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Relationships Between Hydrophobicity and Foaming Characteristics of Food Proteins
Author(s) -
TOWNSEND ALTHEAANN,
NAKAI SHURYO
Publication year - 1983
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.1365-2621.1983.tb10796.x
Subject(s) - viscosity , chemistry , boiling , chemical engineering , hydrophobic effect , chromatography , organic chemistry , materials science , composite material , engineering
Hydrophobocity measured fluorometrically for food proteins and pure proteins using cis‐parinaric acid as a hydrophobic probe had significant correlations to foaming capacity when the proteins in solution were unfolded by heating in boiling water in the presence of 1.5% dodecyl sulphate prior to fluorometric measurement. Hydrophobicity measured without unfolding, which had previously shown a significant correlation to emulsification, was not significantly correlated with foaming capacity. Two highly significant regression equations were generated: one included hydrophobicity and dispersibility and the other, hydrophobicity and viscosity as the independent variables. High hydrophobicity and viscosity and moderate dispersibility were associated with optimum foaming capacity. There was a significant negative relationship between foam stability and charge density. Hydrophobicity and viscosity were also important in foam stability.