Functionalising insoluble pea protein aggregates using high-pressure homogenisation: Effects on physicochemical, microstructural and functional properties

Functionalising insoluble pea protein aggregates using high-pressure homogenisation: Effects on physicochemical, microstructural and functional properties

Food Structure

10.1016/j.foostr.2022.100298

http://dx.doi.org/10.1016/j.foostr.2022.100298

Kian Siang Ong, Jie Hong Chiang, Shaun Yong Jie Sim, David Liebl, Mufeeda Madathummal, Christiani Jeyakumar Henry

Bioengineering, Food Science, Applied Microbiology and Biotechnology

15 October 2022

Ong, K. S., Chiang, J. H., Sim, S. Y. J., Liebl, D., Madathummal, M., & Henry, C. J. (2022). Functionalising insoluble pea protein aggregates using high-pressure homogenisation: Effects on physicochemical, microstructural and functional properties. Food Structure, 34, 100298. https://doi.org/10.1016/j.foostr.2022.100298

Commercial plant protein isolates contain a large fraction of non-functional proteins due to the harsh processing conditions used. Therefore, greater value can be unlocked by functionalising these “inert” plant proteins. Using commercial insoluble pea protein isolate (I-PPI) as an example, this study demonstrates the application of high-pressure homogenisation (HPH) as a physical method to improve the techno-functionality of I-PPI. The dispersions were HPH-treated at 60, 120, or 180 MPa for one, three, and five pressure cycles. HPH treatments resulted in decreased particle size (from 16.7±1.3 to 9.4±0.2 µm at 60 MPa) and increased zeta-potential. Microstructural observations revealed the formation of smaller aggregate clusters and flake-like structures after HPH treatments. The protein solubility of I-PPI (15.9±2.0%) under acidic conditions (pH 2) significantly increased at all HPH treatment levels, with the greatest increase at 120 MPa for 5 passes (27.2±2.0%). Remarkably, the non-gelling I-PPI was able to form self-standing gels (15% w/w) after HPH treatments, with the greatest gel strength observed at 180 MPa. The emulsifying and foaming stability of HPH-treated I-PPI increased from 60 to 120 MPa but decreased at 180 MPa. Overall, our results demonstrate a key paradigm in protein modification: transforming insoluble plant proteins into functional protein ingredients.

Publisher Copyright

This research / project is supported by the A*STAR BMRC - SFS-2 IAF-PP Future Foods: Alternative Proteins (H20H8a002)
Grant Reference no. : H20H8a002

https://oar.a-star.edu.sg/communities-collections/articles/18956

2213-3291

Singapore Institute of Food and Biotechnology Innovation