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Heat inactivation of polyphenol oxidase and peroxidase as a function of water activity: A case study of mango drying

Korbel E., Servent A., Billaud C., Brat P.. 2013. Drying Technology, 31 (13-14) : p. 1675-1680.

DOI: 10.1080/07373937.2013.808659

An innovative method was developed to study the specific uncoupled effect of temperature and water activity (Aw) during mango drying. Thermal treatment of reconstituted lyophilized mango powder at targeted Aw enabled evaluation of the inactivation of polyphenol oxidase and peroxidase activity in a range 0.98-0.6 Aw and a time-temperature range of 1-4 h and 50-60_C. We established that thermal treatment of the enzymatic extract was not the same as the inactivation phenomena that occurred in the mango matrix, mainly due to differences in the pH of the buffer extract (6.4) and reconstituted food matrix (3.8). Even if the inactivation of these two enzymes was directly correlated with the temperature of the treatment, this behavior was also strongly linked to the Aw. A two-step change in the fruit was observed at high Aw (i.e., at 0.98 in fresh fruit), polyphenol oxidase (PPO) was shown to be more thermostable than peroxidase (POD), whereas when evaporation reduced the Aw to around 0.6, the opposite behavior was observed. As a consequence, enzymatic inactivation during drying should be considered as the result of the coupled effects of time-temperature and water activity.

Mots-clés : mangue; activité enzymatique; activité de l'eau; traitement thermique; séchage; oxydoréductase; polyphénol; france; brésil; oxydase; isoperoxydase

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