Physicochemical and Functional Properties of Membrane-Fractionated Heat-Induced Pea Protein Aggregates

Abstract

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This study was carried out to investigate the effect of heat pre-treatment of pea proteins at different pH values on the formation of functional protein aggregates. A 10% (w/v) aqueous mixture of pea protein concentrate (PPC) was adjusted to pH 3.0, 5.0, 7.0, or 9.0 followed by heating at 100°C for 30 min, cooled and centrifuged. The supernatant was sequentially passed through 30 and 50 kDa molecular weight cut-off membranes to collect the <30, 30–50, and >50 kDa fractions. The >50 kDa fractions from pH 3.0 (FT3), 5.0 (FT5), 7.0 (FT7), and 9.0 (FT9) treatments had >60% protein content in contrast to the ≤20% for the <30 and 30–50 kDa fractions. Therefore, the >50 kDa fractions were collected and then compared to the untreated PPC for some physicochemical and functional properties. Protein aggregation was confirmed as the denaturation temperature for FT3 (124.30°C), FT5 (190.66oC), FT7 (206.33oC) and FT9 (203.17oC) was significantly (p < 0.05) greater than that of PPC (74.45oC). Scanning electron microscopy showed that FT5 had a compact structure like PPC while FT3, FT7, and FT9 contained a more continuous network. In comparison to PPC, the >50 kDa fractions showed improved solubility (>60%), oil holding capacity (~100%), protein content (~7%), foam capacity (>10%), foam stability (>7%), water holding capacity (>16%) and surface hydrophobicity (~50%). Least gelation concentration of PPC (18%), FT3 (25%), FT5 (22%), FT7 (22%), and FT9 (25%) was improved to 16, 18, 20, 16, and 18%, respectively, after addition of NaCl.

Keywords

• pea protein
• heat treatment
• protein aggregates
• polypeptide composition
• pH
• surface hydrophobicity