Antimutagenicity of Heat-Denatured Ovalbumin, before and after Digestion, As Compared to Caseinate, BSA, and Soy Protein

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 st...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1998-09, Vol.46 (9), p.3713-3718
Main Authors: Vis, Eric H, Plinck, Anette F, Alink, Gerrit M, van Boekel, Martinus A. J. S
Format: Article
Language:English
Subjects:
ACIDE BILIAIRE
ACIDOS BILIARES
ADN
ALBUMINAS
ALBUMINE
ALBUMINS
BILE ACIDS
BIOASSAYS
Biological and medical sciences
BOVINE SERUM ALBUMIN
CALENTAMIENTO
CHAUFFAGE
COMPARISONS
COMPOSE ORGANOAZOTE
COMPUESTO ORGANICO DEL NITROGENO
CONTROL DE ENFERMEDADES
CONTROLE DE MALADIES
DENATURATION
DESNATURALIZACION
DIET
DIETA
DIGESTION
DISEASE CONTROL
DISEASE PREVENTION
DNA
DNA REPAIR
ENSAYO BIOLOGICO
ESCHERICHIA
GASTROINTESTINAL SIMULATORS
General pharmacology
Geïntegreerde levensmiddelentechnologie en -fysica
HEATING
HIDROLISIS
HYDROLYSE
HYDROLYSIS
INHIBICION
INHIBITION
Integrated Food Science and Food Physics
Leerstoelgroep Toxicologie
Medical sciences
MUTAGENICIDAD
MUTAGENICITE
MUTAGENICITY
N-METHYL-N-NITROSOGUANIDINE
ORGANIC NITROGEN COMPOUNDS
Pharmacognosy. Homeopathy. Health food
Pharmacology. Drug treatments
PLANT PROTEIN
PROTEINAS
PROTEINAS VEGETALES
PROTEINE
PROTEINE VEGETALE
PROTEINS
REGIME ALIMENTAIRE
SIMULACION
SIMULATION
SODIUM CASEINATE
SOJA
SOYBEANS
Sub-department of Toxicology
TEST BIOLOGIQUE
Toxicologie
Toxicology
TRIACILGLICEROL LIPASA
TRIACYLGLYCEROL LIPASE
VLAG
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Summary: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
ISSN:0021-8561
1520-5118
DOI:10.1021/jf980140g