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.

Keywords: Aggregate; Freeze-drying; High dynamic pressure; Microfluidization; Microscopy; Pea globulin; Solubility; Spray-drying; Structure; Suspension stability.