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 76Subject Categories
Polymer Chemistry
Food Engineering
Polymer Technologies
DOI
10.3390/colloids6040076