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A Study of the Forces Involved in the Incorporation of L‐Methionine into Soy Protein by the One‐Step Plastein‐Like Process
Author(s) -
NOAR S. R.,
SHIPE W. F.
Publication year - 1984
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1984.tb14977.x
Subject(s) - methionine , soy protein , chemistry , covalent bond , ultrafiltration (renal) , guanidine , amino acid , casein , chromatography , biochemistry , organic chemistry
Ultrafiltration was used to study the forces involved in the incorporation of methionine into soy protein. Various solvents were used to determine the extent of noncovalent binding. When analyzed with 0.2M citric acid, 60% of the methionine was incorporated into the soy protein. However, when analyzed with 8M Guanidine HCl and 3M KSCN the incorporation was only 20 and 13%, respectively. This reduction in percent incorporation of methionine by protein denaturants indicates that it was not incorporated by covalent bonds. Incorporation is probably due to hydrophobic attraction of the side chain of methionine with apolar regions in the protein.