Abstract
β-lactoglobulin (β-lg) was covalently bonded with fucoidan through Maillard reaction at 60 °C for 96 h under 79% RH condition. The molecular characters of the conjugate were investigated using fourier transform infrared spectroscopy (FT-IR), atomic force microscopy (AFM), and circular dichroism (CD) spectroscopy. And, its thermal properties, surface activity, and zeta-potential were compared with intact β-lg, β-lg-fucoidan mixture, and fucoidan under different pH conditions. AFM indicated that the conjugate was nano-structured, regular spherical-shaped and generally large sized compared to β-lg-fucoidan mixture. CD spectra and FT-IR showed that tertiary structure of β-lg slightly unfolded, but little change in secondary structure occurred. This explained that glycation under Maillard condition resulted in a molten globule state of β-lg. Differential scanning calorimetry (DSC) data exhibited that fucoidan shifted the temperature of phase transition and improved thermal stability of β-lg molecule. In addition, the conjugate prominently decreased the surface tension with pH-dependency.
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This work was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) grant funded by the Ministry of Education (No. 2015R1D1A1A09061228).
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Park, HW., Kim, DY. & Shin, WS. Fucoidan improves the structural integrity and the molecular stability of β-lactoglobulin. Food Sci Biotechnol 27, 1247–1255 (2018). https://doi.org/10.1007/s10068-018-0375-4
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DOI: https://doi.org/10.1007/s10068-018-0375-4