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Article

Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength

by
Krystalia Sarigiannidou
1,†,
Davide Odelli
1,2,†,
Flemming Jessen
1,
Mohammad Amin Mohammadifar
1,
Fatemeh Ajalloueian
3,
Mar Vall-llosera
1,4,
Antonio Fernandes de Carvalho
2 and
Federico Casanova
1,*
1
Research Group for Food Production Engineering, National Food Institute, Technical University of Denmark, Søltofts Plads, 2800 Kongens Lyngby, Denmark
2
Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa (UFV), Viçosa 36570-900, Brazil
3
Center for Intelligent Drug Delivery and Sensing Using Microcontainers and Nanomechanics (IDUN), Department of Health Technology, Technical University of Denmark, 2800 Kongens Lyngby, Denmark
4
Department of Biology and Biological Engineering, Food and Nutrition Science, Chalmers University of Technology, SE-41296 Gothenburg, Sweden
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Colloids Interfaces 2022, 6(4), 76; https://doi.org/10.3390/colloids6040076
Submission received: 23 September 2022 / Revised: 28 November 2022 / Accepted: 2 December 2022 / Published: 7 December 2022
(This article belongs to the Special Issue Biocolloids and Biointerfaces)

Abstract

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.
Keywords: pea protein; enzymatic hydrolysis; interfacial properties; ionic strength pea protein; enzymatic hydrolysis; interfacial properties; ionic strength

Share and Cite

MDPI and ACS Style

Sarigiannidou, K.; Odelli, D.; Jessen, F.; Mohammadifar, M.A.; Ajalloueian, F.; Vall-llosera, M.; de Carvalho, A.F.; Casanova, F. Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength. Colloids Interfaces 2022, 6, 76. https://doi.org/10.3390/colloids6040076

AMA Style

Sarigiannidou K, Odelli D, Jessen F, Mohammadifar MA, Ajalloueian F, Vall-llosera M, de Carvalho AF, Casanova F. Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength. Colloids and Interfaces. 2022; 6(4):76. https://doi.org/10.3390/colloids6040076

Chicago/Turabian Style

Sarigiannidou, Krystalia, Davide Odelli, Flemming Jessen, Mohammad Amin Mohammadifar, Fatemeh Ajalloueian, Mar Vall-llosera, Antonio Fernandes de Carvalho, and Federico Casanova. 2022. "Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength" Colloids and Interfaces 6, no. 4: 76. https://doi.org/10.3390/colloids6040076

APA Style

Sarigiannidou, K., Odelli, D., Jessen, F., Mohammadifar, M. A., Ajalloueian, F., Vall-llosera, M., de Carvalho, A. F., & Casanova, F. (2022). Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength. Colloids and Interfaces, 6(4), 76. https://doi.org/10.3390/colloids6040076

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