Loading…
Physicochemical characterization of changes in pea protein as the result of cold extrusion
•Cold extrusion can be used to selectively modify hydrophobic interactions in protein.•Extrudates may find use in replacing fatty or creamy textures in food products.•Physicochemical data is used to describe textural parameters and extruder responses.•Cold denaturation acts as a novel method of func...
Saved in:
Published in: | Food chemistry 2023-10, Vol.423, p.136240-136240, Article 136240 |
---|---|
Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | •Cold extrusion can be used to selectively modify hydrophobic interactions in protein.•Extrudates may find use in replacing fatty or creamy textures in food products.•Physicochemical data is used to describe textural parameters and extruder responses.•Cold denaturation acts as a novel method of functionalizing pea protein.
Pea protein is a popular plant-based protein for mimicking textures in meat and dairy analogues which are more sustainable than their animal-based counterparts. However, precise mechanisms for generating specific textures through different processing methods are still being evaluated. This work utilizes a novel low-temperature extrusion process to selectively alter the chemical structure of pea protein. Changes in secondary structure, surface hydrophobicity, electrostatic interactions, and disulfide bonding are characterized through FTIR, ANS- probes, zeta potential, and SDS-PAGE. Extrudates are further characterized using texture parameter analysis. It was found that a linear combination of physicochemical data, generated with multiple linear regression modelling, led to reasonable estimates of the specific mechanical energy and textural properties. This work offers a new method of reactive extrusion to selectively modify interactions in pea protein using low temperature extrusion, and applications may include fatty textures, since the extrudates are found to be largely stabilized through hydrophobic interactions evaluated with surface hydrophobicity measurements. |
---|---|
ISSN: | 0308-8146 1873-7072 |
DOI: | 10.1016/j.foodchem.2023.136240 |