Fucoidan improves the structural integrity and the molecular stability of beta-lactoglobulin
DC Field | Value | Language |
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dc.contributor.author | Park, Hyun-Woong | - |
dc.contributor.author | Kim, Do-Yeong | - |
dc.contributor.author | Shin, Weon-Sun | - |
dc.date.accessioned | 2022-07-11T05:22:40Z | - |
dc.date.available | 2022-07-11T05:22:40Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2018-10 | - |
dc.identifier.issn | 1226-7708 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/149238 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | KOREAN SOCIETY FOOD SCIENCE & TECHNOLOGY-KOSFOST | - |
dc.title | Fucoidan improves the structural integrity and the molecular stability of beta-lactoglobulin | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Shin, Weon-Sun | - |
dc.identifier.doi | 10.1007/s10068-018-0375-4 | - |
dc.identifier.scopusid | 2-s2.0-85047665314 | - |
dc.identifier.wosid | 000446317700001 | - |
dc.identifier.bibliographicCitation | FOOD SCIENCE AND BIOTECHNOLOGY, v.27, no.5, pp.1247 - 1255 | - |
dc.relation.isPartOf | FOOD SCIENCE AND BIOTECHNOLOGY | - |
dc.citation.title | FOOD SCIENCE AND BIOTECHNOLOGY | - |
dc.citation.volume | 27 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 1247 | - |
dc.citation.endPage | 1255 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART002393912 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Food Science & Technology | - |
dc.relation.journalWebOfScienceCategory | Food Science & Technology | - |
dc.subject.keywordPlus | BOVINE SERUM-ALBUMIN | - |
dc.subject.keywordPlus | TRANSFORM INFRARED-SPECTROSCOPY | - |
dc.subject.keywordPlus | MAILLARD REACTION | - |
dc.subject.keywordPlus | SECONDARY STRUCTURE | - |
dc.subject.keywordPlus | FUNCTIONAL-PROPERTIES | - |
dc.subject.keywordPlus | THERMAL-DENATURATION | - |
dc.subject.keywordPlus | ASSOCIATION BEHAVIOR | - |
dc.subject.keywordPlus | CIRCULAR-DICHROISM | - |
dc.subject.keywordPlus | ALPHA-LACTALBUMIN | - |
dc.subject.keywordPlus | PROTEIN-STRUCTURE | - |
dc.subject.keywordAuthor | Maillard reaction | - |
dc.subject.keywordAuthor | β-lactoglobulin | - |
dc.subject.keywordAuthor | Fucoidan | - |
dc.subject.keywordAuthor | Conjugation | - |
dc.subject.keywordAuthor | Molten globule state | - |
dc.identifier.url | https://link.springer.com/article/10.1007/s10068-018-0375-4 | - |
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