Copyright (c) 2014 AJC
This work is licensed under a Creative Commons Attribution 4.0 International License.
Characterization of Self-Assembly Complex Micelles Prepared from Casein and Keratin
Corresponding Author(s) : Hong-Ru Wang
Asian Journal of Chemistry,
Vol. 26 No. 12 (2014): Vol 26 Issue 12
Abstract
A novel amphiphilic complex micelles were developed utilizing self-assembly of casein and keratin in aqueous medium. The casein-keratin complex micelles were prepared in the pH ranges of 5.5-9.0 and became more stable and reinforced by the cross-linking effect of the transglutamianse. The formation of casein-keratin complex micelles was confirmed by dynamic light scattering, scanning electron microscope and atomic force microscopy. Results showed that the complex micelles near sphericity and there hydrodynamic diameters are 130-230 nm depending on the different mass ratio of casein to keratin and pH range. The structures of the complex micelles are more compact at low pH and looser at high pH. The complex micelles have the most compact structure at pH 7.5 with the mass ratio of casein to keratin is 2:1.
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References
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S.G. Zhang, Nat. Biotechnol., 21, 1171 (2003); doi:10.1038/nbt874.
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M.B. Janine Biomimicry, Innovation Inspired by Nature, William Morrow Paperbacks, Quill-William Morrow, New York, edn 2 (1997).
H.E. Swaisgood, in ed.: P.F. Fox, Chemistry of the Caseins. Advanced Dairy Chemistry 1: Proteins, Elsevier, New York, pp. 63-110 (1992).
C.G. De Kruif, Int. Dairy J., 9, 183 (1999); doi:10.1016/S0958-6946(99)00058-8.
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M.C.A. Griffin, R.L.J. Lyster and J.C. Price, Eur. J. Biochem., 174, 339 (1988); doi:10.1111/j.1432-1033.1988.tb14103.x.
K. Kanazawa, Casein Nanoparticles, US Patent 20100143424, June 10 (2010).
J.A. Lucey, C. Dick, H. Singh and P.A. Munro, Milchwissenschaft, 52, 603 (1997).
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A. Madadlou, M.E. Mousavi, Z. Emam-Djomeh, D. Sheehan and M. Ehsani, Food Chem., 116, 929 (2009); doi:10.1016/j.foodchem.2009.03.048.
Y. Liu and R. Guo, Biophys. Chem., 136, 67 (2008); doi:10.1016/j.bpc.2008.03.012.
A. Chakraborty and S. Basak, Colloid. Surf. B, 63, 83 (2008); doi:10.1016/j.colsurfb.2007.11.005.
L.M. van de Melli, Textil. Int, 10, 780 (1987).
P.M. Steinert and M.I. Gullino, Biochem. Biophys. Res. Commun., 70, 221 (1976); doi:10.1016/0006-291X(76)91131-1.
H. Thomas, A. Conrads, P.H. Phan, M. van de Löcht and H. Zahn, Int. J. Biol. Macromol., 8, 258 (1986); doi:10.1016/0141-8130(86)90038-3.
F. Ikkai and S. Naito, Biomacromolecules, 3, 482 (2002); doi:10.1021/bm010160i.
X. Pan, S. Yu, P. Yao and Z. Shao, J. Colloid Interf. Sci., 316, 405 (2007); doi:10.1016/j.jcis.2007.09.007.
C. Tonin, A. Aluigi, C. Vineis, A. Varesano, A. Montarsolo and F. Ferrero, J. Therm. Anal., 89, 601 (2007); doi:10.1007/s10973-006-7557-7.
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S. Zhang, T. Holmes, C. Lockshin and A. Rich, Proc. Natl. Acad. Sci. USA, 90, 3334 (1993); doi:10.1073/pnas.90.8.3334.
J.M. Lehn, Science, 295, 2400 (2002); doi:10.1126/science.1071063.
C.A.E. Hauser and S. Zhang, Chem. Soc. Rev., 39, 2780 (2010); doi:10.1039/b921448h.
N. Arora, T. Garg and A. Bilandi, Int. Res. J. Pharm., 3, 41 (2012).
A.O. Karlsson, R. Ipsen and Y. Ardö, LWT-Food. Sci. Technol., 40, 1102 (2007); doi:10.1016/j.lwt.2006.05.012.
E.E. Kheadr, J.F. Vachon, P. Paquin and I. Fliss, Int. Dairy J., 12, 435 (2002); doi:10.1016/S0958-6946(01)00104-2.
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