Protein Adsorption Behavior on the Surface of the Microfiltration Membrane Based on a Quartz Crystal Microbalance (QCM)

Authors

  • Zhou Wang Beijing University of Technology, Beijing 100124, P. R. China
  • Yadong Kong Beijing University of Technology, Beijing 100124, P.R. China
  • Qian Zhang Beijing University of Technology, Beijing 100124, P.R. China
  • Zhan Wang Beijing University of Technology, Beijing 100124, P.R. China
  • Natsagdorj Khaliunaa Beijing University of Technology, Beijing 100124, P.R. China
  • Rooha Khurram Beijing University of Technology, Beijing 100124, P.R. China
  • Yuenan Zhou Beijing University of Technology, Beijing 100124, P.R. China
  • Tungalagtamir Bold Mongolian University of Science and Technology, Ulaanbaatar 14191, Mongolia
  • Khan Bushra Beijing University of Technology, Beijing 100124, P.R. China

DOI:

https://doi.org/10.15377/2409-983X.2018.05.2

Keywords:

Static Adsorption, QCM, Microfiltration Membrane, Isotherm Models

Abstract

How to fast and efficiently determinate the fouling behavior of the microfiltration membrane has great significance for the industrial membrane application. In this paper, the MF membrane was put on the surface of a gold-coated quartz crystal of QCM to study the adsorption behavior of protein at different conditions. The adsorbed mass increased with the increasing of concentration, ionic strength and temperature while decreased with the increasing of pH. Then the BSA adsorption results were compared with the corresponding membrane flux in dead-end cell at the identical conditions. Furthermore, the BSA adsorption process can be described by Langmuir and Freundlich isotherms very well. These results suggested that directly putting the membrane on the surface of a gold-coated quartz crystal of QCM can be used as a rapid and efficient approach to study protein fouling on the membrane surface. This approach using QCM and a small piece of the membrane could yield quantitative information for adsorption kinetics investigation and reduce the workload in large-scale industrial project.

Downloads

Download data is not yet available.

Author Biographies

  • Zhou Wang, Beijing University of Technology, Beijing 100124, P. R. China
    Civil engineering, College of Architecture & Civil Engineering
  • Yadong Kong, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering
  • Qian Zhang, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering
  • Zhan Wang, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering
  • Natsagdorj Khaliunaa, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering
  • Rooha Khurram, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering
  • Yuenan Zhou, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering
  • Tungalagtamir Bold, Mongolian University of Science and Technology, Ulaanbaatar 14191, Mongolia
    Department of Chemical Enjineering
  • Khan Bushra, Beijing University of Technology, Beijing 100124, P.R. China
    Beijing Key Laboratory for Green Catalysis and Separation, College of Environment and Energy Engineering

References

Y. Miura, Y. Watanabe, S. Okabe, Membrane fouling in pilotscale membrane bioreactors (MBRs) treating municipal wastewater: Impact of biofilm formation, Environ. Sci. Technol. 41 (2007) 632-638. https://doi.org/10.1021/es0615371 DOI: https://doi.org/10.1021/es0615371

S.G. Yiantsios, A.J. Karabelas, An experimental study of humic acid and powdered activated carbon deposition on UF membranes and their removal by backwashing, Desalination 140 (2001) 195-209. https://doi.org/10.1016/S0011-9164(01)00368-X DOI: https://doi.org/10.1016/S0011-9164(01)00368-X

K. Kimura, N. Yamato, H. Yamamura, Y. Watanabe, Membrane biofouling in pilot-scale membrane bioreactors (MBRs) treating municipal wastewater, Environ. Sci. Technol. 39 (2005) 6293-6299. https://doi.org/10.1021/es0502425 DOI: https://doi.org/10.1021/es0502425

K. Katsoufidou, S.G. Yiantsios, A.J. Karabelas, An experimental study of UF membrane fouling by humic acid and sodium alginate solutions: the effect of backwashing on flux recovery, Desalination 220 (2008) 214-227. https://doi.org/10.1016/j.desal.2007.02.038 DOI: https://doi.org/10.1016/j.desal.2007.02.038

F., Meng, S.R. Chae, A., Drews, M. Kraume, H.S. Shin, F. Yang, 2009. Review: recent advances in membrane bioreactors (MBRs): membrane fouling and membrane material, Water Res. 43 (2009) 1489-1512. https://doi.org/10.1016/j.watres.2008.12.044 DOI: https://doi.org/10.1016/j.watres.2008.12.044

M.F. Dignac, V. Urbain, Chemical description of extracellular polymers: implication on activated sludge floc structure, Water Sci. Technol. 38 (1998) 45-53. https://doi.org/10.2166/wst.1998.0789 DOI: https://doi.org/10.2166/wst.1998.0789

B. Frølund, T. Griebe, P.H. Nielsen, Enzymatic activity in the activated-sludge floc matrix, Appl. Microbiol. Biot. 43 (1995) 755-761. https://doi.org/10.1007/s002530050481 DOI: https://doi.org/10.1007/BF00164784

B. FrØlund, R. Palmgren, Extraction of extracellular polymers from activated sludge using a cation exchange resin. Water Res. 30 (1996) 1749-1758. https://doi.org/10.1016/0043-1354(95)00323-1 DOI: https://doi.org/10.1016/0043-1354(95)00323-1

J.I. Houghton, T. Stephenson, Effect of influent organic content on digested sludge extracellular polymer content and dewater ability, Water Res. 36 (2002) 3620-3628. https://doi.org/10.1016/S0043-1354(02)00055-6 DOI: https://doi.org/10.1016/S0043-1354(02)00055-6

S. Tsuneda, S. Park, Enhancement of nitrifying biofilm formation using selected EPS produced by heterotrophic bacteria, Water Sci. Technol. 43 (2001) 197-204. https://doi.org/10.2166/wst.2001.0374 DOI: https://doi.org/10.2166/wst.2001.0374

J.Y. Yoon, J.H. Kim, W.S. Kim, Interpretation of protein adsorption phenomena onto functional microspheres, Colloid. Surface. B 12 (1998) 15-22. https://doi.org/10.1016/S0927-7765(98)00045-9 DOI: https://doi.org/10.1016/S0927-7765(98)00045-9

H. Nagaoka, S. Yamanishi, A. Miya, Modeling of biofouling by extracellular polymers in a membrane separation activated sludge system, Water Sci. Technol. 38 (1998) 497- 504. https://doi.org/10.2166/wst.1998.0705 DOI: https://doi.org/10.2166/wst.1998.0705

S. Ognier, C. Wisniewski, Influence of macromolecule adsorption during filtration of a membrane bioreactor mixed liquor suspension, J. Membr. Sci. 209 (2007) 27-37. https://doi.org/10.1016/S0376-7388(02)00123-0 DOI: https://doi.org/10.1016/S0376-7388(02)00123-0

S. Rosenberger, H. Evenblij, S. Tepoele, T. Wintgens, C. Laabs, The importance of liquid phase analyses to understand fouling in membrane assisted activated sludge Processes-six case studies of different European research groups, J. Membr. Sci. 263 (2005) 113-126. https://doi.org/10.1016/j.memsci.2005.04.010 DOI: https://doi.org/10.1016/j.memsci.2005.04.010

M. Yao, K. Zhang, L. Cui, Characterization of proteinpolysaccharide ratios on membrane fouling, Desalination 259 (2010) 11-16. https://doi.org/10.1016/j.desal.2010.04.049 DOI: https://doi.org/10.1016/j.desal.2010.04.049

Y. Ye, P. Le Clech, V. Chen, Fouling mechanisms of alginate solutions as model extracellular polymeric substances, Desalination 175 (2005) 7-20. https://doi.org/10.1016/j.desal.2004.09.019 DOI: https://doi.org/10.1016/j.desal.2004.09.019

Y. Ye, P. Le Clech, V. Chen, Evolution of fouling during crossflow filtration of model EPS solutions, J. Membr. Sci. 264 (2005) 190-199. https://doi.org/10.1016/j.memsci.2005.04.040 DOI: https://doi.org/10.1016/j.memsci.2005.04.040

K. Nakamura, K. Matsumoto, Protein adsorption properties on a microfiltration membrane: a comparison between static and dynamic adsorption methods, J. Membr. Sci. 285 (2006) 126-136. https://doi.org/10.1016/j.memsci.2006.08.012 DOI: https://doi.org/10.1016/j.memsci.2006.08.012

H. Susanto, M. Ulbricht, Influence of ultrafiltration membrane characteristics on adsorptive fouling with dextrans, J. Membr. Sci. 266 (2005) 132-142. https://doi.org/10.1016/j.memsci.2005.05.018 DOI: https://doi.org/10.1016/j.memsci.2005.05.018

P. Aimar, S. Baklouti, V. Sanchez, Membrane-solute interaction: influence on pure solvent transport during ultrafiltration, J. Membr. Sci. 29 (1986) 207-224. https://doi.org/10.1016/S0376-7388(00)82470-9 DOI: https://doi.org/10.1016/S0376-7388(00)82470-9

S.M.G. Demneh, B. Nasernejad, H. Modarres, Modeling investigation of membrane biofouling phenomena by considering the adsorption of protein, polysaccharide and humic acid, Colloid. Surface. B. (2011) 108-114. https://doi.org/10.1016/j.colsurfb.2011.06.018 DOI: https://doi.org/10.1016/j.colsurfb.2011.06.018

Y.N. Zhou, Z. Wang, Q. Zhang, X.J. Xi, J. Zhang, W.T. Yang, Equilibrium and thermodynamic studies on adsorption of BSA using PVDF microfiltration membrane, Desalination 307 (2012) 61-67. https://doi.org/10.1016/j.desal.2012.09.004 DOI: https://doi.org/10.1016/j.desal.2012.09.004

J.Y. Yoon, J.H. Kim, W.S. Kim, The relationship of interaction forces in the protein adsorption onto polymeric microspheres, Colloid Surf. A-Physicochem. Eng. Asp. 153 (1999) 413-419. https://doi.org/10.1016/S0927-7757(98)00533-0 DOI: https://doi.org/10.1016/S0927-7757(98)00533-0

C.G. Marxer, M.C. Coen, L. Schlapbach, Study of adsorption and viscoelastic properties of proteins with a quartz crystal microbalance by measuring the oscillation amplitude, J. Colloid Interface Sci. 261 (2003) 291-298. https://doi.org/10.1016/S0021-9797(03)00089-4 DOI: https://doi.org/10.1016/S0021-9797(03)00089-4

A.G. Hemmersam, M. Foss, J. Chevallier, F. Besenbacher, Adsorption of fibrinogen on tantalum oxide, titanium oxide and gold studied by the QCM-D technique, Colloid. Surface.B. 43 (2005) 208-215. https://doi.org/10.1016/j.colsurfb.2005.04.007 DOI: https://doi.org/10.1016/j.colsurfb.2005.04.007

Y. Liu, X. Yu, R. Zhao, Quartz crystal biosensor for real-time monitoring of molecular recognition between protein and small molecular medicinal agents, Biosens. Bioelectron. 19 (2003) 9-19. https://doi.org/10.1016/S0956-5663(03)00127-1 DOI: https://doi.org/10.1016/S0956-5663(03)00127-1

M.S. Lord, M.H. Stenzel, A. Simmons, B.K. Milthorpe, The effect of charged groups on protein interactions with poly (HEMA) hydrogels, Biomaterials 27 (2006) 567-575. https://doi.org/10.1016/j.biomaterials.2005.06.010 DOI: https://doi.org/10.1016/j.biomaterials.2005.06.010

F. Hook, J. Voros, M. Rodahl, A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide light mode spectroscopy, and quartz crystal microbalance/dissipation, Colloid. Surface. B. 24 (2002) 155-170. https://doi.org/10.1016/S0927-7765(01)00236-3 DOI: https://doi.org/10.1016/S0927-7765(01)00236-3

F. Yin, S. Park, HK. Shin, Study of hemoglobinoctadecylamine Lb film formation and deposition by compressibility analyse, QCM and AFM. Curr. Appl. Phys. 6 (2006) 728-734. https://doi.org/10.1016/j.cap.2005.04.028 DOI: https://doi.org/10.1016/j.cap.2005.04.028

M.S. Lord, B.G. Cousins, P.J. Doherty, The effect of silica nanoparticulate coatings on serum protein adsorption and cellular response, Biomaterials 27 (2006) 4856-4862. https://doi.org/10.1016/j.biomaterials.2006.05.037 DOI: https://doi.org/10.1016/j.biomaterials.2006.05.037

G.V. Lubarsky, M.R. Davidson, R.H. Bradley, Hydrationdehydration of adsorbed protein films studied by AFM and QCM, Biosens. Bioelectron. 22 (2006) 1275-1281. https://doi.org/10.1016/j.bios.2006.05.024 DOI: https://doi.org/10.1016/j.bios.2006.05.024

X. Chu, Z.L. Zhao, G.L. Shen, Quartz crystal microbalance immunoassay with dendritic amplification using colloidal gold immunocomplex, Sensor. Actuat. B-Chem. 114 (2006) 696- 704. https://doi.org/10.1016/j.snb.2005.06.014 DOI: https://doi.org/10.1016/j.snb.2005.06.014

J.S. Kavanaugh, W.F. Moo-Penn, A. Arnone, Accommodation of insertions in helixes: The mutation in hemoglobin catonsville (Pro37. alpha.-Glu-Thr 38. alpha.) generates a 310.fwdarw. alpha. Bulge, Biochemistry 32 (1993) 2509-2513. https://doi.org/10.1021/bi00061a007 DOI: https://doi.org/10.1021/bi00061a007

A. Welle, A. Chiumiento, R. Barbucci, Biomolecular Engineering 24 (2006) 87. https://doi.org/10.1016/j.bioeng.2006.05.027 DOI: https://doi.org/10.1016/j.bioeng.2006.05.027

B. Van der Bruggen, L. Braeken, C. Vandecasteele, Flux decline in nanofiltration due to adsorption of organic compounds, Sep. Purif. Technol. 29 (2002) 23-31. https://doi.org/10.1016/S1383-5866(01)00199-X’ DOI: https://doi.org/10.1016/S1383-5866(01)00199-X

C. Velasco, J.I. Calvo, L. Palacio, J. Carmona, P. Prádanos, A. Hernández, Flux kinetics, limit and critical fluxes for low pressure dead-end microfiltration. The case of BSA Filtration through a Positively Charged Membrane, Chem. Eng. Sci. 129 (2015) 58-68. https://doi.org/10.1016/j.ces.2015.02.003 DOI: https://doi.org/10.1016/j.ces.2015.02.003

H.P. Chu, X. Li, Membrane fouling in a membrane bioreactor (MBR): sludge cake formation and fouling characteristics, Biotechnol. Bioeng. 90 (2005) 323-331. https://doi.org/10.1002/bit.20409 DOI: https://doi.org/10.1002/bit.20409

K.L. Jones, C.R. O'Melia, Protein and humic acid adsorption onto hydrophilic membrane surfaces: effects of pH and ionic strength, J. Membr. Sci. 165 (2000) 31-46. https://doi.org/10.1016/S0376-7388(99)00218-5 DOI: https://doi.org/10.1016/S0376-7388(99)00218-5

A. Fane, C. Fell, A. Suki, The effect of pH and ionic environment on the ultrafiltration of protein solutions with retentive membranes, J. Membr. Sci. 16 (1983) 195-210. https://doi.org/10.1016/S0376-7388(00)81310-1 DOI: https://doi.org/10.1016/S0376-7388(00)81310-1

C.A. Haynes, W. Norde, Globular proteins at solid/liquid interfaces, Colloid. Surface. B. 2 (1994) 517-566. https://doi.org/10.1016/0927-7765(94)80066-9 DOI: https://doi.org/10.1016/0927-7765(94)80066-9

M. Hashino, K. Hirami, T. Ishigami, Y. Ohmukai, T. Maruyama, N. Kubota, H. Matsuyama, Effect of kinds of membrane materials on membrane fouling with BSA, J. Membr. Sci. 384 (2011) 157- 165. https://doi.org/10.1016/j.memsci.2011.09.015 DOI: https://doi.org/10.1016/j.memsci.2011.09.015

J. Hu, S.J. Li, B.L. Liu, Adsorption of BSA onto sulfonated microspheres, Biochem. Eng. J. 23 (2005) 259-263. https://doi.org/10.1016/j.bej.2005.01.018 DOI: https://doi.org/10.1016/j.bej.2005.01.018

X.M. Yan, J. Kong, C.C. Yang, G.Q. Fu, Facile synthesis of hairy core-shell structured magnetic polymer submicrospheres and their adsorption of bovine serum albumin, J. Colloid Interf. Sci. 445 (2015) 9-15. https://doi.org/10.1016/j.jcis.2014.12.022 DOI: https://doi.org/10.1016/j.jcis.2014.12.022

H.J. Mo, K.G. Tay, H.Y. Ng, Fouling of reverse osmosis membrane by protein (BSA): Effects of pH, calcium, magnesium, ionic strength and temperature, J. Membr. Sci. 315 (2008) 28-35. https://doi.org/10.1016/j.memsci.2008.02.002 DOI: https://doi.org/10.1016/j.memsci.2008.02.002

U.V. Dortmund, F. Chemie, O.H Strass, O. Hollmann, C. Czeslik, Characterization of a Planar Poly(acrylic acid) Brush as a Materials Coating for Controlled Protein Immobilization, Langmuir 22 (2006) 3300-3305. https://doi.org/10.1021/la053110y DOI: https://doi.org/10.1021/la053110y

D. Xu, X.L. Tan, C.L. Chen, X.K. Wang, Adsorption of Pb (II) from aqueous solution to MX-80 bentonite: effect of pH, ionic strength, foreign ions and temperature, Applied Clay Science 41 (2008) 37-46. https://doi.org/10.1016/j.clay.2007.09.004 DOI: https://doi.org/10.1016/j.clay.2007.09.004

C.V. Vidal, A.O. Juan, A.I. Muñoz, Adsorption of bovine serum albumin on CoCrMo surface: Effect of temperature and protein concentration, Colloid. Surface B. 80 (2010) 1- 11. https://doi.org/10.1016/j.colsurfb.2010.05.005 DOI: https://doi.org/10.1016/j.colsurfb.2010.05.005

Y.Y. Wang, T. Wang, Y.L. Su, F.B. Peng, H. Wu, Z.Y. Jiang, Remarkable Reduction of Irreversible Fouling and Improvement of the Permeation Properties of Poly(ether sulfone) Ultrafiltration Membranes by Blending with Pluronic F127, Langmuir 21 (2005) 11856-11862. https://doi.org/10.1021/la052052d DOI: https://doi.org/10.1021/la052052d

A.D. Marshall, P.A. Munro, G. Trägårdh, The effect of protein fouling in microfiltration and ultrafiltration on permeate flux, protein retention and selectivity: A literature review, Desalination 91 (1993) 65-108. https://doi.org/10.1016/0011-9164(93)80047-Q DOI: https://doi.org/10.1016/0011-9164(93)80047-Q

Nigam, M.O., Bansal B., Chen X.D, Fouling and cleaning of whey protein concentrate fouled ultrafiltration membranes, Desalination 218 (2008) 313-322. https://doi.org/10.1016/j.desal.2007.02.027 DOI: https://doi.org/10.1016/j.desal.2007.02.027

X.S. Yi, W.X. Shi, S.L. Yua, Y. Wang, N. Suna, L.M. Jin, S. Wang, 2011. Isother and kinetic behavior of adsorption of anion polyacrylamide (APAM) from aqueous solution using two kinds of PVDF UF membranes, J. Hazard. Mater. 189 (2011) 495-501. https://doi.org/10.1016/j.jhazmat.2011.02.063 DOI: https://doi.org/10.1016/j.jhazmat.2011.02.063

T. Kopac, K. Bozgeyik, J. Yener, Effect of pH and temperature on the adsorption of bovine serum albumin onto titanium dioxide, Colloid Surf. A- Physicochem. Eng. Asp. 322 (2008) 19-28. https://doi.org/10.1016/j.colsurfa.2008.02.010 DOI: https://doi.org/10.1016/j.colsurfa.2008.02.010

T. Trongsatitkul, B.M. Budhlall, Temperature dependence of serum protein adsorption in PEGylated PNIPAm Microgels, Colloid Surface B. 103 (2013) 244-252. https://doi.org/10.1016/j.colsurfb.2012.10.053 DOI: https://doi.org/10.1016/j.colsurfb.2012.10.053

N. Shamim, L. Hong, K. Hidajat, M.S. Uddin, Thermosensitive-polymer-coated magnetic nanoparticles: Adsorption and desorption of Bovine Serum Albumin, J. Colloid Interface Sci. 304 (2006) 1-8. https://doi.org/10.1016/j.jcis.2006.08.047 DOI: https://doi.org/10.1016/j.jcis.2006.08.047

C. Veerman, L.M.C. Sagis, J. Heck, E.V.D. Linden, Mesostructure of fibrillar bovine serum albumin gels, Int. J. Biol. Macromol. 31 (2003) 139-146. https://doi.org/10.1016/S0141-8130(02)00074-0 DOI: https://doi.org/10.1016/S0141-8130(02)00074-0

M. Alkan, O. Demirbas, S. Celikcapa, M. Dogan, Sorption of acid red 57 from aqueous solution onto sepiolite, J. of Hazard. Mater. 116 (2004) 135-145. https://doi.org/10.1016/j.jhazmat.2004.08.003 DOI: https://doi.org/10.1016/j.jhazmat.2004.08.003

Y.Y. Zuo, R. Gitiafroz, E. Acosta, Z. Policova, P. N. Cox, M.L. Hair, A.W. Neumann, Effect of Humidity on the Adsorption Kinetics of Lung Surfactant at Air-Water Interfaces, Langmuir 21 (2005) 10593-10601. https://doi.org/10.1021/la0517078 DOI: https://doi.org/10.1021/la0517078

N. Chandrasekaran, S. Dimartino, C.J. Fee, Study of the adsorption of proteins on stainless steel surfaces using QCM-D, Chem. Eng. Res. Des. 91 (2013) 1674-1683. https://doi.org/10.1016/j.cherd.2013.07.017 DOI: https://doi.org/10.1016/j.cherd.2013.07.017

K. C. Dee, D.A. Puleo, R. Bizios, Biomaterials, in An Introduction to Tissue biomaterial interactions, New Jersey, NJ: John Willey and Sons Inc. press. (2002) 165-214. https://doi.org/10.1002/0471270598 DOI: https://doi.org/10.1002/0471270598

A.R. Sarasam, R.K. Krishnswamy, S.V. Madihally, Blending ehitosan with Polycaprolactone: effects on Physicochemical and antibacterial properties, Biornacromoleeules 7 (2006) 1131-1138. https://doi.org/10.1021/bm050935d DOI: https://doi.org/10.1021/bm050935d

L. Feng, J.D. Andrade, Protein adsorption on low temperature isotropic carbon: III. isotherms, competitivity, desorption and exchange of human albumin and fibrinogen, Biomaterials 15 (1994) 323-33. https://doi.org/10.1016/0142-9612(94)90243-7 DOI: https://doi.org/10.1016/0142-9612(94)90243-7

L. Feng, J.D. Andrade, Structure and adsorption properties of fibrinogen, In Proteins at interfaces II; Horbett T., et al., ACS Symposium Series; American Chemical Society: Washington, DC (1995) 66-79. https://doi.org/10.1021/bk-1995-0602.ch005 DOI: https://doi.org/10.1021/bk-1995-0602.ch005

M.Q. Zhang, T. Desai, M. Ferrari, Proteins and cells on PEG immobilized silicon surfaces, Biomaterials 19 (1998) 953- 960. https://doi.org/10.1016/S0142-9612(98)00026-X DOI: https://doi.org/10.1016/S0142-9612(98)00026-X

P. Le-Clech, V. Chen, T.A.G. Fane, Fouling in membrane bioreactors used in wastewater treatment, J. Membr. Sci. 284 (2006) 17-53. https://doi.org/10.1016/j.memsci.2006.08.019 DOI: https://doi.org/10.1016/j.memsci.2006.08.019

J.L.G. Ribelles, Blending polysaccharides with biodegradable Polymers. I. Properties of chitosan/polycaprolactone blends, J. Biomed. Mater. Res. B 85 (2008) 303-313. https://doi.org/10.1002/jbm.b.30947 DOI: https://doi.org/10.1002/jbm.b.30947

G.J. Zhang, S.L. Ji, X. Gao, Z.Z. Liu, Adsorptive fouling of extracellular polymeric substances with polymeric ultrafiltration membranes, J. Membr. Sci. 309 (2009) 28-35. https://doi.org/10.1016/j.memsci.2007.10.012 DOI: https://doi.org/10.1016/j.memsci.2007.10.012

Downloads

Published

2018-12-31

Issue

Section

Articles

How to Cite

1.
Protein Adsorption Behavior on the Surface of the Microfiltration Membrane Based on a Quartz Crystal Microbalance (QCM). J. Chem. Eng. Res. Updates. [Internet]. 2018 Dec. 31 [cited 2026 Mar. 4];5(1):10-9. Available from: https://avanti-journals.com/index.php/jceru/article/view/892

Similar Articles

11-12 of 12

You may also start an advanced similarity search for this article.

Most read articles by the same author(s)