Characterization of polyphenol oxidase from the Manzanilla cultivar (Olea europaea pomiformis) and prevention of browning reactions in bruised olive fruits.
The crude extract of the polyphenol oxidase (PPO) enzyme from the Manzanilla cultivar (Olea europaea pomiformis) was obtained, and its properties were characterized. The browning reaction followed a zero-order kinetic model. Its maximum activity was at pH 6.0. This activity was completely inhibited at a pH below 3.0 regardless of temperature; however, in alkaline conditions, pH inhibition depended on temperature and was observed at values above 9.0 and 11.0 at 8 and 25 degrees C, respectively. The thermodynamic parameters of substrate oxidation depended on pH within the range in which activity was observed. The reaction occurred according to an isokinetic system because pH affected the enzymatic reaction rate but not the energy required to carry out the reaction. In the alkaline pH region, browning was due to a combination of enzymatic and nonenzymatic reactions that occurred in parallel. These results correlated well with the browning behavior observed in intentionally bruised fruits at different temperatures and in different storage solutions. The use of a low temperature ( approximately 8 degrees C) was very effective for preventing browning regardless of the cover solution used.
Segovia-Bravo
Kharla A
KA
Food Biotechnology Department, Instituto de la Grasa (CSIC), Padre Garcia Tejero 4, 41012 Sevilla, Spain.
Jarén-Galan
Manuel
M
García-García
Pedro
P
Garrido-Fernandez
Antonio
A
D004156:Catechol Oxidase / Q000378:metabolism*; D005638:Fruit / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D015416:Maillard Reaction; D031658:Olea / Q000201:enzymology*; D013816:Thermodynamics
D004156:Catechol Oxidase