Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behavior in admixture with alginate

Soluble and natural mixed pea proteins (PP) were extracted from defatted pea seeds according to acidic precipitation (PPP) or ultrafiltration/diafiltration (PPDF) procedures. The isolates contained proteins with a low level of denaturation. Mixed pea globulins isolates presented quite similar solubility and thermal profiles, also a similar polypeptide composition. Vicilin/convicilin 7S (Vic) and legumin 11S (Leg) fractions were obtained by batch chromatography using a salt gradient for the elution. Several incompatible systems were built by mixing the pea proteins with an anionic polysaccharide (sodium alginate, SA), when biopolymers were both negatively charged. Most of mixtures exhibited a phase separation phenomenon. From phase diagrams, experimental binodal curves obtained with either mixed globulins or legumin fraction were apparently very close. However phase boundary was better-defined with the Leg fraction. No macroscopic phase separation was evidenced for mixtures with the vicilin fraction. Microstructure of the PP-SA mixtures was investigated by confocal microscopy (CLSM) according to PP composition and biopolymer initial composition. The Leg-SA and most of PPP-SA mixtures exhibited a droplet-like structure, while structure of PPDF-SA mixtures was aggregated-like. With mixed PP, an alginate entrapment within the PP-enriched phase would disturb phase separation. Also density and shape of the protein-enriched microdomains influenced kinetics of demixing. Polydispersity within the PP-SA mixtures, in terms of wide range molecular weights distribution and charge heterogeneity would explain such differences.