Fucoidan as a carrier of antimicrobial peptide: Preparation and characterization of nisin-loaded particles

Gruškienė, Rūta; Galinskaitė, Aistė; Kavleiskaja, Tatjana; Stanevičienė, Ramunė; Servienė, Elena; Sereikaitė, Jolanta

doi:10.1016/j.lwt.2023.115598

Cited by 3 publications

(2 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…under 4 °C storage conditions. The same trend was observed in the complexation of nisin with fucoidan, i.e., the zeta potential and hydrodynamic diameter of the nanoparticles did not change significantly in most cases after 4 weeks of storage at 4 °C [65]. In summary, the results showed that the storage environment at 4 °C was more suitable for the milk protein-nisin nanoparticles.…”

Section: Storage Stabilitysupporting

confidence: 74%

“…However, no obvious changes were observed in all three nanoparticle complexes under 4 • C storage conditions. The same trend was observed in the complexation of nisin with fucoidan, i.e., the zeta potential and hydrodynamic diameter of the nanoparticles did not change significantly in most cases after 4 weeks of storage at 4 • C [65].…”

Section: Storage Stabilitysupporting

confidence: 73%

See 1 more Smart Citation

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

Foods

View full text Add to dashboard Cite

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.

show abstract

Section: Storage Stabilitysupporting

confidence: 74%

Section: Storage Stabilitysupporting

confidence: 73%