6533b860fe1ef96bd12c3998

RESEARCH PRODUCT

Inactivation and structural changes of polyphenol oxidase in quince ( Cydonia oblonga Miller) juice subjected to ultrasonic treatment

Ayesha MurtazaFrancisco J. BarbaXuan LiuJinfeng BiXiaoyun XuKrystian MarszałekWanfeng HuAamir IqbalM Amjed IqbalMuhammad Farhan Jahangir Chughtai

subject

Circular dichroismHot TemperatureChemical PhenomenaFood Handling030309 nutrition & dieteticsColorProtein aggregationPolyphenol oxidaseProtein Structure Secondary03 medical and health sciences0404 agricultural biotechnologyVegetablesBrowningUltrasonicsParticle SizeRosaceaeProtein secondary structurePlant Proteinschemistry.chemical_classification0303 health sciencesNutrition and Dieteticsbusiness.industryChemistryCircular DichroismUltrasound04 agricultural and veterinary sciencesHydrogen-Ion Concentration040401 food scienceProtein tertiary structureMaillard ReactionFruit and Vegetable JuicesEnzymeFruitBiophysicsbusinessAgronomy and Crop ScienceCatechol OxidaseFood ScienceBiotechnology

description

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.

https://doi.org/10.1002/jsfa.10229