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The protein particles in soymilk were fractionated in size by differential centrifugation.Particles of more than 100nmin diameter (LSP) constituted 40%of the total protein in raw soymilk, 70% of the protein components being IIS globulin.LSPwas not formed in the presence of2-mercaptoethanol and sodium ascorbate.LSP was decreased by heating, and particles of 100-40 nmin diameter (MSP) were increased.The formation of MSPwasnot due to any degradation of LSPbut to the combination of supernatant proteins of less than 40nm in diameter with each other.MSP formed by heating contained the ft subunit of 7S and the basic subunit of USas main components.The particles of more than 40nm in diameter (LSP+MSP)constituted 50%of the total protein in both raw soymilk and soymilk.
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Ono et al. (1991) studied this question.
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