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    Fucoidan improves the structural integrity and the molecular stability of beta-lactoglobulin

    Year: 2018

    Journal: Food Sci. Biotechnol., Volume 27, OCT, page 1247–1255

    Authors: Park, Hyun-Woong; Kim, Do-Yeong; Shin, Weon-Sun

    Organizations: Basic Science Research Program through the National Research Foundation of Korea (NRF) grant - Ministry of Education [2015R1D1A1A09061228]

    Keywords: Maillard reaction; beta-lactoglobulin; Fucoidan; Conjugation; Molten globule state

    beta-lactoglobulin (beta-lg) was covalently bonded with fucoidan through Maillard reaction at 60 degrees C for 96h 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 beta-lg, beta-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 beta-lg-fucoidan mixture. CD spectra and FT-IR showed that tertiary structure of beta-lg slightly unfolded, but little change in secondary structure occurred. This explained that glycation under Maillard condition resulted in a molten globule state of beta-lg. Differential scanning calorimetry (DSC) data exhibited that fucoidan shifted the temperature of phase transition and improved thermal stability of beta-lg molecule. In addition, the conjugate prominently decreased the surface tension with pH-dependency.
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