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Functional and Structural Properties of β‐lactoglobulin as Affected by High Pressure Treatment
Author(s) -
PITTIA PAOLA,
WILDE PETER J.,
HUSBAND FIONA A.,
CLARK DAVID C.
Publication year - 1996
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.1365-2621.1996.tb10944.x
Subject(s) - pulmonary surfactant , adsorption , surface pressure , chemical engineering , chemistry , beta lactoglobulin , aggregate (composite) , protein adsorption , modulus , materials science , whey protein , biophysics , chromatography , composite material , organic chemistry , biochemistry , physics , mechanics , engineering , biology
Pressure (300–900 MPa) so modified β‐lactoglobulin that it displayed reduced emulsifying capacity and foamability compared to native β‐lactoglobulin. However, the pressure‐treated samples showed a greater capacity for protein‐protein interactions in the adsorbed layers of interfaces as evidenced by increased surface‐dilational modulus and resistance to displacement by a surfactant in foams. The observed behavior was explained by a pressure‐induced structural change in β‐lactoglobulin. This increased its hydrophobicity and its potential for aggregate formation which probably accounts for the reduced emulsifying capacity and foamability.