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Molecular Forces in Thermal Association‐Dissociation and Gelation of Legumin from Broad Beans
Author(s) -
ZHENG BAIAN,
MATSUMURA YASUKI,
MORI TOMOHIKO
Publication year - 1992
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.1365-2621.1992.tb05508.x
Subject(s) - legumin , chemistry , dissociation (chemistry) , globulin , chemical engineering , chromatography , storage protein , biochemistry , organic chemistry , biology , engineering , gene , immunology
A 0.5% legumin solution when heated showed neither dissociation into constituent subunits of the legumin nor gel formation, but association of the legumin molecules to form soluble aggregates and network‐like structures occurred. Sulfhydryl content of the protein were shown to possibly be responsible for the depression of dissociation. In the 12.5% legumin solution, gelling process and gel properties were affected by reagents such as NaSCN, N‐ethylmaleimide and 2‐mercaptoethanol. Results indicated that hydrophobic interactions and disulfide bonding helped to enhance the gelling process, where contributions of those forces to the rate of soluble aggregate formation and their junctures were notable.