Drying method determines the structure and the solubility of microfluidized pea globulin aggregates

The effects of microfluidization and drying method on the characteristics and techno-functional properties of pea (Pisum sativum L.) globulin aggregates were investigated. Pea globulin aggregates were microfluidized at 130 MPa and spray-dried or freeze-dried thereafter. Microfluidization decreased a...

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Bibliographic Details
Published in:Food research international 2019-05, Vol.119, p.444-454
Main Authors: Oliete, Bonastre, Yassine, Salim A., Cases, Eliane, Saurel, Rémi
Format: Article
Language:English
Subjects:
Aggregate
Desiccation - methods
Food engineering
Freeze Drying - methods
Freeze-drying
Globulins - chemistry
High dynamic pressure
Hydrophobic and Hydrophilic Interactions
Life Sciences
Microfluidization
Microscopy
Particle Size
Pea globulin
Pisum sativum - chemistry
Powders
Pressure
Protein Stability
Protein Structure, Secondary
Solubility
Spray-drying
Structure
Suspension stability
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Summary:The effects of microfluidization and drying method on the characteristics and techno-functional properties of pea (Pisum sativum L.) globulin aggregates were investigated. Pea globulin aggregates were microfluidized at 130 MPa and spray-dried or freeze-dried thereafter. Microfluidization decreased aggregate size and surface hydrophobicity due to protein re-arrangements. Microfluidized pea globulin aggregates showed higher solubility but less suspension stability than non-microfluidized aggregates. Drying favored the re-aggregation of pea globulins with modifications in secondary structure of proteins more marked for spray-drying, decreased surface hydrophobicity and solubility, but increased suspension stability. Spray-dried aggregates were smaller than freeze-dried, with improved suspension stability. These results indicated that microfluidization and drying determine the structure of pea globulin aggregates and their associated techno-functional properties. These findings are crucial for the preparation of plant protein powders in the food industry. [Display omitted] •Microfluidization at 130 MPa decreases the size of pea globulin aggregates.•Microfluidization at 130 MPa increases interactions between particles.•Drying microfluidized aggregates favored re-aggregation of pea globulins.•Spray-dried microfluidized aggregates are smaller than freeze-dried.•Drying method determines the functional properties of pea globulin aggregates.
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2019.02.015