Fucoidan improves the structural integrity and the molecular stability of beta-lactoglobulinopen access
- Authors
- Park, Hyun-Woong; Kim, Do-Yeong; Shin, Weon-Sun
- Issue Date
- Oct-2018
- Publisher
- KOREAN SOCIETY FOOD SCIENCE & TECHNOLOGY-KOSFOST
- Keywords
- Maillard reaction; β-lactoglobulin; Fucoidan; Conjugation; Molten globule state
- Citation
- FOOD SCIENCE AND BIOTECHNOLOGY, v.27, no.5, pp.1247 - 1255
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- FOOD SCIENCE AND BIOTECHNOLOGY
- Volume
- 27
- Number
- 5
- Start Page
- 1247
- End Page
- 1255
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/149238
- DOI
- 10.1007/s10068-018-0375-4
- ISSN
- 1226-7708
- 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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