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Summary ß-CN and its mutants undergo temperature-induced concentrationdependent micellisation. Polar phosphate residues and the NN-terminal terminal hydrophilic domain are important functional elements enhancing the chaperone-like activities of native β-CN. Dimerization of C208 β-CN with two distal hydrophilic domains improved considerably its chaperone-like activity in comparison with its monomeric form and with C4 β-CND. NN-terminal t i l hydrophilic h d hili domain d i plays l significant i ifi t role l as important i t t functional elements enhancing the chaperone-like activity of native β-CN Exposure of hydrophobic domains increases immuno reactivity in 208 ββ-CN CN dimer The France-Egypt Year Of Science And Technology, 2010
Our INRA team Isabelle Bronnec Aynur Akhmadova – PhD student JJean-Marc M Ch Chobert b t Sh Shady d El GGaish i h – PhD student t d t Yvan Choiset Tatyana Konnova – PhD student Michèle Dalgalarrondo Asghar Taheri Kafrani – PhD student Hanitra Rabesona Iuliya Schutskaya – PhD student Thomas Haertlé Reza Yousefi – post doctoral Collaborations Prof Dr V.I. Muronetz, Faculty of Bioengineering, Lomonosov University, Moscow, Russia Prof Dr Yu. D. Zuev, Institute of Biochemistry and Biophysics, RAS, Kazan, Russia. Prof Dr A. A. Moosavi-Movahedi, Institute of Biochemistry and Biophysics, Tehran University, IR Iran. The France-Egypt Year Of Science And Technology, 2010
Page 1 and 2: ENGINEERING OF DAIRY PROTEINS AND T
Page 3 and 4: Average composition of f cow milk i
Page 5 and 6: Caséine κ 169 aa 19037 Da 1 Chymo
Page 7 and 8: P P P P β casein MKVLILACLV ALALAR
Page 9 and 10: F I Trp 143 monomer λ ↑ °CC Int
Page 11 and 12: Same conditions as for DLS. λmmax
Page 13 and 14: SDS-PAGE of bovine β casein and mu
Page 15 and 16: SDS-PAGE of the dimerizing β casei
Page 17 and 18: Hydrophilic Hydrophilic-Hydrophilic
Page 19 and 20: Chhaperone-like activity ac (%) Cha
Page 21 and 22: Consequence of Cys incorporation on
Page 23: − Average IgE (ng/ml) 35 30 25 20

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