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Enginering of β casein Recombinant β casein, wild type, expressed in E. coli : WT Recombinant β casein, mutated, expressed in E. coli: MU MRELEEL RELEELNVPG EIVESLSSSE ESITRINKKI EKFQSEEQQQ TEDELQDKIH PFAQTQSLVY PFPGPIPNSL PQNIPPLTQT PVVVPPFLQP EVMGVSKVKE AMAPKHKEMP FPKYPVEPFT ESQSLTLTDV ENLHLPLPLL QSWMHQPHQP LPPTVMFPPQ SVLSLSQSKV LPVPQKAVPY PQRDMPIQAF LLYQEPVLGP VRGPFPIIV Sequence containing three glutamates well conserved in Ruminants Addition of three negative charges: change of hydrophilic/hydrophobic ratio The France-Egypt Year Of Science And Technology, 2010
Same conditions as for DLS. λmmax Trp 1 mg/mL 00,4 4 mg/mL λmaxTrp 0,2mg/mL λmaxTrp max Trp λm 342 340 338 336 334 332 342 340 338 336 334 332 Native Intrinsic Fluorescence of Tryptophan Tryptophan (1) (1) (2) 10 20 30 40 50 Temperature, °C WT 10 20 30 40 50 T emperature, t °C Temperature, °C λmmaxTrp max Trp λm The France-Egypt Year Of Science And Technology, 2010 342 340 338 336 334 332 MU 10 20 30 40 50 Temperature, °C
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: F I Trp 143 monomer λ ↑ °CC Int
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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