Chemical Properties of Enzymatically Modified Proteins Produced from Soy Protein by Covalent Attachment of Methionine
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概要
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Enzymatically modified proteins (BMP) with different methionine levels were produced from soy protein isolate using an improved plastein reaction. The products having methionine at approximate levels of 4%, 7%, and 14%, designated as EMP4, EMP7, and EMP14, respectively, were investigated to characterize their chemical properties particularly in terms of the state and location of the methionine residues. Leucine aminopeptidase treatment of the EMP products did not find any significant amount of methionine residues at the N -terminals, but carboxypeptidase A treatment liberated methionine efficiently in accordance with the methionine levels in the EMP products. Treatment with LiBH4 reduced the methionine content of EMP14 by approximately 64%. A significant amount of homoserine was produced when EMP14 was treated with BrCN. All these data indicate that the covalently attached methionine molecules are localized at or near the C-terminals of the EMP molecul
- 社団法人 日本農芸化学会の論文
著者
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Aso Hiroshi
Department Of Computer Science And Electronics Kyushu Institute Of Technology
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KIMURA Hiroko
Kagawa Nutrition University
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Watanabe Michiko
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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KIMURA Hiroko
Kagawa Nutrition Collage
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ASO Hiroshi
Department of Agricultural Chemistry, The University of Tokyo
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