Abstract
The antimutagenicity of ovalbumin was investigated and compared to that of sodium caseinate, bovine serum albumin and soy protein. Antimutagenicity was measured against N-methyl-N‘-nitro-N-nitrosoguanidine (MNNG) in the E. coli DNA repair liquid suspension assay. Heat-denatured ovalbumin showed a strong increase in antimutagenicity compared to undenatured ovalbumin. The antimutagenicity of heat-denatured ovalbumin was superior to the antimutagenicity found for the other proteins tested. After digestion of native and heat-denatured ovalbumin using the pH-stat method, antimutagenicity remained. Antimutagenicity measurements with samples taken from a gastro-intestinal simulator showed strong comutagenic properties. This turned out to be due to comutagenicity against MNNG caused by bile acids and lipase. It was concluded that food proteins exhibit different antimutagenic properties toward MNNG and that the choice of a particular protein digestion model can influence results to a great extent. Keywords: Antimutagenicity; bovine serum albumin; cancer prevention; casein; dietary protein; E. coli; MNNG; ovalbumin; pH-stat; protein digestion; soy protein
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