Journal
FOOD CHEMISTRY
Volume 141, Issue 4, Pages 3837-3845Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2013.06.041
Keywords
Maillard reaction products; Bovine casein peptide; ACE inhibitory activity; Antioxidant activity; Antiproliferative activity
Funding
- Innovative Research Team of Higher Education of Heilongjiang Province [2010td11]
- Project for National Natural Science Foundation of China [31000801]
- Innovation Group Program of the Northeast Agriculture University of China [CXT007-4-1]
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The purpose of this study was to evaluate the biological activities and physicochemical properties of Maillard reaction products (MRPs), derived from aqueous reducing sugar (ribose, galactose and lactose) and bovine casein peptide (BCP) model systems. The fluorescence intensity of ribose-BCP MRPs reached the maximum value within 1 h, while it took 3 h for galactose-BCP MRPs. Size exclusion chromatography of all the MRPs indicated molecular rearrangements and production of new smaller molecules, as a function of the heating time. The consumption of ribose and amino groups was the highest in the ribose-BCP MRPs. BCP lost its known angiotensin-l-converting enzyme (ACE) inhibitory activity by the Maillard reaction with reducing sugars. Ribose-BCP MRPs had the lowest ACE inhibitory activity, but they showed the highest 2,2-diphenyl-1-picryl-hydrazyl (DPPH) radical scavenging activity and ferrous reducing power among all the MRPs. Galactose-BCP MRPs inhibited, slightly the growth of Caco-2 cells, while ribose-BCPand lactose-BCP MRPs had no cytotoxicity. Crown Copyright (C) 2013 Published by Elsevier Ltd. All rights reserved.
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