Tyrosinase inhibitory activity of the olive oil flavor compounds.
A series of alpha,beta-unsaturated aldehydes, otherwise known as (2E)-alkenals, characterized from the olive Olea europaea L. (Oleaceae) oil flavor was found to inhibit the oxidation of L-3, 4-dihydroxyphenylalanine (L-DOPA) catalyzed by mushroom tyrosinase, and the inhibition kinetics analyzed by a Lineweaver-Burk plot found that they are noncompetitive inhibitors. The inhibition mechanism presumably comes from their ability to form a Schiff base with a primary amino group in the enzyme. In addition, the hydrophobic alkyl chain length from the hydrophilic enal group seems to relate to their affinity to the enzyme, and this results in their inhibitory potency.
Kubo
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Department of Environmental Science, Policy and Management, University of California, Berkeley 94720-3112, USA. ikubo@uclink4.berkeley.edu
Kinst-Hori
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D005421:Flavoring Agents / Q000494:pharmacology*; D007700:Kinetics; D008956:Models, Chemical; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors*; D000069463:Olive Oil; D010938:Plant Oils; D013329:Structure-Activity Relationship
D005421:Flavoring Agents; D000069463:Olive Oil; D010938:Plant Oils; D014442:Monophenol Monooxygenase