1. Drying method determines the structure and the solubility of microfluidized pea globulin aggregates.
- Author
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Oliete B, Yassine SA, Cases E, and Saurel R
- Subjects
- Hydrophobic and Hydrophilic Interactions, Microscopy, Particle Size, Powders, Pressure, Protein Stability, Protein Structure, Secondary, Solubility, Desiccation methods, Freeze Drying methods, Globulins chemistry, Pisum sativum chemistry
- Abstract
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., (Copyright © 2019. Published by Elsevier Ltd.)
- Published
- 2019
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