Foams are essential in many food applications and require surface-active ingredients such as proteins for formation and stabilization. We investigated the influence of high-pressure homogenization on foaming properties of insoluble pea protein dispersions (5% w/w) at pH 3 and 5. Unhomogenized insoluble pea protein dispersions did not foam at either pH 3 or 5, as they consisted of large insoluble pea protein aggregates with limited surface activity. At pH 3, the homogenized pea protein dispersions generated foams due to higher protein solubility and surface activity through disruption of large protein aggregates into smaller particles. The foam stability decreased with increasing homogenization pressure and number of cycles due to a reduction in continuous phase viscosity. At pH 5, the insoluble pea proteins foamed when the homogenization resulted in formation of aggregates made of smaller protein entities, which was the case for homogenization ≥ 100 MPa and three cycles. In general, the foam capacity (amount of formed foam) was higher at pH 3 due to improved protein solubility and surface activity that facilitated incorporation of air, while the foam stability (resistance against foam collapse) was better at pH 5 because of the presence of larger protein aggregates that formed thicker and more viscous films around the air bubbles benefitting retention of gas bubbles. Overall, homogenization improved the foaming properties of insoluble pea proteins at pH 3 and 5. Practical Application Insoluble pea protein dispersions formed foams at pH 3 and 5 after homogenization highlighting the potential of this processing step for the food industry. The improvement in functionality of plant-derived ingredients helps to increase their use for consumer goods, thereby supporting the transition to more sustainable food system.
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http://dx.doi.org/10.1111/1750-3841.16320 | DOI Listing |
Spectrochim Acta A Mol Biomol Spectrosc
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Department of Bioresource Engineering, McGill University, Macdonald Campus, 21111 Lakeshore Road, Ste-Anne-de-Bellevue, QC H9X 3V9, Canada.
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Department of Food Science, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Protein bar hardening negatively impacts shelf life, quality, and consumer acceptance. Although oxidation is known to negatively affect the flavor and texture of foods, the specific roles of lipid and protein oxidation in bar hardening have not been thoroughly investigated. Furthermore, most research has concentrated on dairy proteins, with a notable lack of studies addressing the hardening of plant-based protein bars.
View Article and Find Full Text PDFWorld J Microbiol Biotechnol
January 2025
Department of Zoology, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.
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View Article and Find Full Text PDFSoft Matter
January 2025
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
The impact of animal-based food production on climate change drives the development of plant-based alternatives. We demonstrate the use of colloidal thermogelation on a real nanoemulsion system to create structured gels that could be of interest for thermo-mechanical processing of next-generation plant-based food applications. We use a commercial pea protein isolate (PPI) without further purification to stabilize a 20 vol% peanut oil-in-water nanoemulsion at pH = 7 by high-pressure homogenization (HPH) and demonstrate the temperature induced gelation behavior of the nanoemulsion as a function of the HPH processing parameters.
View Article and Find Full Text PDFFood Res Int
December 2024
Department of Food Science, College of Agriculture and Veterinary Medicine, United Arab Emirates University, Al Ain, United Arab Emirates. Electronic address:
This study aimed to evaluate the effects of date pomace fibers (DF) on the physicochemical properties of plant-based ground patty analogues. Previously optimized pea and wheat protein isolates were incorporated with varying concentrations of DF, i.e.
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