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Abstract

The Degree of Hydrolysis DH and the scavenging activity of DPPH radical of Whey Protein Hydrolysates WPH were investigated. The untreated commercial whey protein concentrate was hydrolyzed with trypsin, promatex, flavorzyme, protease N and crude commercial enzymes, 2709 alkaline protease and ASI.398 neutral protease for 4 h at enzymes146 optimal conditions of pH and temperature. All the enzymes yielded WPH that possessed antioxidant activity. Flavorzyme and ASI.398 neutral protease derived hydrolysates having the highest Diphenyl-picrylhydrazyl DPPH scavenging activity while 2709 alkaline protease yielded the highest DH. Trypsin-derived WPH was readily soluble in the DPPH assay solution compared to other WPH and was therefore used to investigate the effect of other hydrolysis conditions. Temperature, pH, substrate concentration and enzyme to substrate ES ratio, were shown to influence DH and DPPH scavenging activity of the trysin-derived WPH. There was no correlation of DH and DPPH scavenging activity.