Purification and Characterization of a Surface-active Macropeptide Produced from Succinylated αs1-Casein by Modification with Papain
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概要
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The preceding paper described that when succinylated αs1-casein, ca. 25, 000 daltons, was modified with papain in the presence of L-leucine n-dodecyl ester (Leu-OC12), an approximately 20, 000-dalton macropeptide was formed as the main product. In the present work we have investigated its chemical structure and surface function. A treatment for purification at the petroleum ether/water interface gave an electrophoretically homogeneous 20, 000-dalton macropeptide which functioned as a surfactant to emulsify corn oil as well as "-octane. Pulsed NMR and ESR studies demonstrated that the macropeptide, when used to emulsify n-octane in water, acted to restrict the mobility of those molecules involved in the emulsion. Various data from chemical analyses coupled with knowledge about the primary structure of αs1-casein showed that the 20, 000-dalton macropeptide was structured as succinyl-Arg1-....-Phe145-Leu-OC12. A discussion is included to explain the surface function of this peptide in relation to its amphiphilic structure.
- 社団法人 日本農芸化学会の論文
著者
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Watanabe Michiko
Department Of Agricultural Chemistry The University Of Tokyo
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TOIGUCHI Seiichiro
Department of Agricultural Chemistry, The University of Tokyo
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ARAI Soichi
Department of Agricultural Chemicatry, The University of Tokyo
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MAEDA Sumio
Department of Agricultural Chemistry, The University of Tokyo
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