Diphenolases from two cherry laurel cultivars (Laurocerasus officinalis Roem. 'Globigemmis' and 'Oxygemmis') were highly active against 3-(3,4-dihydroxyphenyl)propionic acid (DHPPA) at acidic pH values with temperature optima of 50 and 40 degreesC, respectively. Although the pH-stability profiles showed that both enzymes were fully stable at pH 7.0, their stabilities decreased significantly at alkaline pH values. Thermal-stabilities of the cherry laurel diphenolases indicated that enzymes from the two cultivars share similar thermodynamic properties and heat-sensitivities as a result of heat-inactivation. In addition, ascorbate and metabisulfite, at 1 mM final concentrations, almost completely inhibited the oxidation of DHPPA by the enzymes, indicating the sensitivities of the cherry laurel diphenolases from the two cultivars towards general Polyphenol oxidases inhibitors. It can be concluded that the crude enzymes prepared from the cherry laurel fruits of the two cultivars, at an early stage of development, possess diphenolase activities sharing similar behaviours. (C) 2004 Elsevier Ltd. All rights reserved.