Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jong Wook Hong | - |
dc.date.accessioned | 2019-12-08T19:38:29Z | - |
dc.date.available | 2019-12-08T19:38:29Z | - |
dc.date.issued | 2018-08 | - |
dc.identifier.citation | CRYOBIOLOGY, v. 85, page. 33-38 | en_US |
dc.identifier.issn | 0011-2240 | - |
dc.identifier.issn | 1090-2392 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0011224018301512?via%3Dihub | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/119751 | - |
dc.description.abstract | Ice binding proteins (IBPs) have been attracting significant interest on account of their characteristic of inhibiting ice growth and recrystallization. Owing to their unique characteristics, IBPs have been studied for applications in food, pharmaceuticals, and medicine, as well as from a general scientific point of view. In this study, we have used differential scanning calorimetry (DSC) and Raman spectroscopy as tools to understand the ice binding activity of the Arctic-yeast-originating extracellular ice binding glycoprotein (LeIBP) isolated from Leucosporidium sp. AY30. From the DSC results, an increase in the specific heat capacity was confirmed for 1 mg/mL LeIBP, which suggested that additional heat flow was required for the change in temperature. In addition, the temperature corresponding to the phase change of the solution was measured, and Raman spectroscopy was carried out on the frozen and molten phases, respectively. From the results of Raman analysis, we confirmed that the helical vibrations related to the ice binding sites on LeIBP were dramatically suppressed when the LeIBP solution was frozen. Furthermore, principal component analysis (PCA) of the Raman spectra yielded the contrast factor between the freezing and melting states. Both DSC and Raman spectroscopy are widely used to study the ice binding activity and the structural changes associated with molecular vibrations in cryobiology. | en_US |
dc.description.sponsorship | This research was supported by Polar Academic Program (PD15010) of Korea Polar Research Institute (KOPRI), and KOPRI grant number (PE18210). This was also supported by Basic Science Research Program (2018R1A2B6005354) through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning of Korea. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | en_US |
dc.subject | Antifreeze protein | en_US |
dc.subject | LeIBP | en_US |
dc.subject | Raman spectroscopy | en_US |
dc.subject | Differential scanning calorimetry (DSC) | en_US |
dc.subject | Principal component analysis (PCA) | en_US |
dc.title | Properties of phase transition of ice binding protein from Arctic yeast (LeIBP) utilizing differential scanning calorimetry (DSC) and Raman spectroscopy | en_US |
dc.type | Article | en_US |
dc.relation.volume | 85 | - |
dc.identifier.doi | 10.1016/j.cryobiol.2018.10.005 | - |
dc.relation.page | 33-38 | - |
dc.relation.journal | CRYOBIOLOGY | - |
dc.contributor.googleauthor | Lee, Sanghwa | - |
dc.contributor.googleauthor | Lee, Jun Hyuck | - |
dc.contributor.googleauthor | Kim, Han-Woo | - |
dc.contributor.googleauthor | Hong, Jong Wook | - |
dc.relation.code | 2018004989 | - |
dc.sector.campus | S | - |
dc.sector.daehak | GRADUATE SCHOOL[S] | - |
dc.sector.department | DEPARTMENT OF BIONANOTECHNOLOGY | - |
dc.identifier.pid | jwh | - |
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