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Cold Gelation of β‐lactoglobulin in the Presence of Iron
Author(s) -
Remondetto G.E.,
Paquin P.,
Subirade M.
Publication year - 2002
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.1365-2621.2002.tb10643.x
Subject(s) - microstructure , homogeneous , chemistry , chemical engineering , whey protein , trapping , chromatography , materials science , crystallography , thermodynamics , physics , engineering , ecology , biology
To protect and transport iron, we investigated the trapping properties of a network formed from β‐lactoglobulin. We studied the influence of different parameters—pH, iron, and protein concentrations—on gel properties (optical and mechanical properties, WHC, and microstructure). For all conditions tested, the results show the formation of a cold gel in the presence of iron. The mechanical properties reveal that the elastic behavior and the strength of rupture increase with higher protein concentrations and decrease with higher iron concentrations. The water‐holding capacity is high for low iron concentrations. The microstructure shows that, at low iron/protein ratios, a homogeneous filamentous network is obtained whereas, at high iron/protein ratios, more random aggregated particles are present.