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

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.
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https://hal-univ-bourgogne.archives-ouvertes.fr/hal-02172984
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Soumis le : vendredi 22 octobre 2021 - 07:45:20
Dernière modification le : dimanche 26 juin 2022 - 01:57:52
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Bonastre Oliete, Salim A. yassine, Eliane Cases, Rémi Saurel. Drying method determines the structure and the solubility of microfluidized pea globulin aggregates. Food Research International, Elsevier, 2019, 119, pp.444-454. ⟨10.1016/j.foodres.2019.02.015⟩. ⟨hal-02172984⟩

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