Thermal and high pressure inactivation kinetics of polyphenoloxidase (PPO) and peroxidase (POD) in pineapple
puree were developed within the domain of 0.1–600 MPa, 30-70°C and 0–20 min, in which, PPO was more resistant
compared to POD. The inactivation orders (n) for PPO and POD during thermal treatment were 1.018 and
1.028, derived from nth order kinetic model; whereas n values for PPO and POD during high pressure domain
(200–600 MPa/30–70 °C) were 0.991 and 0.995, respectively. Pressure and temperature acted in antagonistic
manner on both the enzymes within 200–300 MPa; however, they became synergistic beyond 400 MPa. An
empirical model considering the pressure dependency of activation energy and temperature dependency of
activation volume was developed which adequately described the inactivation behavior of both enzymes. At
70 ºC/20 min, high pressure like 600 MPa protected the bioactive components better in the sample than at
0.1 MPa.
Industrial relevance: Preparation of stable pineapple puree includes the requisite of inactivating the browning
enzymes like polyphenoloxidase (PPO) and peroxidase (POD), which are responsible for less market value of
the product. A detailed kinetic evolution of these enzymes is obligatory for the design and optimization
of process to be applied, as both the oxidoreductases react in different way depending on the source and experimental
domain. The stability of these enzymes has been compared between thermal and high-pressure processes.
The developed empirical model in this study will help in identifying the optimum condition targeted
towards the inactivation of browning enzymes during high-pressure processing of pineapple puree with
an extended shelf-life.
Thermal and high pressure inactivation kinetics of polyphenoloxidase (PPO) and peroxidase (POD) in pineapplepuree were developed within the domain of 0.1–600 MPa, 30-70°C and 0–20 min, in which, PPO was more resistantcompared to POD. The inactivation orders (n) for PPO and POD during thermal treatment were 1.018 and1.028, derived from nth order kinetic model; whereas n values for PPO and POD during high pressure domain(200–600 MPa/30–70 °C) were 0.991 and 0.995, respectively. Pressure and temperature acted in antagonisticmanner on both the enzymes within 200–300 MPa; however, they became synergistic beyond 400 MPa. Anempirical model considering the pressure dependency of activation energy and temperature dependency ofactivation volume was developed which adequately described the inactivation behavior of both enzymes. At70 ºC/20 min, high pressure like 600 MPa protected the bioactive components better in the sample than at0.1 MPa.Industrial relevance: Preparation of stable pineapple puree includes the requisite of inactivating the browningenzymes like polyphenoloxidase (PPO) and peroxidase (POD), which are responsible for less market value ofthe product. A detailed kinetic evolution of these enzymes is obligatory for the design and optimizationof process to be applied, as both the oxidoreductases react in different way depending on the source and experimentaldomain. The stability of these enzymes has been compared between thermal and high-pressure processes.The developed empirical model in this study will help in identifying the optimum condition targetedtowards the inactivation of browning enzymes during high-pressure processing of pineapple puree withan extended shelf-life.
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