Drying method determines the structure and the solubility of microfluidized pea globulin aggregates
| Autor: | Eliane Cases, Bonastre Oliete, Rémi Saurel, Salim A. Yassine |
|---|---|
| Přispěvatelé: | Procédés Alimentaires et Microbiologiques [Dijon] (PAM), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Université Bourgogne Franche-Comté [COMUE] (UBFC) |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Globulin
Pea globulin 030309 nutrition & dietetics Spray-drying Protein Structure Secondary Pisum Suspension (chemistry) 03 medical and health sciences Freeze-drying 0404 agricultural biotechnology [SDV.IDA]Life Sciences [q-bio]/Food engineering Pressure Food science Desiccation Particle Size Solubility Microfluidization Protein secondary structure 2. Zero hunger Aggregate 0303 health sciences Microscopy biology Protein Stability Chemistry Peas food and beverages Structure Globulins 04 agricultural and veterinary sciences biology.organism_classification 040401 food science Freeze Drying Plant protein Spray drying High dynamic pressure biology.protein Powders Hydrophobic and Hydrophilic Interactions Suspension stability Food Science |
| Zdroj: | Food Research International Food Research International, Elsevier, 2019, 119, pp.444-454. ⟨10.1016/j.foodres.2019.02.015⟩ Europe PubMed Central |
| ISSN: | 0963-9969 |
| DOI: | 10.1016/j.foodres.2019.02.015⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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