TY - JOUR
T1 - Interfacial Properties of Pea Protein Hydrolysate
T2 - The Effect of Ionic Strength
AU - Sarigiannidou, Krystalia
AU - Odelli, Davide
AU - Jessen, Flemming
AU - Mohammadifar, Mohammad Amin
AU - Ajalloueian, Fatemeh
AU - Vall-llosera, Mar
AU - de Carvalho, Antonio Fernandes
AU - Casanova, Federico
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
KW - Pea protein
KW - Enzymatic hydrolysis
KW - Interfacial properties
KW - Ionic strength
U2 - 10.3390/colloids6040076
DO - 10.3390/colloids6040076
M3 - Journal article
SN - 2504-5377
VL - 6
JO - Colloids and Interfaces
JF - Colloids and Interfaces
IS - 4
M1 - 76
ER -