In the present study, the influence of the phospholipid phase state on the activity of the xanthophyll cycle enzyme violaxanthin de-epoxidase (VDE) was analyzed using different phosphatidylethanolamine species as model lipids. By using
31P NMR spectroscopy, differential scanning calorimetry and temperature dependent enzyme assays, VDE activity could directly be related to the lipid structures the protein is associated with. Our results show that the gel (L
β) to liquid-crystalline (L
![greek small letter alpha greek small letter alpha](http://www.sciencedirect.com/scidirimg/entities/204e.gif)
) phase transition in these single lipid component systems strongly enhances both the solubilization of the xanthophyll cycle pigment violaxanthin in the membrane and the activity of the VDE. This phase transition has a significantly stronger impact on VDE activity than the transition from the L
![greek small letter alpha greek small letter alpha](http://www.sciencedirect.com/scidirimg/entities/204e.gif)
to the inverted hexagonal (H
II) phase. Especially at higher temperatures we found increased VDE reaction rates in the presence of the L
![greek small letter alpha greek small letter alpha](http://www.sciencedirect.com/scidirimg/entities/204e.gif)
phase compared to those in the presence of H
II phase forming lipids. Our data furthermore imply that the H
II phase is better suited to maintain high VDE activities at lower temperatures.