Inactivation and structural changes of polyphenol oxidase in quince (Cydonia oblonga Miller) juice subjected to ultrasonic treatment.
Catechol Oxidase
/ antagonists & inhibitors
Chemical Phenomena
Circular Dichroism
Color
Food Handling
Fruit
/ chemistry
Fruit and Vegetable Juices
/ analysis
Hot Temperature
Hydrogen-Ion Concentration
Maillard Reaction
Particle Size
Plant Proteins
/ metabolism
Protein Structure, Secondary
Rosaceae
/ chemistry
Ultrasonics
Vegetables
/ chemistry
activity and structure relation
aggregation
blue shift
inactivation mechanism
polyphenol oxidase (PPO)
ultrasonic processing
Journal
Journal of the science of food and agriculture
ISSN: 1097-0010
Titre abrégé: J Sci Food Agric
Pays: England
ID NLM: 0376334
Informations de publication
Date de publication:
30 Mar 2020
30 Mar 2020
Historique:
received:
10
06
2019
revised:
17
09
2019
accepted:
26
12
2019
pubmed:
27
12
2019
medline:
11
11
2020
entrez:
27
12
2019
Statut:
ppublish
Résumé
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. 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. 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.
Sections du résumé
BACKGROUND
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
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
CONCLUSIONS
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.
Substances chimiques
Plant Proteins
0
Catechol Oxidase
EC 1.10.3.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2065-2073Subventions
Organisme : Research and Demonstration on Key Technologies of New Citrus Juice Processing
ID : 2017 yfd0400701
Informations de copyright
© 2019 Society of Chemical Industry.
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