Effect of Conductivity Control on the Separation of Whey Proteins by Bipolar Membrane Electroacidification

Journal of Agricultural and Food Chemistry

Volumn 52, Issue 7, 2004, Pages 1980-1984

  Bazinet, Laurent ^a,c   Ippersiel, Denis ^a   Mahdavi, Behzad ^b  

^a FOOD RESEARCH AND DEVELOPMENT CENTRE   (Canada)

^b HYDRO QUÉBEC   (Canada)

^c UNIVERSITÉ LAVAL   (Canada)

Author keywords

Conductivity; Electrochemical acidification; Fractionation; Whey protein

Indexed keywords

POTASSIUM CHLORIDE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; WHEY PROTEIN;

ACIDIFICATION; ARTICLE; BIPOLAR MEMBRANE ELECTROACIDIFICATION; CHEMICAL COMPOSITION; CONDUCTANCE; DISPERSION; ELECTROCHEMISTRY; ELECTRODIALYSIS; KINETICS; PH; PRECIPITATION; PROTEIN ANALYSIS; VISCOSITY; WHEY;

CHEMICAL FRACTIONATION; ELECTRIC CONDUCTIVITY; ELECTRICITY; ELECTROCHEMISTRY; HYDROGEN-ION CONCENTRATION; MILK PROTEINS; PRECIPITATION; SOLUBILITY; SOLUTIONS;

MUS;

EID: 1842430851     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0348469     Document Type: Article

References (24)

1. Ayers, J. S.; Petersen, M. J. Whey protein recovery using a range of novel ion exchangers. N. Z. J. Dairy Sci. Technol. 1985, 20, 129-142.
2. Skudder, P. J. Evaluation of a porous silica-based ion-exchange medium for the production of protein fraction from rennet- and acid-whey. J. Dairy Res. 1985, 52, 167-181.
3. Al-Mashikh, S. A.; Nakai, S. Reduction of β-lactoglobulin content of cheese whey by polyphosphate precipitation. J. Food Sci. 1987, 52, 1237-1240.
4. Pearce, R. J. Thermal separation of β-lactoglobulin and α-lactalbumin in bovine cheddar cheese whey. Aust. J. Dairy Technol. 1983, 38, 144-149.
5. Pierre, A.; Fauquant, J. Principes pour un procédé industriel de fractionnement des protéines du lactosérum. Lait 1986, 66 (4), 405-419.
6. Barbier, J. P.; Rialland, J. P. Selective separation of alpha-lactalbumin from whey proteins. European Patent No. 0209414 A1, 1987.
7. Bramaud, C.; Aimar, P.; Daufin, G. Optimisation of a whey protein fractionation process based on the selective precipitation of α-lactalbumin. Lait 1997, 77, 411-423.
8. Mailliart, P.; Ribadeau-Dumas, B. Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting-out at low pH. J. Food Sci. 1988, 53 (3), 743-745, 752.
9. Amundson, C. H.; Watanawanichakorn, S.; Hill, C. G., Jr. Production of Enriched Protein Fractions of β-lactoglobulin and α-lactalbumin from Cheese Whey. J. Food Process. Preserv. 1982, 6, 55-71.
10. Slack, A. W.; Amundson, C. H.; Hill, C. G. Production of enriched β-lactoglobulin and α-lactalbumin whey protein fractions. J. Food Process. Preserv. 1986, 10, 19-30.
11. Bazinet, L.; Ippersiel, D.; Mahdavi, B. Separation of whey protein by bipolar membrane electroacidification. Innovative Food Sci. Emerging Technol. 2004, 5, 17-25.
12. Bazinet, L.; Lamarche, F.; Ippersiel, D.; Amiot, J. Bipolar Membrane Electroacidification to Produce Bovine Milk Casein Isolate. J. Agric. Food Chem. 1999, 47, 5291-5296.
13. s2 genetic variants. Lait 1992, 72, 235-247.
14. Bradford, M. M. A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding. Anal. Biochem. 1976, 72, 248-254.
15. Bazinet, L.; Ippersiel, D.; Gendron, C.; Beaudry, J.; Mahdavi, B.; Amiot, J.; Lamarche, F. Cationic Balance in Skim Milk during Bipolar Membrane Electroacidification. J. Membr. Sci. 2000, 173, 201-209.
16. AOAC International. Method 930-30: Ash of dried Milk. In Official Methods of Analysis of AOAC International, 16th ed.; The Association: Arlington, VA, 1995; Vol 2.
17. SAS Institute Inc. In SAS/Stat user's guide, 4th ed.; SAS Institute Inc.: Cary, NC, 1989; Vol. 2, Version 6, p 846.
18. Townend, R.; Timasheff, S. N. Molecular interactions in β-lactoglobulin. III. Light scattering investigation of the stoichiometry of the association between pH 3.7 and 5.2. J. Am. Chem. Soc. 1960, 82, 3168-3174.
19. Pessen, H.; Purcell, J. M.; Farrell, H. M., Jr. Proton relaxation rates of water in dilute solutions of β-lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a self-associating globular protein. Biochim. Biophys. Acta 1985, 828, 1-12.
20. Boulet, M.; Britten, M.; Lamarche, F. Voluminosity of some food proteins in aqueous dispersions at various pH and ionic strengths. Food Hydrocolloids 1998, 12, 433-441.
21. Boulet, M.; Britten, M.; Lamarche, F. Aggregation of some food proteins in aqueous dispersions: effects of concentration, pH and ionic strength. Food Hydrocolloids 2000, 14, 135-144.
22. Hermansson, A. M. Functional properties of proteins for food-flow properties. J. Texture Stud. 1975, 5, 425-439.
23. Prentice, J. H. Measurements in the rheology of foodstuffs; Elsevier Applied Science: New York, 1984.
24. Goodwin, J. W. In Colloid Science; Everett, D. H., Ed.; The Chemical Society: London, UK, 1975; Vol. 2, p 246.