ABSTRACTConditions 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 condition
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