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Inactivation and structural changes of polyphenol oxidase in quince ( Cydonia oblonga Miller) juice subjected to ultrasonic treatment
Author(s) -
Iqbal Aamir,
Murtaza Ayesha,
Marszałek Krystian,
Iqbal M Amjed,
Chughtai Muhammad F J,
Hu Wanfeng,
Barba Francisco J,
Bi Jinfeng,
Liu Xuan,
Xu Xiaoyun
Publication year - 2020
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.10229
Subject(s) - polyphenol oxidase , chemistry , protein secondary structure , protein tertiary structure , browning , circular dichroism , ultrasonic sensor , enzyme , polyphenol , food science , ultrasound , biophysics , biochemistry , antioxidant , biology , peroxidase , physics , acoustics
BACKGROUND Polyphenol oxidase (PPO) is considered a problem in the food industry because it starts browning reactions during fruit and vegetable processing. Ultrasonic treatment is a technology used to inactivate the enzyme; however, the mechanism behind PPO inactivation is still unclear. For this reason, the inactivation, aggregation, and structural changes in PPO from quince juice subjected to ultrasonic treatments were investigated. Different intensities and times of ultrasonic treatment were used. Changes in the activity, aggregation, conformation, and structure of PPO were investigated through different structural analyses. RESULTS Compared to untreated juice, the PPO activity in treated juice was reduced to 35% at a high ultrasonic intensity of 400 W for 20 min. The structure of PPO determined from particle size distribution (PSD) analysis showed that ultrasound treatment caused initial dissociation and subsequent aggregation leading to structural modification. The spectra of circular dichroism (CD) analysis of ultrasonic treated PPO protein showed a significant loss of α ‐helix, and reorganization of secondary structure. Fluorescence analysis showed a significant increase in fluorescence intensity of PPO after ultrasound treatment with evident blue shift, revealing disruption in the tertiary structure. CONCLUSION In summary, ultrasonic treatment triggered protein aggregation, distortion of tertiary structure, and loss of α ‐helix conformation of secondary structure causing inactivation of the PPO enzyme. Hence, ultrasound processing at high intensity and duration could cause the inactivation of the PPO enzyme by inducing aggregation and structural modifications. © 2019 Society of Chemical Industry