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Abstract
Bovine casein peptide had a strong angiotensin-I-converting enzyme inhibitory activity. The objective of this study was to evaluate the effects of the galactose concentration on angiotensin-I-converting enzyme inhibitory activity, antioxidant activity, and physicochemical properties of Maillard reaction products derived from bovine casein peptide and galactose in aqueous model system. The browning intensities of galactose-bovine casein peptide Maillard reaction products increased remarkably with the galactose concentration increased during heat treatment, while its pH and amino groups decreased significantly. The fluorescence compounds of galactose-bovine casein peptide Maillard reaction products reached the maximum when the galactose concentration was 45 g/L. Compounds with molecular weight between 2941 and 8864 Da were dominant while compounds smaller than 250 Da were also produced during the reactions, as characterized by size exclusion chromatography. Galactose-bovine casein peptide Maillard reaction products lost 14.6% of the original angiotensin-I-converting enzyme inhibitory activity of bovine casein peptide after the addition of galactose concentration ranged from 0 to 12%, but its strong antioxidant activities were obtained. A high galactose concentration could decrease angiotensin-I-converting enzyme inhibitory activity of bovine casein peptide and enhance its antioxidant activities.
Acknowledgments
The authors would like to thank Teagasc Food Research Centre at Moorepark for the analysis of the size-exclusion chromatography.
FUNDING
This study was supported by the project for the National “Twelfth Five-Year” Plan for Science and Technology Support Program of China (No. 2013BAD18B06), the Open Research Fund for Key Laboratory of Dairy Science (Northeast Agricultural University), the Ministry of Education, Harbin China (201201), and the Innovative Research Team of Higher Education of Heilongjiang Province (2010td11).
