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, Antonio Fernandes de Carvalho, Federico Casanova*

*Corresponding author for this work

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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.
Original languageEnglish
Article number76
JournalColloids and Interfaces
Issue number4
Number of pages17
Publication statusPublished - 2022


  • Pea protein
  • Enzymatic hydrolysis
  • Interfacial properties
  • Ionic strength


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