Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength
Journal article, 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

Author

Krystalia Sarigiannidou

Technical University of Denmark (DTU)

Davide Odelli

Technical University of Denmark (DTU)

Federal University of Viçosa

Flemming Jessen

Technical University of Denmark (DTU)

Mohammad Amin Mohammadifar

Technical University of Denmark (DTU)

Fatemeh Ajalloueian

Technical University of Denmark (DTU)

Mar Vall-Llosera Juanola

Technical University of Denmark (DTU)

Chalmers, Biology and Biological Engineering, Food and Nutrition Science

Antonio Fernandes de Carvalho

Federal University of Viçosa

Federico Casanova

Technical University of Denmark (DTU)

Colloids and Interfaces

25045377 (eISSN)

Vol. 6 4 76

Subject Categories

Polymer Chemistry

Food Engineering

Polymer Technologies

DOI

10.3390/colloids6040076

More information

Latest update

1/9/2023 1