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

• Published in: Food science and biotechnology pp. 1247 - 1255
• Main Authors: 박현웅, 김도영, 신원선
• Format: Journal Article
• Language: English
• Published: 한국식품과학회 01.10.2018
• Subjects: 식품과학
• ISSN: 1226-7708; 2092-6456
• DOI: 10.1007/s10068-018-0375-4

b-lactoglobulin (b-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 b-lg, b-lg-fucoidan mixture, and fucoidan under different pH conditions. AFM indicated that the conjugate was nano-structured, regular sphericalshaped and generally large sized compared to b-lg-fucoidan mixture. CD spectra and FT-IR showed that tertiary structure of b-lg slightly unfolded, but little change in secondary structure occurred. This explained that glycation under Maillard condition resulted in a molten globule state of b-lg. Differential scanning calorimetry (DSC) data exhibited that fucoidan shifted the temperature of phase transition and improved thermal stability of b-lg molecule. In addition, the conjugate prominently decreased the surface tension with pH-dependency. KCI Citation Count: 7