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RESEARCH PRODUCT

Inhibitory Effect of Azamacrocyclic Ligands on Polyphenol Oxidase in Model and Food Systems

Jose Vicente Ros LisSara Muñoz-pinaÁLvaro Martínez-camarenaEnrique García-españaÁNgel ArgüellesEstefanía Delgado‐pinarAna María Andrés GrauBegoña Verdejo

subject

0106 biological sciencesPPOTECNOLOGIA DE ALIMENTOSMacrocyclic polyaminesLigands01 natural sciencesPolyphenol oxidaseQUIMICA ORGANICANon-competitive inhibitionBrowningEnzyme InhibitorsInhibitory effectIC50InhibitionPlant Proteinschemistry.chemical_classificationEnzymatic activityChemistryReal systemsLigand010401 analytical chemistryGeneral Chemistry0104 chemical sciencesFruit and Vegetable JuicesKineticsEnzymeBiochemistryFruitMalusGeneral Agricultural and Biological SciencesCatechol Oxidase010606 plant biology & botany

description

[EN] Enzymatic browning is one of the main problems faced by the food industry due to the enzyme polyphenol oxidase (PPO) provoking an undesirable color change in the presence of oxygen. Here, we report the evaluation of 10 different azamacrocyclic compounds with diverse morphologies as potential inhibitors against the activity of PPO, both in model and real systems. An initial screening of 10 ligands shows that all azamacrocyclic compounds inhibit to some extent the enzymatic browning, but the molecular structure plays a crucial role on the power of inhibition. Kinetic studies of the most active ligand (L2) reveal a S-parabolic I-parabolic noncompetitive inhibition mechanism and a remarkable inhibition at micromolar concentration (IC50 = 10 mu M). Furthermore, L2 action has been proven on apple juice to significantly reduce the enzymatic browning.

https://doi.org/10.1021/acs.jafc.0c02407