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Preparation and Properties of Acid‐Modified Sunflower Protein Isolate
Author(s) -
CLAUGHTON S. M.,
PEARCE R. J.
Publication year - 1989
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.1365-2621.1989.tb03080.x
Subject(s) - isoelectric point , deamidation , chemistry , hydrolysis , chromatography , sunflower , solubility , formic acid , lysine , peptide bond , molecular mass , cleavage (geology) , peptide , amino acid , biochemistry , organic chemistry , enzyme , materials science , biology , agronomy , fracture (geology) , composite material
Sunflower protein isolate (SFPI), 1–10% w/v dispersion, was heated in HC1 (0.025–0.1M) at 90°C. Extents of deamidation and peptide bond hydrolysis were a function of both acid and protein concentration. SDS gel electrophoresis indicated that acid modification of SFPI induced cleavage of a major protein component of molecular weight about 66,000 daltons into two smaller components. Acid modification decreased the isoelectric point of the protein and resulted in a marked increase in solubility at near neutral pH values. Acid‐modified SFPI, soluble at pH 7, was successfully incorporated into a model infant formula. Acid modification also improved foam expansion and foam stability properties of SFPI.