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Acetylation of faba bean legumin: conformational changes and aggregation
Author(s) -
Schwenke Klaus Dieter,
Knopfe Constanze,
Seifert Arndt,
Görnitz Eckhard,
Zirwer Dietrich
Publication year - 2000
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/1097-0010(20010101)81:1<126::aid-jsfa788>3.0.co;2-y
Subject(s) - legumin , chemistry , circular dichroism , polylysine , protein secondary structure , acetylation , vicilin , vicia faba , ionic strength , protein tertiary structure , biochemistry , storage protein , organic chemistry , biology , botany , aqueous solution , gene
The effect of progressive acetylation upon the conformation of the 11S globulin legumin from faba bean has been studied using chemical analysis, UV, fluorescence and CD spectroscopy, viscometry and analytical ultracentrifugation. The modification did not induce complete dissociation of the oligomeric protein. Only 30% of the protein was found to be a dissociated 3S subunit after excessive acetylation, whereas 70% was a dimeric legumin aggregate with a molecular mass of about 700 kDa. The aggregation of the highly modified legumin in high‐ionic‐strength buffer solution leads to soluble higher legumin oligomers. The acetylation resulted in a moderate molecular expansion of legumin due to a changed tertiary structure, whereas the far‐UV circular dichroism spectra did not provide definitive evidence of a decrease in domain‐stabilizing β‐sheet conformations in their secondary structure. © 2000 Society of Chemical Industry