Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 신원선 | - |
dc.date.accessioned | 2019-12-09T18:37:23Z | - |
dc.date.available | 2019-12-09T18:37:23Z | - |
dc.date.issued | 2018-10 | - |
dc.identifier.citation | FOOD SCIENCE AND BIOTECHNOLOGY, v. 27, no. 5, page. 1247-1255 | en_US |
dc.identifier.issn | 1226-7708 | - |
dc.identifier.issn | 2092-6456 | - |
dc.identifier.uri | https://link.springer.com/article/10.1007%2Fs10068-018-0375-4 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/120357 | - |
dc.description.abstract | 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. | en_US |
dc.description.sponsorship | 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). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | KOREAN SOCIETY FOOD SCIENCE & TECHNOLOGY-KOSFOST | en_US |
dc.subject | Maillard reaction | en_US |
dc.subject | beta-lactoglobulin | en_US |
dc.subject | Fucoidan | en_US |
dc.subject | Conjugation | en_US |
dc.subject | Molten globule state | en_US |
dc.title | Fucoidan improves the structural integrity and the molecular stability of beta-lactoglobulin | en_US |
dc.type | Article | en_US |
dc.relation.no | 5 | - |
dc.relation.volume | 27 | - |
dc.identifier.doi | 10.1007/s10068-018-0375-4 | - |
dc.relation.page | 1247-1255 | - |
dc.relation.journal | FOOD SCIENCE AND BIOTECHNOLOGY | - |
dc.contributor.googleauthor | Park, Hyun-Woong | - |
dc.contributor.googleauthor | Kim, Do-Yeong | - |
dc.contributor.googleauthor | Shin, Weon-Sun | - |
dc.relation.code | 2018010979 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF HUMAN ECOLOGY[S] | - |
dc.sector.department | DEPARTMENT OF FOOD & NUTRITION | - |
dc.identifier.pid | hime | - |
dc.identifier.orcid | http://orcid.org/0000-0003-2357-582X | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.