Abstract
Enzymatically modified proteins (EMP) 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 molecules, probably as oligomers.
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