Opin Chem Biol , vol.5 , Issue.3 , pp. 248-256
    • Lowe, C.R.1
  • 62
    • 0035975869 scopus 로고    scopus 로고
    • New developments in affinity chromatography with potential application in the production of biopharmaceuticals
    • 62 Lowe, C.R., Lowe, A.R., Gupta, G., New developments in affinity chromatography with potential application in the production of biopharmaceuticals. J Biochem Biophys Methods 49:1–3 (2001), 561–574.
    • (2001) J Biochem Biophys Methods , vol.49 , Issue.1-3 , pp. 561-574
    • Lowe, C.R.1    Lowe, A.R.2    Gupta, G.3
  • 63
    • 84868158860 scopus 로고    scopus 로고
    • Integrated continuous production of recombinant therapeutic proteins
    • 63 Warikoo, V., Godawat, R., Brower, K., et al. Integrated continuous production of recombinant therapeutic proteins. Biotechnol Bioeng 109:12 (2012), 3018–3029.
    • (2012) Biotechnol Bioeng , vol.109 , Issue.12 , pp. 3018-3029
    • Warikoo, V.1    Godawat, R.2    Brower, K.3
  • 64
    • 84880510340 scopus 로고    scopus 로고
    • Continuous downstream processing of biopharmaceuticals
    • 64 Jungbauer, A., Continuous downstream processing of biopharmaceuticals. Trends Biotechnol 31:8 (2013), 479–492.
    • (2013) Trends Biotechnol , vol.31 , Issue.8 , pp. 479-492
    • Jungbauer, A.1
  • 66
    • 81855169740 scopus 로고    scopus 로고
    • Downstream bioprocessing: recent advances and future promise
    • 66 Cramer, S.M., Holstein, M.A., Downstream bioprocessing: recent advances and future promise. Curr Opin Chem Eng 1:1 (2011), 27–37.
    • (2011) Curr Opin Chem Eng , vol.1 , Issue.1 , pp. 27-37
    • Cramer, S.M.1    Holstein, M.A.2
  • 67
    • 84896835916 scopus 로고    scopus 로고
    • Recovery of microquantities of human epidermal growth factor from Escherichia coli Homogenate and Pichia pastoris culture medium using expanded bed adsorption
    • 67 Rosti, I.A., Ramanan, R.N., Tan, J.S., Ling, T.C., Ariff, A.B., Recovery of microquantities of human epidermal growth factor from Escherichia coli Homogenate and Pichia pastoris culture medium using expanded bed adsorption. Sep Sci Technol 49:5 (2014), 702–708.
    • (2014) Sep Sci Technol , vol.49 , Issue.5 , pp. 702-708
    • Rosti, I.A.1    Ramanan, R.N.2    Tan, J.S.3    Ling, T.C.4    Ariff, A.B.5
  • 68
    • 84893797452 scopus 로고    scopus 로고
    • Clarification and capture of high-concentration refold pools for E. coli-based therapeutics using expanded bed adsorption chromatography
    • 68 Xu, X., Hirpara, J., Epting, K., et al. Clarification and capture of high-concentration refold pools for E. coli-based therapeutics using expanded bed adsorption chromatography. Biotechnol Prog 30:1 (2014), 113–123.
    • (2014) Biotechnol Prog , vol.30 , Issue.1 , pp. 113-123
    • Xu, X.1    Hirpara, J.2    Epting, K.3
  • 69
    • 85003794896 scopus 로고    scopus 로고
    • Monoliths in bioprocess technology
    • 69 Rajamanickam, V., Herwig, C., Spadiut, O., Monoliths in bioprocess technology. Chromatography 2:2 (2015), 195–212.
    • (2015) Chromatography , vol.2 , Issue.2 , pp. 195-212
    • Rajamanickam, V.1    Herwig, C.2    Spadiut, O.3
  • 70
    • 84884571568 scopus 로고    scopus 로고
    • Anion-exchange purification of recombinant factor IX from cell culture supernatant using different chromatography supports
    • 70 Ribeiro, D.A., Passos, D.F., Ferraz, H.C., Castilho, L.R., Anion-exchange purification of recombinant factor IX from cell culture supernatant using different chromatography supports. J Chromatogr B Anal Technol Biomed Life Sci 938 (2013), 111–118.
    • (2013) J Chromatogr B Anal Technol Biomed Life Sci , vol.938 , pp. 111-118
    • Ribeiro, D.A.1    Passos, D.F.2    Ferraz, H.C.3    Castilho, L.R.4
  • 71
    • 84891699480 scopus 로고    scopus 로고
    • Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris
    • 71 Krainer, F.W., Pletzenauer, R., Rossetti, L., Herwig, C., Glieder, A., Spadiut, O., Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris. Protein Expr Purif 95 (2014), 104–112.
    • (2014) Protein Expr Purif , vol.95 , pp. 104-112
    • Krainer, F.W.1    Pletzenauer, R.2    Rossetti, L.3    Herwig, C.4    Glieder, A.5    Spadiut, O.6
  • 72
    • 33646049189 scopus 로고    scopus 로고
    • Current therapeutic antibody production and process optimization
    • 72 Li, F., Lee, B., Zho, J.X., Tressel, T., Yang, X., Current therapeutic antibody production and process optimization. BioProccessing J 5 (2006), 16–25.
    • (2006) BioProccessing J , vol.5 , pp. 16-25
    • Li, F.1    Lee, B.2    Zho, J.X.3    Tressel, T.4    Yang, X.5
  • 73
    • 83455255467 scopus 로고    scopus 로고
    • The future of downstream processing
    • 73 Gottschalk, U., The future of downstream processing. BioPharm Int 24:9 (2011), 38–47.
    • (2011) BioPharm Int , vol.24 , Issue.9 , pp. 38-47
    • Gottschalk, U.1
  • 74
    • 84903626070 scopus 로고    scopus 로고
    • Understanding pharmaceutical quality by design
    • 74 Yu, L.X., Amidon, G., Khan, M.A., et al. Understanding pharmaceutical quality by design. AAPS J 16:4 (2014), 771–783.
    • (2014) AAPS J , vol.16 , Issue.4 , pp. 771-783
    • Yu, L.X.1    Amidon, G.2    Khan, M.A.3
  • 75
    • 79953678087 scopus 로고    scopus 로고
    • Process analytical technology (PAT) for biopharmaceuticals
    • 75 Glassey, J., Gernaey, K.V., Clemens, C., et al. Process analytical technology (PAT) for biopharmaceuticals. Biotechnol J 6:4 (2011), 369–377.
    • (2011) Biotechnol J , vol.6 , Issue.4 , pp. 369-377
    • Glassey, J.1    Gernaey, K.V.2    Clemens, C.3
  • 76
    • 85003920320 scopus 로고    scopus 로고
    • Available from: [Accessed 14.07.16].
    • 76 bioTRAK database. Available from: http://bptc.com [Accessed 14.07.16].
  • 77
    • 85003899239 scopus 로고    scopus 로고
    • Biosimilars: Reviewing US law and US/EU patents; bottom up model suggests 12 products and $7-$8B market by 2020
    • Bernstein Research. Available from: [Accessed 06.10.16].
    • 77 Gal R. Biosimilars: Reviewing US law and US/EU patents; bottom up model suggests 12 products and $7-$8B market by 2020. Bernstein Research. Available from: http://www.gabionline.net/layout/set/print/content/view/full/2030 [Accessed 06.10.16].
    • Gal, R.1
  • 78
    • 85003953394 scopus 로고    scopus 로고
    • Top 25 Pharmaceutical Products in 2015
    • Available from: [Accessed 11.10.16].
    • 78 Dezzani L. Top 25 Pharmaceutical Products in 2015. Available from: https://igeahub.com/2016/04/30/top-25-pharmaceutical-products-in-2015/ [Accessed 11.10.16].
    • (2015)
    • Dezzani, L.1
  • 79
    • 84930092437 scopus 로고    scopus 로고
    • The advent of biosimilars for the treatment of diabetes: current status and future directions
    • 79 Polimeni, G., Trifirò, G., Ingrasciotta, Y., Caputi, A.P., The advent of biosimilars for the treatment of diabetes: current status and future directions. Acta Diabetol 52:3 (2015), 423–431.
    • (2015) Acta Diabetol , vol.52 , Issue.3 , pp. 423-431
    • Polimeni, G.1    Trifirò, G.2    Ingrasciotta, Y.3    Caputi, A.P.4
  • 81
    • 84927537064 scopus 로고    scopus 로고
    • Technologies for glycomic characterization of biopharmaceutical erythropoietins
    • 81 Hua, S., Oh, M.J., Ozcan, S., Seo, Y.S., Grimm, R., An, H.J., Technologies for glycomic characterization of biopharmaceutical erythropoietins. TrAC Trends Anal Chem 68 (2015), 18–27.
    • (2015) TrAC Trends Anal Chem , vol.68 , pp. 18-27
    • Hua, S.1    Oh, M.J.2    Ozcan, S.3    Seo, Y.S.4    Grimm, R.5    An, H.J.6
  • 82
    • 84948714780 scopus 로고    scopus 로고
    • Biosimilars in rheumatology: current perspectives and lessons learnt
    • 82 Dörner, T., Kay, J., Biosimilars in rheumatology: current perspectives and lessons learnt. Nat Rev Rheumatol 11:12 (2015), 713–724.
    • (2015) Nat Rev Rheumatol , vol.11 , Issue.12 , pp. 713-724
    • Dörner, T.1    Kay, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.