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DOI QR Code

Separation and flux characteristics in cross-flow ultrafiltration of bovine serum albumin and bovine hemoglobin solutions

  • Hsiao, Ruey-Chang (Department of Chemical and Material Engineering, Lung Hwa University of Science and Technology) ;
  • Hung, Chia-Lin (Department of Chemical Engineering and Materials Science, Yuan Ze University) ;
  • Lin, Su-Hsia (Department of Chemical and Materials Engineering, Nanya Institute of Technology) ;
  • Juang, Ruey-Shin (Department of Chemical Engineering and Materials Science, Yuan Ze University)
  • 투고 : 2010.09.06
  • 심사 : 2011.04.06
  • 발행 : 2011.04.25

초록

The flux behavior in the separation of equimolar bovine serum albumin (BSA) and bovine hemoglobin (HB) in aqueous solutions by cross-flow ultrafiltration (UF) was investigated, in which polyacylonitrile membrane with a molecular weight cut-off (MWCO) of 100 kDa was used. BSA and HB have comparable molar mass (67,000 vs. 68,000) but different isoelectric points (4.7 vs. 7.1). The effects of process variables including solution pH (6.5, 7.1, and 7.5), total protein concentration (1.48 and 7.40 ${\mu}M$), transmembrane pressure (69, 207, and 345 kPa), and solution ionic strength (with or without 0.01 M NaCl) on the separation were examined. It was shown that the ionic strength had a negligible effect on separation performance under the conditions studied. Although BSA and HB are not rigid bodies, the flux decline in the present cross-flow UF did not result from the mechanism of cake filtration with compression. In this regard, the specific cake resistance when pseudo steady-state was reached was evaluated and discussed.

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참고문헌

  1. Avramescu, M.E., Borneman, Z. and Wessling, M. (2003), "Mixed-matrix membrane adsorbers for protein separation", J. Chromato. A, 1006(1-2), 171-183. https://doi.org/10.1016/S0021-9673(03)00562-4
  2. Becht, N.O., Malik, D.J. and Tarleton, E.S. (2008), "Evaluation and comparison of protein ultrafiltration testresults: Dead-end stirred cell compared with a cross-flow system", Sep. Purif. Technol., 62(1), 228-239. https://doi.org/10.1016/j.seppur.2008.01.030
  3. Bhattacharjee, S., Ghosh, S., Datta, S. and Bhattacharjee, C. (2006), "Studies on ultrafiltration of casein whey using a rotating disk module: Effects of pH and membrane disk rotation", Desalination, 195(1-3), 95-108. https://doi.org/10.1016/j.desal.2005.09.037
  4. Causserand, C., Kara, Y. and Aimar, P. (2001), "Protein fractionation using selective adsorption on clay surface before filtration", J. Membr. Sci. 186(2), 165-181. https://doi.org/10.1016/S0376-7388(01)00332-5
  5. Charcosset, C. (2006), "Membrane process in biotechnology: An overview", Biotechnol. Adv., 24(5), 482-492. https://doi.org/10.1016/j.biotechadv.2006.03.002
  6. Chen, H.L., Chen, Y.S. and Juang, R.S. (2007), "Separation of surfactin from fermentation broths by acid precipitation and two-stage dead-end ultrafiltration processes", J. Membr. Sci., 299(1-2), 114-121. https://doi.org/10.1016/j.memsci.2007.04.031
  7. Choi, S.W., Park, J.M., Chang, Y., Yoon, J.Y., Haam, S., Kim, J.H. and Kim, W.S. (2003), "Effect of electrostatic repulsive force on the permeate flux and flux modeling in the microfiltration of negatively charged microspheres", Sep. Sci. Technol., 30(1), 69-77.
  8. Chollangi, A. and Hossain, M.M. (2007), "Separation of proteins and lactose from dairy wastewater," Chem. Eng. Process., 46(5), 398-404. https://doi.org/10.1016/j.cep.2006.05.022
  9. Christel, C., Yilmaz, K. and Pierre, A. (2001), "Protein fraction using selective adsorption on clay surface before filtration", J. Membr. Sci., 186(2), 165-181. https://doi.org/10.1016/S0376-7388(01)00332-5
  10. de Wit, J.N. and van Kessel, T. (1996), "Effects of ionic strength on the solubility of whey protein products: A colloid chemical approach", Food Hydrocolloids, 10(2), 143-149. https://doi.org/10.1016/S0268-005X(96)80028-2
  11. Eijndhoven-van, R.H.C.M., Saksena, S. and Zydney, A.L. (1995), "Protein fractionation using electrostatic interactions in membrane filtration", Biotechnol. Bioeng., 48(4), 406-414. https://doi.org/10.1002/bit.260480413
  12. Feins, M. and Sirkar, K.K. (2005), "Novel internally staged ultrafiltration for protein purification", J. Membr. Sci., 248(1-2), 137-148. https://doi.org/10.1016/j.memsci.2004.09.035
  13. Ghosh, R. (2002), "Study of membrane fouling by BSA using pulsed injection technique", J. Membr. Sci., 195(1), 115-123. https://doi.org/10.1016/S0376-7388(01)00550-6
  14. Hwang, K.J. and Sz, P.Y. (2010), "Filtration characteristics and membrane fouling in cross-flow microfiltration of BSA/dextran binary suspension", J. Membr. Sci., 347, 75-82. https://doi.org/10.1016/j.memsci.2009.10.008
  15. Lin, S.H., Hung, C.L. and Juang, R.S. (2008a), "Applicability of exponential time dependence of flux decline during dead-end ultrafiltration of binary protein solutions", Chem. Eng. J., 145(2), 211-217. https://doi.org/10.1016/j.cej.2008.04.003
  16. Lin, S.H., Hung, C.L. and Juang, R.S. (2008b), "Effect of operating parameters on the separation of proteins in aqueous solutions by dead-end ultrafiltration", Desalination, 234, 116-125. https://doi.org/10.1016/j.desal.2007.09.077
  17. Musale, D.A. and Kulkarni, S.S. (1997), "Relative rates of protein transmission through poly(acrylonitrile) based ultrafiltration membranes", J. Membr. Sci., 136(1-2), 13-23. https://doi.org/10.1016/S0376-7388(97)00179-8
  18. Saxena, A., Bijay, B.P., Tripathi, P., Kumar, M. and Shahi, V.K. (2009), "Membrane-based techniques for the separation and purification of proteins: An overview", Adv. Colloid Interface Sci., 145(1-2), 1-22. https://doi.org/10.1016/j.cis.2008.07.004
  19. Keskinler, B., Akay, G., Bayhan, Y.K. and Erham, E. (2002), "Effect of ionic environment on crossflow microfiltration behavior of yeast suspension", J. Membr. Sci., 206(1-2), 351-360. https://doi.org/10.1016/S0376-7388(01)00773-6
  20. Kimberly, L.J. and Charles, R.O. (2000), "Protein and humic acid adsorption onto hydrophilic membrane surfaces: Effects of pH and ionic strength", J. Membr. Sci., 165(1), 31-46. https://doi.org/10.1016/S0376-7388(99)00218-5
  21. Kumar, K. and De, S. (2010), "Modeling of flux enhancement in presence of concentration polarization by pressure pulsation during laminar cross flow ultrafiltration", Membrane Water Treatment, an Intern. J., 1, 253-271. https://doi.org/10.12989/mwt.2010.1.4.253
  22. Salehi, E. and Madaeni, S.S. (2010), "Influence of conductive surface on adsorption behavior of ultrafiltration membrane", Appl. Surf. Sci., 256(10), 3010-3017. https://doi.org/10.1016/j.apsusc.2009.11.065
  23. Schippers, J.C. and Verdouw, J. (1980), "The modified fouling index, a method of determining fouling characteristics of water", Desalination, 32, 137-148. https://doi.org/10.1016/S0011-9164(00)86014-2
  24. Song, L. (1998), "A new model for the calculation of the limiting flux in ultrafiltration", J. Membr. Sci., 144(1-2), 173-185. https://doi.org/10.1016/S0376-7388(98)00057-X
  25. Stopka, J., Bugan, S.G., Schlosser, S. and Larbot, A. (2001), "Microfiltration of beer yeast suspension through stamped ceramic membrane", Sep. Purif. Technol., 25(1-3), 533-546.
  26. Teng, M.Y., Lin, S.H. and Juang, R.S. (2006), "Effect of ultrasound on the separation of binary protein mixtures by cross-flow ultrafiltration", Desalination, 200, 280-282. https://doi.org/10.1016/j.desal.2006.03.338
  27. Wang, Y. and Rodgers, V.G.J. (2008), "Free-solvent model shows osmotic pressure is the dominant factor in limiting flux during protein ultrafiltration", J. Membr. Sci., 320(1-2), 335-343. https://doi.org/10.1016/j.memsci.2008.04.014
  28. William, K., Elizabeth, K. and Geoffrey, B.C. (1995), "High velocity reversed-phase chromatography of proteins and peptides: Use of conventional $C_{18}$, 300 $\AA$, 15 mm particles", J. Chromato. A, 690, 9-19. https://doi.org/10.1016/0021-9673(94)01013-5