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Volumn 7, Issue 10, 2012, Pages 1221-1232

Model-based high-throughput process development for chromatographic whey proteins separation

Author keywords

Column modeling; High throughput screening; Process development; Protein chromatography; Whey proteins separation

Indexed keywords

COLUMN MODELING; HIGH-THROUGHPUT SCREENING; PROCESS DEVELOPMENT; PROTEIN CHROMATOGRAPHY; WHEY PROTEINS;

EID: 84867220763     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201200191     Document Type: Article
Times cited : (23)

References (41)
  • 2
    • 0033212566 scopus 로고    scopus 로고
    • Maximizing the value of milk through separation technologies.
    • Huffman, L. M., James Harper, W., Maximizing the value of milk through separation technologies. J. Dairy Sci. 1999, 82, 2238-2244.
    • (1999) J. Dairy Sci. , vol.82 , pp. 2238-2244
    • Huffman, L.M.1    James Harper, W.2
  • 4
    • 0037725285 scopus 로고    scopus 로고
    • Whey proteins as a model system for chromatographic separation of proteins.
    • Pedersen, L., Mollerup, J., Hansen, E., Jungbauer, A., Whey proteins as a model system for chromatographic separation of proteins. J. Chromatogr., B 2003, 790, 161-173.
    • (2003) J. Chromatogr., B , vol.790 , pp. 161-173
    • Pedersen, L.1    Mollerup, J.2    Hansen, E.3    Jungbauer, A.4
  • 5
    • 28144465528 scopus 로고    scopus 로고
    • Design considerations for the batch capture of proteins from raw whole milk by ion exchange chromatography.
    • Fee, C. J., Chand, A., Design considerations for the batch capture of proteins from raw whole milk by ion exchange chromatography. Chem. Eng. Technol. 2005, 28, 1360-1366.
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1360-1366
    • Fee, C.J.1    Chand, A.2
  • 6
    • 31144473781 scopus 로고    scopus 로고
    • Capture of lactoferrin and lactoperoxidase from raw whole milk by cation exchange chromatography.
    • Fee, C. J., Chand, A., Capture of lactoferrin and lactoperoxidase from raw whole milk by cation exchange chromatography. Sep. Purif. Technol. 2006, 48, 143-149.
    • (2006) Sep. Purif. Technol. , vol.48 , pp. 143-149
    • Fee, C.J.1    Chand, A.2
  • 7
    • 1842574306 scopus 로고    scopus 로고
    • Fractionation of proteins from whey using cation exchange chromatography.
    • Doultani, S., Turhan, K. N., Etzel, M. R., Fractionation of proteins from whey using cation exchange chromatography. Process Biochem. 2004, 39, 1737-1743.
    • (2004) Process Biochem. , vol.39 , pp. 1737-1743
    • Doultani, S.1    Turhan, K.N.2    Etzel, M.R.3
  • 8
    • 0032577398 scopus 로고    scopus 로고
    • Preparative ion-exchange chromatography of proteins from dairy whey.
    • Gerberding, S. J., Byers, C. H., Preparative ion-exchange chromatography of proteins from dairy whey. J. Chromatogr., A 1998, 808, 141-151.
    • (1998) J. Chromatogr., A , vol.808 , pp. 141-151
    • Gerberding, S.J.1    Byers, C.H.2
  • 9
    • 0032489020 scopus 로고    scopus 로고
    • Bovine whey fractionation based on cation-exchange chromatography.
    • Hahn, R., Schulz, P. M., Schaupp, C., Jungbauer, A., Bovine whey fractionation based on cation-exchange chromatography. J. Chromatogr., A 1998, 795, 277-287.
    • (1998) J. Chromatogr., A , vol.795 , pp. 277-287
    • Hahn, R.1    Schulz, P.M.2    Schaupp, C.3    Jungbauer, A.4
  • 10
    • 0034536951 scopus 로고    scopus 로고
    • Isolation of lactoperoxidase, lactoferrin, α-lactalbumin, β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography.
    • Ye, X., Yoshida, S., Ng, T. B., Isolation of lactoperoxidase, lactoferrin, α-lactalbumin, β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography. Int. J. Biochem. Cell Biol. 2000, 32, 1143-1150.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 1143-1150
    • Ye, X.1    Yoshida, S.2    Ng, T.B.3
  • 11
    • 65949115720 scopus 로고    scopus 로고
    • Fractionation of β-lactoglobulin from whey by mixed matrix membrane ion exchange chromatography.
    • Saufi, S. M., Fee, C. J., Fractionation of β-lactoglobulin from whey by mixed matrix membrane ion exchange chromatography. Biotechnol. Bioeng. 2009, 103, 138-147.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 138-147
    • Saufi, S.M.1    Fee, C.J.2
  • 12
    • 81855166642 scopus 로고    scopus 로고
    • Simultaneous anion and cation exchange chromatography of whey proteins using a customizable mixed matrix membrane.
    • Saufi, S. M., Fee, C. J., Simultaneous anion and cation exchange chromatography of whey proteins using a customizable mixed matrix membrane. J. Chromatogr., A 2011, 1218, 9003-9009.
    • (2011) J. Chromatogr., A , vol.1218 , pp. 9003-9009
    • Saufi, S.M.1    Fee, C.J.2
  • 13
    • 78751568006 scopus 로고    scopus 로고
    • Recovery of lactoferrin from whey using cross-flow cation exchange mixed matrix membrane chromatography.
    • Saufi, S. M., Fee, C. J., Recovery of lactoferrin from whey using cross-flow cation exchange mixed matrix membrane chromatography. Sep. Purif. Technol. 2011, 77, 68-75.
    • (2011) Sep. Purif. Technol. , vol.77 , pp. 68-75
    • Saufi, S.M.1    Fee, C.J.2
  • 14
    • 46249092863 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: I. Method development and column modeling.
    • Coffman, J. L., Kramarczyk, J. F., Kelley, B. D., High-throughput screening of chromatographic separations: I. Method development and column modeling. Biotechnol. Bioeng. 2008, 100, 605-618.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 605-618
    • Coffman, J.L.1    Kramarczyk, J.F.2    Kelley, B.D.3
  • 15
    • 46249100489 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: IV. Ion-exchange.
    • Kelley, B. D., Switzer, M., Bastek, P., Kramarczyk, J. F. et al., High-throughput screening of chromatographic separations: IV. Ion-exchange. Biotechnol. Bioeng. 2008, 100, 950-963.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 950-963
    • Kelley, B.D.1    Switzer, M.2    Bastek, P.3    Kramarczyk, J.F.4
  • 16
    • 46249099122 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: II. Hydrophobic interaction.
    • Kramarczyk, J. F., Brian, D. K., Jonathan, L. C., High-throughput screening of chromatographic separations: II. Hydrophobic interaction. Biotechnol. Bioeng. 2008, 100, 707-720.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 707-720
    • Kramarczyk, J.F.1    Brian, D.K.2    Jonathan, L.C.3
  • 17
    • 46249087945 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: III. Monoclonal antibodies on ceramic hydroxyapatite.
    • Wensel, D. L., Kelley, B. D., Coffman, J. L., High-throughput screening of chromatographic separations: III. Monoclonal antibodies on ceramic hydroxyapatite. Biotechnol. Bioeng. 2008, 100, 839-854.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 839-854
    • Wensel, D.L.1    Kelley, B.D.2    Coffman, J.L.3
  • 18
    • 28244461283 scopus 로고    scopus 로고
    • High throughput screening of chromatographic phases for rapid process development.
    • Bensch, M., Wierling, P. S., Lieres, E. v., Hubbuch, J., High throughput screening of chromatographic phases for rapid process development. Chem. Eng. Technol. 2005, 28, 1274-1284.
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1274-1284
    • Bensch, M.1    Wierling, P.S.2    Lieres, E.3    Hubbuch, J.4
  • 19
    • 34948906395 scopus 로고    scopus 로고
    • High-throughput screening of packed-bed chromatography coupled with SELDI-TOF MS analysis: monoclonal antibodies versus host cell protein.
    • Wierling, P. S., Bogumil, R., Knieps-Grünhagen, E., Hubbuch, J., High-throughput screening of packed-bed chromatography coupled with SELDI-TOF MS analysis: monoclonal antibodies versus host cell protein. Biotechnol. Bioeng. 2007, 98, 440-450.
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 440-450
    • Wierling, P.S.1    Bogumil, R.2    Knieps-Grünhagen, E.3    Hubbuch, J.4
  • 20
    • 33644908243 scopus 로고    scopus 로고
    • High-throughput process development for recombinant protein purification.
    • Rege, K., Pepsin, M., Falcon, B., Steele, L., Heng, M., High-throughput process development for recombinant protein purification. Biotechnol. Bioeng. 2006, 93, 618-630.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 618-630
    • Rege, K.1    Pepsin, M.2    Falcon, B.3    Steele, L.4    Heng, M.5
  • 21
    • 33947536218 scopus 로고    scopus 로고
    • Platform technology for developing purification processes.
    • Eppink, M. H. M., Schreurs, R., Gijsen, A., Verhoeven, K., Platform technology for developing purification processes. BioPharm Int. 2007, 20, 44-50.
    • (2007) BioPharm Int. , vol.20 , pp. 44-50
    • Eppink, M.H.M.1    Schreurs, R.2    Gijsen, A.3    Verhoeven, K.4
  • 22
    • 79951674715 scopus 로고    scopus 로고
    • High-throughput process development for biopharmaceutical drug substances.
    • Bhambure, R., Kumar, K., Rathore, A. S., High-throughput process development for biopharmaceutical drug substances. Trends Biotechnol. 2011, 29, 127-135.
    • (2011) Trends Biotechnol. , vol.29 , pp. 127-135
    • Bhambure, R.1    Kumar, K.2    Rathore, A.S.3
  • 23
    • 34347373866 scopus 로고    scopus 로고
    • Statistical designs and response surface techniques for the optimization of chromatographic systems.
    • Ferreira, S. L. C., Bruns, R. E., da Silva, E. G. P., dos Santos, W. N. L., Statistical designs and response surface techniques for the optimization of chromatographic systems. J. Chromatogr., A 2007, 1158, 2-14.
    • (2007) J. Chromatogr., A , vol.1158 , pp. 2-14
    • Ferreira, S.L.C.1    Bruns, R.E.2    da Silva, E.G.P.3    dos Santos, W.N.L.4
  • 24
    • 84866907990 scopus 로고    scopus 로고
    • Experimental design in chromatography: A tutorial review.
    • DOI: 10.1016/j.jchromb.2012.01.02.
    • Brynn Hibbert, D., Experimental design in chromatography: A tutorial review. J. Chromatogr., B 2012, DOI: 10.1016/j.jchromb.2012.01.02.
    • (2012) J. Chromatogr., B
    • Brynn Hibbert, D.1
  • 25
    • 60849096390 scopus 로고    scopus 로고
    • High throughput screening for the design and optimization of chromatographic processes: Automated optimization of chromatographic phase systems.
    • Susanto, A., Treier, K., Knieps-Grünhagen, E., Lieres, E. v., Hubbuch, J., High throughput screening for the design and optimization of chromatographic processes: Automated optimization of chromatographic phase systems. Chem. Eng. Technol. 2009, 32, 140-154.
    • (2009) Chem. Eng. Technol. , vol.32 , pp. 140-154
    • Susanto, A.1    Treier, K.2    Knieps-Grünhagen, E.3    Lieres, E.4    Hubbuch, J.5
  • 26
    • 84857969029 scopus 로고    scopus 로고
    • Application of genetic algorithms and response surface analysis for the optimization of batch chromatographic systems.
    • Treier, K., Lester, P., Hubbuch, J., Application of genetic algorithms and response surface analysis for the optimization of batch chromatographic systems. Biochem. Eng. J. 2012, 63, 66-75.
    • (2012) Biochem. Eng. J. , vol.63 , pp. 66-75
    • Treier, K.1    Lester, P.2    Hubbuch, J.3
  • 27
    • 0026799147 scopus 로고
    • Steric mass-action ion exchange: Displacement profiles and induced salt gradients.
    • Brooks, C. A., Cramer, S. M., Steric mass-action ion exchange: Displacement profiles and induced salt gradients. AIChE J. 1992, 38, 1969-1978.
    • (1992) AIChE J. , vol.38 , pp. 1969-1978
    • Brooks, C.A.1    Cramer, S.M.2
  • 28
    • 33644779618 scopus 로고    scopus 로고
    • Applied thermodynamics: A new frontier for biotechnology.
    • Mollerup, J. M., Applied thermodynamics: A new frontier for biotechnology. Fluid Phase Equilib. 2006, 241, 205-215.
    • (2006) Fluid Phase Equilib. , vol.241 , pp. 205-215
    • Mollerup, J.M.1
  • 29
    • 35348976192 scopus 로고    scopus 로고
    • The thermodynamic principles of ligand binding in chromatography and biology.
    • Mollerup, J. M., The thermodynamic principles of ligand binding in chromatography and biology. J. Biotechnol. 2007, 132, 187-195.
    • (2007) J. Biotechnol. , vol.132 , pp. 187-195
    • Mollerup, J.M.1
  • 30
    • 46049110928 scopus 로고    scopus 로고
    • A review of the thermodynamics of protein association to ligands, protein adsorption, and adsorption isotherms.
    • Mollerup, J. M., A review of the thermodynamics of protein association to ligands, protein adsorption, and adsorption isotherms. Chem. Eng. Technol. 2008, 31, 864-874.
    • (2008) Chem. Eng. Technol. , vol.31 , pp. 864-874
    • Mollerup, J.M.1
  • 31
    • 77957682042 scopus 로고    scopus 로고
    • High-throughput isotherm determination and thermodynamic modeling of protein adsorption on mixed mode adsorbents.
    • Nfor, B. K., Noverraz, M., Chilamkurthi, S., Verhaert, P. D. E. M., High-throughput isotherm determination and thermodynamic modeling of protein adsorption on mixed mode adsorbents. J. Chromatogr., A 2010, 1217, 6829-6850.
    • (2010) J. Chromatogr., A , vol.1217 , pp. 6829-6850
    • Nfor, B.K.1    Noverraz, M.2    Chilamkurthi, S.3    Verhaert, P.D.E.M.4
  • 32
    • 28144445191 scopus 로고    scopus 로고
    • Electrostatic interaction chromatography process for protein separations: Impact of engineering analysis of biorecognition mechanism on process optimization.
    • Yamamoto, S., Electrostatic interaction chromatography process for protein separations: Impact of engineering analysis of biorecognition mechanism on process optimization. Chem. Eng. Technol. 2005, 28, 1387-1393.
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1387-1393
    • Yamamoto, S.1
  • 33
    • 0037008247 scopus 로고    scopus 로고
    • Preparative liquid chromatography.
    • Guiochon, G., Preparative liquid chromatography. J. Chromatogr., A 2002, 965, 129-161.
    • (2002) J. Chromatogr., A , vol.965 , pp. 129-161
    • Guiochon, G.1
  • 36
    • 35348910088 scopus 로고    scopus 로고
    • Development, modelling, optimisation and scale-up of chromatographic purification of a therapeutic protein.
    • Mollerup, J. M., Hansen, T. B., Kidal, S., Sejergaard, L., Staby, A., Development, modelling, optimisation and scale-up of chromatographic purification of a therapeutic protein. Fluid Phase Equilib. 2007, 261, 133-139.
    • (2007) Fluid Phase Equilib. , vol.261 , pp. 133-139
    • Mollerup, J.M.1    Hansen, T.B.2    Kidal, S.3    Sejergaard, L.4    Staby, A.5
  • 37
  • 38
    • 84859652583 scopus 로고    scopus 로고
    • Optimizing a chromatographic three component separation: A comparison of mechanistic and empiric modeling approaches.
    • Osberghaus, S., Hepbildikler, S., Nath, S., Haindl, S., Optimizing a chromatographic three component separation: A comparison of mechanistic and empiric modeling approaches. J. Chromatogr., A 2012, 1237, 86-95.
    • (2012) J. Chromatogr., A , vol.1237 , pp. 86-95
    • Osberghaus, S.1    Hepbildikler, S.2    Nath, S.3    Haindl, S.4
  • 39
    • 84868157621 scopus 로고    scopus 로고
    • Multi-dimensional fractionation and characterization of crude protein mixtures: Towards establishment of a database of protein purification process development parametes.
    • DOI: 10.1002/bit.24576.
    • Nfor, B. K., Ahamed, T., Dedem, G. v., Verhaert, P. D. E. M. et al., Multi-dimensional fractionation and characterization of crude protein mixtures: Towards establishment of a database of protein purification process development parametes. Biotechnol. Bioeng. 2012, DOI: 10.1002/bit.24576.
    • (2012) Biotechnol. Bioeng.
    • Nfor, B.K.1    Ahamed, T.2    Dedem, G.3    Verhaert, P.D.E.M.4
  • 40
    • 44349103765 scopus 로고    scopus 로고
    • Selection of pH-related parameters in ion-exchange chromatography using pH-gradient operations.
    • Ahamed, T., Chilamkurthi, S., Nfor, B. K., Verhaert, P. D. E. M., Selection of pH-related parameters in ion-exchange chromatography using pH-gradient operations. J. Chromatogr., A 2008, 1194, 22-29.
    • (2008) J. Chromatogr., A , vol.1194 , pp. 22-29
    • Ahamed, T.1    Chilamkurthi, S.2    Nfor, B.K.3    Verhaert, P.D.E.M.4
  • 41
    • 34548014804 scopus 로고    scopus 로고
    • pH-gradient ion-exchange chromatography: An analytical tool for design and optimization of protein separations.
    • Ahamed, T., Nfor, B. K., Verhaert, P. D. E. M., van Dedem, G. W. K., pH-gradient ion-exchange chromatography: An analytical tool for design and optimization of protein separations. J. Chromatogr., A 2007, 1164, 181-188.
    • (2007) J. Chromatogr., A , vol.1164 , pp. 181-188
    • Ahamed, T.1    Nfor, B.K.2    Verhaert, P.D.E.M.3    van Dedem, G.W.K.4


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