ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
A precipitate that formed in egg white at low ionic strength affected the transparency of heat-induced gels prepared at pH 2-4 and low ionic strength. The precipitate solubilized with SDS solution containing 2-mercaptoethanol and urea included major proteins of the egg white, as shown by SDS-polyacrylamide gel electrophoresis. The bands of ovalbumin, conalbumin and other protein were smaller when the precipitate was washed with water, but lysozyme and ovomacroglobulin probably remained in the precipitate fraction. It seemed that ovalbumin, conalbumin, and other proteins co-precipitated with these two kinds of proteins. Lysozyme added to the supernatant of egg white after dialysis, did not appear to produce turbidity upon heating at pH 2.5, but whole egg white was converted to a turbid gel upon being heated at this pH.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1988.tb10236.x
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