Food and Bioprocess Technology

, Volume 11, Issue 5, pp 1039–1049 | Cite as

The Inactivation Kinetics of Soluble and Membrane-Bound Polyphenol Oxidase in Pear during Thermal and High-Pressure Processing

Original Paper
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Abstract

Polyphenol oxidase (PPO) from pear was characterized with catechol as substrate. The Michaelis constant of soluble and membrane-bound PPO were 15.6 and 23.8 mM, respectively, and their optimum pH for activity were 6.0 and 6.5, respectively. The inactivation kinetics of soluble and membrane-bound PPO during thermal (45–75 °C) and high-pressure thermal processing (600 MPa, 40–80 °C) were studied. The inactivation kinetics of pear PPO were described by a first-order model at all processing conditions. Compared to soluble PPO, membrane-bound PPO was more sensitive to thermal and high-pressure inactivation. Both soluble and membrane-bound PPO displayed higher sensitivity towards thermal inactivation at pH 3.5 (pH of pear puree made from pears dipped in citric acid prior to blending) compared to pH 4.4 (pH of non-acidified pear puree). High pressure and temperature had synergistic inactivation effects on pear PPO at pH 4.4 while slight antagonistic effects were observed at pH 3.5.

Keywords

Polyphenol oxidase Pear Characterization Thermal inactivation High-pressure inactivation First-order model 

Notes

Acknowledgements

We gratefully acknowledge the support provided by Rod Smith during the high-pressure processing experiments.

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Copyright information

© Crown 2018

Authors and Affiliations

  1. 1.State Key Laboratory of Food Science and TechnologyNanchang UniversityNanchangChina
  2. 2.CSIRO Agriculture and FoodWerribeeAustralia

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