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Kinetics of inactivation of quality-deteriorating enzymes and degradation of selective phytoconstituents in pink guava pulp during thermal processing
Thermal inactivation kinetics of peroxidase (POD), polyphenol oxidase (PPO), pectin methyl esterase (PME) and ascorbate oxidase (AO) were studied over the temperature range of 45–85 °C along with the degradation kinetics of ascorbic acid (AA) and lycopene in Psidium guajava pulp. POD, PPO, PME and A...
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Published in: | Journal of food science and technology 2018-08, Vol.55 (8), p.3273-3280 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Thermal inactivation kinetics of peroxidase (POD), polyphenol oxidase (PPO), pectin methyl esterase (PME) and ascorbate oxidase (AO) were studied over the temperature range of 45–85 °C along with the degradation kinetics of ascorbic acid (AA) and lycopene in
Psidium guajava
pulp. POD, PPO, PME and AO followed first-order kinetics whereas AA degradation data was explained by pseudo first-order kinetics. Lycopene degradation was suitably fitted in an exponential model, indicating continuous degradation of lycopene and higher degradation at higher temperature. Activation energy (Ea) of POD, PPO, PME, and AO was 63.79 ± 1.28, 60.36 ± 1.21, 63.22 ± 1.06 and 106.33 ± 8.51 kJ/mol, respectively. AA had Ea (95.82 ± 1.92 kJ/mol) higher than lycopene (54.92 ± 1.10 kJ/mol). PME (Z = 39.4 ± 0.1 °C) showed highest heat stability while AO (Z = 14.3 ± 1.1 °C) was least stable amongst the enzymes studied. AA (Z = 23.5 ± 0.5 °C) was weakest amongst the phytoconstituents in guava pulp and its retention was challenged during thermal processing. The thermal resistance of quality deteriorating enzyme of guava was found to be higher than that of the common spoilage organisms such as
Saccharomyces cerevisiae
and
Lactobacillus plantarum
reported for processed fruit products. Thus, this research hints towards the need for more robust thermal processing for inactivation of quality deteriorating enzymes. |
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ISSN: | 0022-1155 0975-8402 |
DOI: | 10.1007/s13197-018-3262-3 |