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STUDY OF PROTEIN‐POLYPHENOL INTERACTION BY DIFFERENTIAL SPECTROSCOPY
Author(s) -
Woof J. B.,
Pierce J. S.
Publication year - 1968
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1968.tb03170.x
Subject(s) - rutin , chemistry , ultraviolet visible spectroscopy , aqueous solution , polyphenol , catechin , flavonoid , sodium , gelatin , spectroscopy , chromatography , organic chemistry , antioxidant , physics , quantum mechanics
Differential spectroscopy in the ultraviolet and visible regions can be used to follow the reaction between flavonoids and other polyphenols and protainaceous compounds. All the protein‐polyhydroxyphenol pairs tested gave difference spectra except those involving catechin, indicating that the reaction is relatively non‐specific. Peptides and amino acids also interact with flavonoids in aqueous solutions at ambient temperatures. Interaction was independent of pH In the range 3·0–7·5 but was affected by the ions present. Sodium chloride increased spectral intensity markedly. The intensity of spectra of rutin/gelatin systems increased up to a maximum at 55–60° C. followed by a decline. The interaction was reversible up to 60° C. but above this temperature the changes were irreversible. Dihydroquercetin combines with the α‐amylase protein chain in a stepwise manner with evidence of definite complexes of molar flavonoid: protein ratios of 2:1 6:1 and 10:1. Similar complexes are formed between rutin and gelatin. The rate of reaction is rapid but the rate curves also suggest rapid formation of an intermediate compound followed by slower changes into another more stable form.