Yam (Dioscorea cayenensis-rotundata cv. Kponan) is a staple food in many tropical regions. A biochemical characterization study of crude polyphenol oxidase from yam (PPO) was carried out to provide useful information for food processing operations. Two polyphenol oxidases of edible yam (Dioscorea cayenensis-rotundata cv. Kponan) cultivated in Côte d'Ivoire were purified to homogeneity. The purification procedure consisted of ammonium sulphate fractionation, ion-exchange, size exclusion and hydrophobic interaction chromatography. The enzymes designated PPO1 and PPO2 had native molecular weights of approximately 113.7±0.34 and 115.65 ±1.78 kDa, respectively, and functioned as dimeric (PPO2) and monomeric (PPO1) structures. The two isoforms isolated had different optimum pHs and temperatures. The maximal activity of PPO1 occurred at 35ºC and pH 6.0. On the other hand, PPO2 had a maximum activity at 25ºC and pH 6.6. The enzymes were stable at their optimal temperatures (25ºC and 35ºC) and their pH stability was in the range of 5.6-7.0. Polyphenol oxidases (PPO1 and PPO2) remained their full activity in the presence of ion Mn 2+ , Fe 2+ , Na + and Cu 2+ but were

Peroxidase (POD) associated with the browning of fresh-cut fruits and vegetableswas extracted from purple skin eggplant(Solanum melongena L.) and characterised using reliable spectrophotometric methods. Maximal POD activity was found at 35 °C and pH 6.0 with guaiacol as the substrate. The enzyme was stable at his optimal temperature (35 °C) and hisat pH stability was in the range of 5.6 - 6.6.Peroxidase retained its full activity in the presence of ion K+, Cu2+, Na+, Pb2+ and Ba2+ but were inhibited strongly by the ion Fe2+ and Mg2+ and the reducing agents as sodium thiosulfateand ascorbic acid. Effect of heattreatment on eggplant peroxidase showed that D-values decreased with increasing temperature, indicating faster peroxidase inactivation at higher temperatures.At 60 °C, the D-values ranged from 20.42 to 54.24 min. Hence, heat treatment at 60 °C for 30 min reduced browning of eggplant fruit.These data can be used to predict prevention of browning in the purple skin eggplantby thermal inactivation and the use of chimical agents onthe enzyme.

Le brunissement enzymatique est associé à l'action des polyphénol oxydases (PPO) et des peroxydases (POD). Les produits de ces enzymes provoquent des changements indésirables de couleur et de saveur des aubergines transformées. Une dopamine oxydase responsable du brunissement enzymatique a été isolée de l’aubergine violette (Solanum melongena L.). Ainsi, l’inactivation thermique et l’analyse thermodynamique ont été étudiées sur une base cinétique afin de contrôler ce phénomène physiologique. Les études cinétiques ont montré que l’inactivation thermique de l’activité dopamine oxydase de l’aubergine violette suivait une cinétique de premier ordre aux températures comprises entre 35 – 80 °C, avec des constantes de vitesse (k) comprise entre 0,0101 ± 0,0001 et 0,0865 ± 0,0004 min-1. Les temps de réduction décimale (D) et k ont diminué et augmenté respectivement avec l’augmentation de la température, indiquant une inactivation plus rapide de la dopamine oxydase à des températures plus élevées. Les résultats suggèrent que dopamine oxydase est une enzyme relativement thermostable avec une constante de résistance (Z) de 50.25 ± 0,7 °C et une énergie d'activation (Ea) de 40.65 ± 0,6 kJmol-1. Les résultats thermodynamiques ont indiqué que les réactions d'oxydation étaient : non spontanées (ΔG > 0), légèrement endothermiques (ΔH > 0) et réversibles (ΔS < 0). Ces données cinétiques peuvent être utilisées dans la prévention du brunissement enzymatique de la pulpe d’aubergine violette par l'inactivation thermique de l'enzyme. Enzymatic browning is associated with the action of polyphenol oxidases (PPO) and peroxidases (POD). The products of these enzymes cause undesirable changes of color and flavor of processed eggplant products. A dopamine oxidase responsible for enzymatic browning was isolated from violet eggplant (Solanum melongena L.). Thus, thermal inactivation and thermodynamic analysis were studied on a kinetic basis to control this physiological phenomenon. Kinetic studies showed that thermal inactivation of dopamine oxidase activity in purple eggplant followed first-order kinetics at temperatures between 35 - 80 °C, with speed constants (k) values between 0.0101 ± 0.0001 and 0.0865± 0.0004 min-1. The decimal reduction times (D) and k values decreased and increased, respectively, with increasing temperature, indicating more rapid inactivation of dopamine oxidase at higher temperatures. The results suggest that dopamine oxidase is a relatively thermostable enzyme with a resistance constant (Z) value of 50.25 ± 0.7 °C and an activation energy (Ea) of 40.65 ± 0.6 kJmol-1. Thermodynamic results indicated that the oxidation reactions were: non-spontaneous (ΔG > 0), slightly endothermic (ΔH > 0), and reversible (ΔS < 0). These kinetic data can be used in the prevention of enzymatic browning of purple eggplant pulp by thermal inactivation of the enzyme.

No abstract

Enzymatic browning is associated with the action of polyphenol oxidases (PPO) and peroxidases (POD). The products of these enzymes cause undesirable changes of color and flavor of processed eggplant products. The present study aimed to evaluate kinetic properties and thermodynamics parameters of PPO and POD activities for controlling this undesirable process in extract from of violet eggplant. The effect of heat treatment on polyphenol oxidase and peroxidase activities in violet eggplant were studied over a range of 30 to 80 °C. T1/2-values of enzymatic activities are between 6.15 ± 0.03 and 13,27 ± 0,04 min at 80 °C, they decreased with increasing temperature, indicating a difference thermostability of each enzyme. D- and k-values decreased and increased, respectively, with increasing temperature, indicating faster of these enzymes inactivation at higher temperatures. Results suggested that polyphenol oxydase and peroxidase were relatively thermostable enzymes with a Z-value which from 50.25 and from 88.33 °C and Ea of 41.21 and of 27.78 kJmol-1. Thermodynamic parameters were also calculated. The Gibbs free energy ΔG values range from 43.24 ± 0,03 to 91.45 ± 0,01 kJ/mol. These kinetic data can be used to predict prevention of browning in the violet eggplant (Solanum melongena L.) by thermal inactivation of enzymes.