Characterization of Polyphenoloxidase from 2 Peach (Prunus persica L.) Varieties Grown in Argentina

ADRIANA GARRO; ESTELA GASULL

FOOD SCIENCE AND BIOTECHNOLOGY

KOREAN SOC FOOD SCIENCE TECHNOLOGY

Año: 2010 vol. 19 p. 627 - 632

1226-7708

Polyphenoloxidase was extracted from September peach (SEPPO) and Summerset peach (SUPPO) and its physicochemical characteristics were analyzed. The optimum pH was 6.5 for SEPPO and 5.5 for SUPPO. The optimum temperature was 35ºC for SEPPO and 39.4ºC forSUPPO. Activation energy (Ea) from thermal activation was 41.5 kJ/mol for SEPPO and 37.5 kJ/mol for SUPPO.Heating at 60ºC by 5 min, SUPPO was denatured whereas SEPPO retained 2.6% of activity. Activation enthalpy (ΔH#) and activation entropy (ΔS#) for SEPPO heat-inactivationwere 69.9 J/mol and −83.5 kJ/mol·K for SUPPO, ΔH# was 91.8 J/mol while ΔS# was −21.0 kJ/mol·K. Substrate specificity (Vmax/KM) was 4-methylcatechol>catechol>pyrogallol for SEPPO and 4-mehtylcatechol>pyrogallol> catechol for SUPPO. For both enzymes, the order of inhibition effectiveness using reductor agents was metabisulphite>ascorbic acid. Benzaldehyde, 4-hydroxybenzaldehyde, and DL-dopa were competitive inhibitors, and their KI valueswere 38.86, 8.43, and 2.08 mM, respectively.