Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength
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 hydrolysi...
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Published in | Colloids and interfaces Vol. 6; no. 4; p. 76 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Basel
MDPI AG
01.12.2022
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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ISSN: | 2504-5377 2504-5377 |
DOI: | 10.3390/colloids6040076 |