Role of Tyrosine Residues in Interactions between Casein Components |
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Authors: | Masaaki Yoshikawa Etsuro Sugimoto Hideo Chiba |
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Affiliation: | Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto |
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Abstract: | It was indicated from ultraviolet difference spectra and ultracentrifugal experiments that associations occurred between two casein components (αs- and κ-caseins, β- and κ-caseins and αs- and β-caseins) at lower CaCl2 concentrations (2~3 mm) and that aromatic amino acid residues participated in the associations. Chemical modification studies with 2-hydroxy-5-nitrobenzylbromide indicated that tryptophane residues of each casein component were not essential for these associations. It was also demonstrated by nitration of tyrosine residues with tetranitromethane that tyrosine residues of κ-casein were essential for αs·κ-association and for β·κ-association and that tyrosine residues of αs-casein were important to αs·β-association.Interactions between casein components were also studied at higher CaCl2 concentration (10 mm) which is enough for micelle formation. It was found that tyrosine residues of κ- casein played an important role for the stabilization of αs- and β-caseins. Properties of the nitrated-β-casein were almost the same as that of the native β-casein except the absorption spectrum. αs·β-Interaction in the presence of 10 mm CaCl2 was investigated by use of the nitrated-β-casein instead of the native β-casein. It was proved that αs-casein was stabilized by the nitrated-β-casein and that precipitation of the nitrated-β-casein increased in the presence of αs-casein.The mechanism of interactions between casein components at higher CaCl2 concentration (10 mm) are discussed in connection with the associations at lower CaCl2 concentrations (2~3 mm). |
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Keywords: | antioxidant liposome model membrane polyphenol ubiquinone |
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