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Heat‐Induced Gelation of Hen's Egg Yolk Low Density Lipoprotein (LDL) Dispersion
Author(s) -
NAKAMURA RYO,
FUKANO TETSUYA,
TANIGUCHI MASAMI
Publication year - 1982
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.1365-2621.1982.tb04958.x
Subject(s) - isoelectric point , chemistry , bovine serum albumin , yolk , ovalbumin , lipoprotein , chromatography , low density lipoprotein , dispersion (optics) , albumin , biochemistry , cholesterol , food science , biology , immunology , antigen , physics , optics , enzyme
The heat‐induced gelation of hen's egg yolk low density lipoprotein (LDL) dispersion (3.5%) was studied in comparison with ovalbumin (OV) and bovine serum albumin (BSA). Stable gels of both OV and BSA were formed only at the narrow pH regions, but LDL gels obtained at every pH between 4 and 9 were stable. The presence of large amounts of salts decreased the rigidity of both OV and BSA gels, especially on the acid side of the isoelectric point of the proteins, but did not affect that of LDL gels at every pH tested. The results indicated that the heat‐induced LDL gels were more stable than those of OV and BSA under various environmental conditions.