Plant protein-based emulsifiers: Mechanisms, techniques for emulsification enhancement and applications

Nisin is used as a natural food preservative because of its broad-spectrum antimicrobial activity against Gram-positive bacteria. However, free nisin is susceptible to various factors that reduce its antimicrobial activity. Milk protein, a protein derived from milk, has self-assembly properties and is a good carrier of bioactive substances. In this study, lactoferrin–nisin nanoparticles (L-N), bovine serum albumin–nisin nanoparticles (B-N), and casein–nisin nanoparticles (C-N) were successfully prepared by a self-assembly technique, and then their properties were investigated. The studies revealed that lactoferrin (LF) and nisin formed L-N mainly through hydrophobic interactions and hydrogen bonding, and L-N had the best performance. The small particle size (29.83 ± 2.42 nm), dense reticular structure, and good thermal stability, storage stability, and emulsification of L-N laid a certain foundation for its application in food. Further bacteriostatic studies showed that L-N enhanced the bacteriostatic activity of nisin, with prominent inhibitory properties against Listeria monocytogenes, Staphylococcus aureus, and Bacillus cereus, which mainly disrupted the cell membrane of the bacteria. The above results broaden our understanding of milk protein–nisin nanoparticles, while the excellent antibacterial activity of L-N makes it promising for application as a novel food preservative, which will help to improve the bioavailability of nisin in food systems.

Section: Resultsmentioning

confidence: 99%

The Effect of Nanoscale Modification of Nisin by Different Milk-Derived Proteins on Its Physicochemical Properties and Antibacterial Activity

Wang,

Liu,

Huang

et al. 2024

“…The ability of proteins to create and stabilize emulsions are essential for many food products, including beverages and condiments. This is due to the fact that most proteins have surface-active properties and can act as surfactants [43]. As shown in Figure 6B, it can be seen that the emulsifying capacity decreased after ball milling and ultrasound treatment.…”

Section: Emulsifying Propertiesmentioning

confidence: 90%

Effect of Physical Modifications on Physicochemical and Functional Properties of Walnut Protein

Li,

Liu,

Hei

et al. 2023

Self Cite

Walnut protein is a high-quality vegetable protein with promising applications in the food industry; however, its potential is hindered by low solubility and associated properties. We utilized various physical modification techniques (cold plasma; ball milling; superfine grinding; ultrasound; wet ball milling; and high-pressure microjet) to enhance walnut proteins’ physicochemical and functional properties. The changes in particle size, microstructure, surface hydrophobicity, fluorescence, solubility, foaming, and emulsification were investigated. Cold plasma and ultrasound treatments minimally affected particle size and morphology. Cold plasma increased the particle size D4,3 from 145.20 μm to 152.50 μm. Ultrasonication reduced the particle size D4,3 to 138.00 μm. The variation was within ±10 μm, while the particle size of walnut protein significantly decreased after the other four modification treatments. The greatest variation in particle size was in the superfine grinding, with the D4,3 being reduced to 23.80 μm. Ultrasound treatment converted the β-sheet into an α-helix, while the other methods transformed the α-helix into a β-sheet. The dispersion stability notably improved after wet ball milling and high-pressure microjet treatments, which was accompanied by a significant increase in solubility from 6.9% (control) to 13.6% (wet ball milling) and 31.7% (high-pressure microjet). The foaming and emulsification properties were also enhanced through these modifications (foaming improved from 47% to 55.33% and emulsification improved from 4.32 m2/g to 8.27 m2/g). High-pressure microjet treatment proved most effective at improving solubility in the functional properties of walnut protein. These findings are expected to help broaden the potential utilization of walnut protein in the food industry, including in beverages and emulsions.

“…ARS has a high protein content, exceeding 10%. Proteins are widely known as emulsifying and foaming agents [36], so their presence in this extract could have synergistic effects with saponins. The ash content of the three samples tested is less than 1%, so its impact on subsequent tests will be very limited.…”

Section: Characterization Of the Different Saponin Extractsmentioning

confidence: 99%

Applications of Saponin Extract from Asparagus Roots as Functional Ingredient

Hamdi,

Viera-Alcaide,

Jiménez-Araujo

et al. 2024

When replanting an asparagus field, the roots of the previous crop are crushed and incorporated into the soil, creating problems of autotoxicity and fungal infections. Asparagus roots can be considered as a valuable byproduct, since they are very rich in saponins (3–6%), compounds currently considered as bio-emulsifiers. The objective is to evaluate the emulsifying and foaming capacity of a saponin extract from asparagus roots (ARS) and compare it with other commercial extracts. ARS was obtained using a process patented by our research group. The results have shown that ARS has activity similar to Quillaja extract. Its critical micellar concentration falls between that of Quillaja and Tribulus extracts (0.064, 0.043, and 0.094 g/100 mL, respectively). Both emulsifying and foaming activities are affected by pH, salt, and sucrose to a similar extent as the other extracts. Additionally, it has demonstrated an inhibitory effect on pancreatic lipase, which is even better than the other two studied extracts, as indicated by its IC50 value (0.7887, 1.6366, and 2.0107 mg/mL for asparagus, Quillaja, and Tribulus, respectively). These results suggest that ARS could serve as a natural emulsifying/foaming agent for healthier and safer food products and as a potential aid in treatments for obesity and hyperlipidemia.