カゼインミセル成分におよぼす温度と尿素の影響

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The influences of temperature and urea on casein micelle components were studied by the methods of ultracentrifuge, gel-filtration and gellectrophoresis.Amount of casein, particularly β-casein in supernatants prepared by centrifuge(80min. at 22000g) increased at 4°C or decreased at 25°C within 1 to 2h. extremely and then the equilibrium between micellar and supernatant casein was established after 4h. at 4°C or after 2 to 3h. at 25°C.The temperature-dependent dissociation and association of β-casein in micelle suspensions were assumed to occur mostly between 12 and 20°C by reducing or raising temperature judging from the amount of supernatant β-casein observed as stored for 4h. at 4, 8, 12, 20, 25 and 30°C, respectively.The effects of urea resembled those of reducing temperature and the amount of supernatant casein increased distinctly in the presence of 1M urea at 25°C. Polymers(α-β-κ-casein complex containing more β-casein) of molecular weight approximately 50000 to 100000 were released from micelle on gel-filtration of Sephadex G-200 in the presence of 1.5M urea.From these results it was assumed that most of β-casein within micelle was accessible to solvents and incorporated into micelle by hydrophobic bonding and had an important role in forming micelle.
社団法人日本畜産学会の論文