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Drying method determines the structure and the solubility of microfluidized pea globulin aggregates.
- Source :
-
Food research international (Ottawa, Ont.) [Food Res Int] 2019 May; Vol. 119, pp. 444-454. Date of Electronic Publication: 2019 Feb 08. - Publication Year :
- 2019
-
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.<br /> (Copyright © 2019. Published by Elsevier Ltd.)
Details
- Language :
- English
- ISSN :
- 1873-7145
- Volume :
- 119
- Database :
- MEDLINE
- Journal :
- Food research international (Ottawa, Ont.)
- Publication Type :
- Academic Journal
- Accession number :
- 30884676
- Full Text :
- https://doi.org/10.1016/j.foodres.2019.02.015