A novel functional wrapping design by complexation of ε-polylysine with liposomes entrapping bioactive peptides
An innovative edible wrapping with potential use for designing functional foods with antimicrobial capacity was developed by complexation of ε-polylysine with peptide-loaded liposomes. Unmarketable long-term frozen cooked shrimp (Litopenaeus vannamei) muscle was used as a source of both bioactive peptides and complex liposomal suspension carrier, producing a sustainable value-added protein wrapping material with desirable sensory properties. A <10-kDa peptide fraction (SH) with antioxidant and angiotensin-converting enzyme inhibitory capacity was encapsulated in partially purified phosphatidylcholine (PC) liposomes (LSH) with an entrapment efficiency of 85 %. The average size and zeta potential of LSH were 164 ± 2 nm and –37.0 ± 1.7 mV, respectively. The LSH surface changed from electronegative to electropositive upon adsorption of ε-polylysine (PL) with an optimal concentration of 0.5 %. The average diameter and zeta potential of the resulting complex ε-polylysine-adsorbed liposomes containing the peptide hydrolysate (PL-LSH) were 216 ± 5 nm and +51.1 ± 1.1 mV, respectively. The ε-PL proved to be effective as liposome stabilizing and antimicrobial agent. The PL-LSH suspension was incorporated in the formulation of the protein wrapping to provide it with both bioactive and antimicrobial properties. The wrapping showed low water solubility (≈30 %) and low mechanical resistance (tensile strength = 0.23 ± 0.06 MPa; elongation at break = 0.91 ± 0.19 %) properties that allowed it to be very versatile for varied food design and was effective against Listeria monocytogenes, Escherichia coli, Staphylococcus aureus and Yersinia enterocolitica.
| Main Authors: | , , , , , |
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| Other Authors: | |
| Format: | artículo biblioteca |
| Published: |
Springer
2016
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| Subjects: | Liposome complexation, Bioactive peptides, ε-Polylysine, Antimicrobial, Shrimp, Edible film, |
| Online Access: | http://hdl.handle.net/10261/140049 http://dx.doi.org/10.13039/501100003329 |
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