ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Conditions for gel formation of heated globin and inhibition of thermocoagulation of ovalbumin and bovine serum albumin by globin were investigated. Globin was highly soluble even when heated at 100°C at pH below 5. Globin also considerably inhibited thermocoagulation of ovalbumin and serum albumin near their isoelectric point. A great increase of viscosity was observed when 1% globin solution was heated at above 80°C in the narrow pH range between pH 5.2 and 5.4. Heated globin formed a transparent gel at concentration above 3% under well controlled heat conditions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1982.tb04951.x
Permalink