ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
: To understand why protein granules resist heat treatment, we measured denaturation, viscosity, and solubility of heated native and disrupted granules and estimated the effect on their emulsifying ability. Granule disruption by sodium chloride caused protein solubility to drop dramatically and viscosity to rise sharply above 72° C. Solubility of native granules was unaffected by heat, and viscosity increased slightly. Electrophoresis revealed that, whatever the granules structure, low-density lipoproteins (LDL) and α-high-density lipoproteins (α-HDL) were denatured, whereas phosvitin and β-HDL were resistant to heat. Disrupted granules provided weaker emulsifying ability than native granules. The structure of native granules cannot prevent protein denaturation but can avoid aggregation of LDL and α-HDL from different granules.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.2000.tb16052.x
Permalink