Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength

Krystalia Sarigiannidou; Davide Odelli; Flemming Jessen; Mohammad Amin Mohammadifar; Fatemeh Ajalloueian; Mar Vall-Llosera Juanola; Antonio Fernandes de Carvalho; Federico Casanova

doi:10.3390/colloids6040076

Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength
Artikel i vetenskaplig tidskrift, 2022

The effect of a tryptic hydrolysis as well as the effect of ionic strength (0–0.4 M NaCl) was investigated on the oil/water interfacial properties of soluble pea protein hydrolysate (SPPH) at neutral pH and room temperature (20 ± 0.01 °C). SEC-MALS and SDS-Page analysis showed that tryptic hydrolysis created a lower molecular weight polypeptide mixture, whereas FTIR analysis and DSC thermograms demonstrated a more disordered and flexible structure. The bulk properties of SPPH were studied in terms of hydrodynamic diameter and turbidity, where higher particle size (+ ~13 nm) and turbidity were observed at 0.4 M NaCl. Regarding the interfacial properties, the surface activity of SPPH improved by increasing ionic strength, with maximum interfacial pressure (14.28 mN/m) at 0.4 M NaCl. Nevertheless, the addition of NaCl negatively affected the elasticity and strength of the interfacial film, where the sample without salt exhibited the highest dilatational and shear storage modulus in all the frequencies considered.

enzymatic hydrolysis

ionic strength

interfacial properties

pea protein