2017
DOI: 10.1155/2017/3072582
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Isolation and Thermal Stabilization of Bacteriocin Nisin Derived from Whey for Antimicrobial Modifications of Polymers

Abstract: This work describes novel alternative for extraction of bacteriocin nisin from a whey fermentation media and its stabilization by using polyethylene glycol as matrix with high practical applicability. This product was compared with commercially available nisin product stabilized by sodium chloride and nisin extracted and stabilized by using ammonium sulfate and polysorbate 80.The stability of samples was tested by means of long-term storage at −18, 4, 25, and 55 ∘ C up to 165 days. The nisin content in the sam… Show more

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Cited by 11 publications
(6 citation statements)
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“…Conversely, the peptide antibiotic nisin was more sensitive to temperature, proteolytic enzymes, and a basic pH. This result is consistent with previous stability studies, demonstrating that nisin was stable at −18 • C but substantially degraded at temperatures above 25 • C [33]. The antibacterial activity of nisin was also shown to be diminished when treated with proteases or a pH above 10 because of the presence of enzymatic and chemical cleavage sites in the peptide antibiotic [34,35].…”
Section: Discussionsupporting
confidence: 90%
“…Conversely, the peptide antibiotic nisin was more sensitive to temperature, proteolytic enzymes, and a basic pH. This result is consistent with previous stability studies, demonstrating that nisin was stable at −18 • C but substantially degraded at temperatures above 25 • C [33]. The antibacterial activity of nisin was also shown to be diminished when treated with proteases or a pH above 10 because of the presence of enzymatic and chemical cleavage sites in the peptide antibiotic [34,35].…”
Section: Discussionsupporting
confidence: 90%
“…Nisin has been reported as an effective antimicrobial additive to polyolefins, polyesters, and vinyl‐based polymers via surface and bulk modifications . However, the biological activity of nisin is often constrained by time limitations; when it decomposes, the antibacterial properties of the polymer system are diminished . Several works have described a possible specific interaction of proteins, including nisin, with polyethylene glycol (PEG), as a means of protecting the biofunctionality of the same against external factors such as fluctuations in pH, increased temperature, and ionic strength .…”
Section: Introductionmentioning
confidence: 99%
“…They thus need to be modified or functionalized to ensure stability in physiological solutions. The stability of nisin, a frequently used variant for biomedical applications as an antibacterial agent or food preservative, is dependent on the environmental pH [ 20 ]. For instance, solubilized nisin is active and stable in acidic pH, whereas its solubility decreases in alkaline pH, which hinders its biological activity.…”
Section: Stability Of Bacteriocinsmentioning
confidence: 99%