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

• Published in: Food research international 2019-05, Vol.119, p.444-454
• Main Authors: Oliete, Bonastre, Yassine, Salim A., Cases, Eliane, Saurel, Rémi
• Format: Article
• Language: English
• Subjects: Aggregate; Desiccation - methods; Food engineering; Freeze Drying - methods; Freeze-drying; Globulins - chemistry; High dynamic pressure; Hydrophobic and Hydrophilic Interactions; Life Sciences; Microfluidization; Microscopy; Particle Size; Pea globulin; Pisum sativum - chemistry; Powders; Pressure; Protein Stability; Protein Structure, Secondary; Solubility; Spray-drying; Structure; Suspension stability
• ISSN: 0963-9969; 1873-7145
• DOI: 10.1016/j.foodres.2019.02.015

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. [Display omitted] •Microfluidization at 130 MPa decreases the size of pea globulin aggregates.•Microfluidization at 130 MPa increases interactions between particles.•Drying microfluidized aggregates favored re-aggregation of pea globulins.•Spray-dried microfluidized aggregates are smaller than freeze-dried.•Drying method determines the functional properties of pea globulin aggregates.