Effect of the Pretreatment Combining Glycation and Pulsed Electric Fields on the Antigenicity and Structure of β-Lactoglobulin
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Abstract:
β-Lactoglobulin (β-Lg) is a nutrient-rich bovine whey protein, but it is a major allergen in milk. In this study, we investigated β-Lg, and the changes in the antigenicity of the β-Lg in β-Lg-galactose conjugates and the structural properties of reaction products as determined using indirect competitive enzyme-linked immunosorbent assay, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), circular dichroism spectroscopy, and fluorescence spectroscopy. The reaction conditions were as follows: mass ratio of β-Lg and galactose, 1:2, modification temperature, 60 ℃, reaction time, 3 h and reaction pH 7.4. The pulsed electric field (PEF) intensity was varied. The results showed that after the pretreatment with glycation and PEF, the antigenicity of β-Lg significantly reduced, and PEF pretreatment promoted the decrease in antigenicity. When the sample was treated with PEF at 25 kV/cm for 90 μs, followed by glycation, the largest drop in the antigenicity of β-Lg was achieved (about 72.9%). After pretreatment with glycation coupled with PEF, the molecular weight of β-Lg increased. The contents of α-helix and β-turns decreased while the content of β-sheet and random coil increased. The intrinsic fluorescence intensity and surface hydrophobicity decreased, and the free sulfhydryl content first increased and then decreased. In this study, we describe a novel method for producing low-allergic β-Lg.
