Journal
FOOD RESEARCH INTERNATIONAL
Volume 119, Issue -, Pages 444-454Publisher
ELSEVIER
DOI: 10.1016/j.foodres.2019.02.015
Keywords
Pea globulin; Aggregate; Microfluidization; High dynamic pressure; Spray-drying; Freeze-drying; Microscopy; Structure; Solubility; Suspension stability
Categories
Funding
- European Funds for Regional Development (FEDER-FSE Bourgogne 2014/2020)
- French Inter-Ministerial Unique Funds (FUI)
- Region of Burgundy (France) as part of project LEGUP [32015 03 03]
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The effects of microfluidization and drying method on the characteristics and techno-functional properties of pea (Pisurn 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.
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