Resistance of adsorbed nisin to exchange with bovine serum albumin, α-lactalbumin, β-lactoglobulin, and β-casein at silanized silica surfaces Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/0r967808b

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  • Nisin is an antibacterial peptide, which when adsorbed on a surface can inhibit bacterial adhesion and viability. The ability of noncovalently immobilized nisin to withstand exchange by the milk proteins bovine serum albumin, β-lactoglobulin, α-lactalbumin, and β-casein on surfaces that had been silanized with dichlorodiethylsilane to exhibit high and low hydrophobicities was examined using in situ ellipsometry. Kinetic behavior was recorded for nisin adsorption for 1h and 8h, followed in each case by rinsing in protein-free buffer solution, and sequential contact with a single milk protein for 4h. Concerning nisin adsorption to each surface, a higher adsorbed mass was consistently recorded on the hydrophilic relative to the hydrophobic surface, independent of adsorption time. While desorption was greater from the hydrophilic surface in the 1h test, the amount desorbed was quite similar on each surface in the 8h tests. The sequential data were consistent with the assumptions that nisin organization at the interface involved adsorption in at least two different states, possibly existing in more than one layer, and that in the absence of exchange, upon addition of the second protein adsorbed mass would increase by an amount equivalent to its experimentally observed monolayer coverage. The Mass of nisin exchanged was generally higher on the hydrophobic compared to the hydrophilic surface presumably because of the presence of a more diffuse outer layer in the former case. β-casein was the most effective eluting agent among the proteins studied, while α-lactalbumin was the least effective, apparently adsorbing onto the nisin layers with little exchange. Both bovine serum albumin and β-lactoglobulin were moderately effective in exchanging with adsorbed nisin, with the amount of nisin removed by bovine serum albumin being more substantial, possibly due to its greater flexibility.
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