Microcapsules based on glycinin–sodium dodecyl sulfate complex coacervation

References

• BARTKOWIAK, A. and HUNKELER, D., 1999, Alginate—oligochitosan microcapsules. A mechanistic study relating membrane and capsule properties to reaction conditions. Chemistry of Materials, 11, 2486–2492.
   Google Scholar
• BARTKOWIAK, A. and HUNKELER, D., 2000, Alginate-oligochitosan microcapsules. II. control of mechanical resistance and permeability of the membrane. Chemistry of Materials, 12, 206–212.
   Web of Science ®Google Scholar
• BENITA, S., 1996, Microencapsulation: Methods and Industrial Applications (New York: Marcel Dekker).
   Google Scholar
• BIGI, A., COJAZZI, G., PANZAVOLTA, S., RUBINI, K. and ROVERI, N., 2001, Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking. Biomaterials, 22, 763–768.
   PubMedGoogle Scholar
• CHOBERT, J. M., BRIAND, L., GUEGUEN, J., POPINEAU, Y., LARRE, C. and HAERTLE, T., 1996, Recent advances in enzymatic modifications of food proteins for improving their functional properties. Nahrung, 40, 177–182.
   Google Scholar
• COPELAND, R. A., 1994, Methods for protein analysis: A practical guide to laboratory protocols (London: Chapman & Hall).
   Google Scholar
• DESOIZE, B., JARDILLIER, J. C., KANOUN, K., GUERIN, D. and LEVY, M. C., 1986, In-vitro cytotoxic activity of cross-linked protein microcapsules. Journal of Pharmacy and Pharmacology, 38, 8–13.
   PubMedGoogle Scholar
• DUCLAIROIR, C., NAKACHE, E., MARCHAIS, H. and ORECCHIONI, A. M., 1998, Formation of gliadin nanoparticles: Influence of the solubility parameter of the protein solvent. Colloid and Polymer Science, 276, 321–327.
   Google Scholar
• EZPELETA, I., IRACHE, J. M., STAINMESSE, S., CHABENAT, C., GUEGUEN, J., POPINEAU, Y. and ORECCHIONI, A. M., 1996, Gliadin nanoparticles for the controlled release of all-trans-retinoic acid. International Journal of Pharmaceutics, 131, 191–200.
   Google Scholar
• EZPELETA, I., IRACHE, J. M., GUEGUEN, J. and ORECCHIONI, A. M., 1997, Properties of glutaraldehyde cross-linked vicilin nano- and microparticles. Journal of Microencapsulation, 14, 557–565.
   PubMedGoogle Scholar
• GERRARD, J. A., BROWN, P. K. and FAYLE, S. E., 2003, Maillard crosslinking of food proteins II: the reactions of glutaraldehyde, formaldehyde and glyceraldehyde with wheat proteins in vitro and in situ. Food Chemistry, 80, 35–43.
   Google Scholar
• GROBOILLOT, A. F., CHAMPAGNE, C. P., DARLING, G. D., PONCELET, D. and NEUFELD, R. J., 1993, Membrane formation by interfacial cross-linking of chitosan for microencapsulation of Lactococcus lactis. Biotechnology and Bioengineering, 42, 1157–1163.
   PubMedGoogle Scholar
• GUEGUEN, J., 1999, Prospects for plant proteins in foods. Nahrung, 43, 359–360.
   Google Scholar
• HAJDU, J. and FRIEDRICH, P., 1975, Reaction of glutaraldehyde with NH2 compounds. Analytical Biochemistry, 65, 273–280.
   PubMedGoogle Scholar
• HAGUE, Z. and KITO, M., 1982, Lipophilization of soybean glycinin: covalent attachment to long chain fatty acids. Agricultural and Biological Chemistry, 46, 597–599.
   Google Scholar
• HYNDMAN, CL., GROBOILLOT, A.F., PONCELET, D., CHAMPAGNE, C.P. and NEUFELD, R.J., 1993, Microencapsulation of Lactococcus lactis within cross-linked gelatin membranes. Journal of Chemical Technology and Biotechnology, 56, 259–263.
   Google Scholar
• Ipcm, K., YOSHIZAWA, H., UEMURA, Y. and HATATE, Y., 1997, Multi-layered gelatin/acacia microcapsules by complex coacervation method. Journal of Chemical Engineering of Japan, 30, 793–798.
   Web of Science ®Google Scholar
• IRACHE, J. M., BERGOUGNOUX, L., EZPELETA, I., GUEGUEN, J. and ORECCHIONI, A. M., 1995, Optimization and in vitro stability of legumin nanoparticles obtained by a coacervation method. International Journal of Pharmaceautics, 126, 103–109.
   Google Scholar
• JAYAKRISHNAN, A. and JAMEELA, S. R., 1996, Glutaraldehyde as a fixative in bioprostheses and drug delivery matrices. Biomaterials, 17, 471–484.
   PubMed Web of Science ®Google Scholar
• KORN, A. H., FEAIRHELLER, S. H. and FILACHIONE, E. M., 1972, Glutaraldehyde: nature of the reagent. Journal of Molecular Biology, 65, 525–529.
   PubMedGoogle Scholar
• LEGRAND, J., GUEGUEN, J., BEROT, S., POPINEAU, Y. and NOURI, L., 1997, Acetylation of pea isolate in a torus microreactor. Biotechnology and Bioengineering, 53, 409-414. LEVY, M. C. and ANDRY, M. C., 1990, Microcapsules prepared through interfacial cross- linking of starch derivates. International Journal of Pharmaceutics, 62, 27–35.
   Google Scholar
• LEVY, M. C. and ANDRY, M. C., 1991, Mixed-walled microcapsules made of cross-linked proteins and polysaccharides: preparation and properties. Journal of Microencapsulation, 8, 335–347.
   PubMedGoogle Scholar
• LUNDBLAD, R. L., 1995, Techniques in Protein Modification, (Boca Raton: CRC Press).
   Google Scholar
• MAGDASSI, S., 1996, Surface Activity of Proteins: Chemical and Physicochemical Modifications (Marcel Dekker).
   Google Scholar
• MAGDASSI, S. and VINETSKY, Y., 1996, Microencapsulation of oil-in-water emulsions by proteins. In S. Benita (ed.), Microencapsulation: Methods and Industrial Applications, (New York: Marcel Dekker).
   Google Scholar
• MAGDASSI, S., VINETSKY, Y. and RELKIN, P., 1996, Formation and structural heat-stability of 13-lactoglobulin/surfactant complexes. Colloids and Surfaces ( B), 6, 353–362
   Google Scholar
• MAUGUET, M. C., HIRECH, K., BRUJES, L., CARNELLE, G. and LEGRAND, J., 1999, Microcapsules prepared from gelatin/gum arabic systems by complex coacervation. Recents Progres en Ge'nie des Proce'dis, 13, 183–190.
   Google Scholar
• MAUGUET, M. C., LEGRAND, J., BRUJES, L., CARNELLE, G., LARRE, C. and POPINEAU, Y., 2002, Gliadin matrices for microencapsulation processes by simple coacervation method. Journal of Microencapsulation, 19, 377–384.
   PubMedGoogle Scholar
• OTTO, H., TAKAMIYA, H. and VOGT, A., 1973, A two-stage method for cross-linking antibody globulin to ferritin by glutaraldehyde. Comparison between the one-stage and two-stage method. Journal of Immunological Methods, 3, 137–146.
   PubMedGoogle Scholar
• PETERS, K. and RICHARDS, F. M., 1977, Chemical cross-linking: reagents and problems in studies of membrane structure. Annual Review of Biochemistry, 46, 523–551.
   PubMedGoogle Scholar
• Q1, M., HETTIARACHCHY, N. S. and KALAPATHY, U., 1997, Solubility and emulsifying properties of soy protein isolates modified by pancreatin. Journal of Food Science, 62, 1110–1115.
   Google Scholar
• RUBINO, 0. P., KOWALSKY, R. and SWARBRICK, J., 1993, Albumin microspheres as a drug delivery system: relation among turbidity ratio, degree of cross-linking, and drug release. Pharmaceutical Research, 10, 1059–1065.
   Google Scholar
• SINGH, 0. N. and BURGESS, D. J., 1989, Characterization of albumin-alginic acid complex coacervation. Journal of Pharmacy and Pharmacology, 41, 670–672.
   Google Scholar
• SITOHY, M., POPINEAU, Y. CHOBERT, J. M. and HAERTLE, T., 1999, Mild method of simultaneous methionine grafting and phosphorylation of soybean globulins improves their functional properties. Nahrung, 43, 3–8.
   Google Scholar
• SUBIRADE, M., KELLY, I., GUEGUEN, J. and PEZOLET, M., 1998, Molecular basis of film formation from soybean protein: comparison between the conformation of glycinin in aqueous solution and in films. International Journal of Biological Macromolecules, 23, 241–249.
   PubMedGoogle Scholar
• VAN OSS, C. J., 1989, Coacervation, complex-coacervation and flocculation. Journal of Dispersion Science and Technology, 9, 561–573.
   Google Scholar
• VINETSKY, Y. and MAGDASSI, S., 1997, Formation and surface properties of microcapsules based on gelatin-sodium dodecyl sulfate interactions. Colloids and Surfaces (A), 122, 227–235.
   Google Scholar
• VIROBEN, G., BARBOT, J., MOULOUNGUI, Z. and GUEGUEN, J., 2000, Preparation and characterization of films from pea protein. Journal of Agricultural and Food Chemistry, 48, 1064–1069.
   PubMedGoogle Scholar
• WAGNER, J. R. and GUEGUEN, J., 1995, Effects of dissociation, deamidation, and reducing treatment on structural and surface active properties of soy glycinin. Journal of Agricultural and Food Chemistry, 43, 1993–2000.
   Google Scholar
• WAGNER, J. R. and GUEGUEN, J., 1999, Surface functional properties of native, acid-treated, and reduced soy glycinin.1. Foaming properties. Journal of Agricultural and Food Chemistry, 47, 2173–2180.
   PubMedGoogle Scholar
• WAGNER, J. R. and GUEGUEN, J., 1999, Surface functional properties of native, acid-treated, and reduced soy glycinin.2. Emulsifying properties. Journal of Agricultural and Food Chemistry, 47, 2181–2187.
   PubMedGoogle Scholar
• Wu, W. U., HETTIARACHCHY, N. S. and Q1, M., 1998, HYDROPHOBICITY, solubility, and emulsifying properties of soy peptides prepared by papain modification and ultrafiltration. Journal of the American Oil Chemists Society, 75, 845–850.
   Google Scholar