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Self-association of β casein Micellar aggregates Temperature and concentration ddependent d The France-Egypt Year Of Science And Technology, 2010 Andrews et al. , 1979 Payens et al., 1963 Farrell et al., 2001 Thurn et al. , 1987 Kajiwara et al. , 1988 Sood et al. , 1990 Sood et al. , 1997 Leclerc et al. , 1998 Leclerc et al. , 1997
F I Trp 143 monomer λ ↑ °CC Intrinsic Fluorescence of tryptophan tryptophan (1) (1) F I micelle λ max Trp = 341 nm λ max Trp = 336 nm The France-Egypt Year Of Science And Technology, 2010 λ
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: P P P P β casein MKVLILACLV ALALAR
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 and 24: − Average IgE (ng/ml) 35 30 25 20
Page 25: Our INRA team Isabelle Bronnec Aynu

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