Abstract
ABSTRACTThe 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.
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