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http://yadda.icm.edu.pl:443/baztech/element/bwmeta1.element.baztech-a409aa2b-6cd8-48a7-a7f4-6dba463fecc8

Czasopismo

Environment Protection Engineering

Tytuł artykułu

Influence of pH on permeability of ceramic membranes and selectivity in ultrafiltration of model BSA and myoglobin solutions

Autorzy Gabriel-Półrolniczak, U.  Szaniawska, D.  Ćwirko, K. 
Treść / Zawartość
Warianty tytułu
Języki publikacji EN
Abstrakty
EN The results of ultrafiltration tests carried out with model BSA and myoglobin solutions using ceramic 50 and 150 kDa membranes have been presented. Membrane permeability and selectivity were investigated in function of pH, transmembrane pressure (TMP) as well as molecular modelling data for proteins such as size, geometrical parameters and pH of minimal free energy of folding. The study has shown that the permeate flux J(v) depends on TMP, whereas the protein rejection is mainly influenced by pH. The results demonstrated that molecular modelling data are not sufficient to explain the membrane behaviour and the membrane–protein charge interactions and fouling effects must be also considered to explain the rejection mechanisms.
Słowa kluczowe
PL ultrafiltracja   membrany ceramiczne   przepuszczalność błony   albumina surowicy bydlęcej   albumina (BSA)   albuminy surowicy   mioglobina   mikrofiltracja  
EN ultrafiltration   ceramic membranes   membrane permeability   bovine serum albumin   BSA   myoglobin   microfiltration  
Wydawca Oficyna Wydawnicza Politechniki Wrocławskiej
Czasopismo Environment Protection Engineering
Rocznik 2014
Tom Vol. 40, nr 4
Strony 135--141
Opis fizyczny Bibliogr. 15 poz., rys.
Twórcy
autor Gabriel-Półrolniczak, U.
  • Transport Engineering and Economics Faculty, Maritime University of Szczecin, ul. Henryka Pobożnego 11, 70-507 Szczecin, Poland
autor Szaniawska, D.
  • Transport Engineering and Economics Faculty, Maritime University of Szczecin, ul. Henryka Pobożnego 11, 70-507 Szczecin, Poland, d.szaniawska@am.szczecin.pl
autor Ćwirko, K.
  • Marine Engineering Faculty, Maritime University of Szczecin, Wały Chrobrego 1–2, 70-500 Szczecin, Poland
Bibliografia
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[2] HUANG L., MORRISSEY M.T., Fouling of membranes during microfiltration of surimi wash water. Roles of pore blocking and surface cake formation, J. Membrane Sci., 1998, 144, 113.
[3] SRIDANG P.C., KAIMAN J., POTTIER A., WISNIEWSKI C., Benefits of MBR in seafood wastewater treatment and water reuse, Desalination, 2006, 200, 712.
[4] AFONSO M.D., BÓRQUEZ R., Nanofiltration of wastewaters from fish meal industry, Desalination, 2002, 151, 131.
[5] CASANI S., LETH T., KNØCHEL S., Water reuse in a shrimp processing line. Safety considerations using a HACCP approach, Food Control, 2006, 17, 540.
[6] CASA E.J., GUADIX A., IBANEZ I., GUADIX E.M., Influence of pH and salt concentration on cross-flow microfiltration of BSA through ceramic membranes, Biochem. Eng. J., 2007, 33, 110.
[7] NOORDMAN T.R., KETELAAR T.H., DONKERS F., WESSELINGH J.A., Concentration and desalination of protein solutions by ultrafiltration, Chem. Eng. Sci., 2002, 57, 693.
[8] KUCA M., SZANIAWSKA D., Application of microfiltration and ceramic membranes for treatment of salted aqueous effluents from fish processing, Desalination, 2009, 241, 227.
[9] KUCA M., Application of ultrafiltration for regeneration of waste brine from fish processing, Thesis, West Pomeranian University of Technology, Szczecin 2009 (in Polish).
[10] Food Chemistry. Saccharides, Lipids and Proteins, Z.E. Sikorski (Ed.), Vol. 2, Wydawnictwa Naukowo- Techniczne WNT, Warsaw 2007 (in Polish).
[11] PEDRETTI A., VILLA L., VISTOLI G., Vega. A versatile program to convert, handle and visualize molecular structure on Windows-based PCs, J. Mol. Graph., 2002, 21, 47.
[12] LI H., ROBERTSON A.D., JENSEN J.H., Very fast empirical prediction and rationalization of protein pKa values, Proteins: Structure, Function, and Bioinformatics, 2005, 61, 704.
[13] KISSICK D.J., DETTMAR C.M., BECKER M., MULICHAK A.M., CHEREZOV V., GINELL S.L., BATTAILE K.P., KEEFE L.J., FISCHETTI R.F., SIMPSON G.J., Towards protein-crystal centering using second-harmonic generation (SHG) microscopy, Acta Crystallogr., 2013, Sect. D, 69, 843.
[14] BUJACZ A., Structures of bovine, equine and leporine serum albumin, Acta Crystallogr., 2012, Sect. D, 68, 1278.
[15] PETTERSEN E.F., GODDARD T.D., HUANG C.C., COUCH G.S., GREENBLATT D.M., MENG E.C., FERRIN T.E., UCSF Chimera. A visualization system for exploratory research and analysis, J. Comput. Chem., 2004, 25 (13), 1605
Kolekcja BazTech
Identyfikator YADDA bwmeta1.element.baztech-a409aa2b-6cd8-48a7-a7f4-6dba463fecc8
Identyfikatory
DOI 10.5277/epe140411