Angiotensin-I Converting Enzyme Inhibitory Activity of Coffee Melanoidins
2007
Rufian-Henares, J.A. | Morales, F.J.
Melanoidins formed at the last stage of the Maillard reaction have been pointed out to possess certain functional properties. Potential antihypertensive activity of food melanoidins (coffee, beer, and sweet-wine) has been evaluated according to in-vitro ACE-inhibitory activity. Precision of the assay (3.2% of coefficient of variation, n = 10) for melanoidins is similar to those reported of well-known antihypertensive peptides. Assay was applied on food melanoidins obtained from coffee (three roasting degrees), beer, and sweet-wine. All samples showed in-vitro ACE-inhibitory activity. The activity in coffee melanoidins was significantly higher at more severe heating conditions. These experiments demonstrate that food melanoidins could inhibit ACE activity. In-vitro ACE-inhibitory activity of coffee melanoidins is likely located within the melanoidin structure. But ACE-inhibitory activity is also partly due to the low-molecular-weight compound nonchemically bound to the melanoidin structure, then melanoidins can act as carrier-protecting agents. These compounds could be naturally phenolic compounds present in the green beans or intermediary Maillard reaction products with antihypertensive activity.
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