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Properties of phase transition of ice binding protein from Arctic yeast (LeIBP) utilizing differential scanning calorimetry (DSC) and Raman spectroscopy

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Title
Properties of phase transition of ice binding protein from Arctic yeast (LeIBP) utilizing differential scanning calorimetry (DSC) and Raman spectroscopy
Other Titles
DSC와 Raman spectroscopy 방법을 이용한 북극 효모유래 얼음결합단백질의 얼음결합기작 연구
Authors
Lee, Sanghwa
Hong, Jong Wook
Kim, Han-Woo
Lee, Jun Hyuck
Subject
Life Sciences & Biomedicine - Other Topics; Physiology
Keywords
Antifreeze protein; LeIBP; Raman spectroscopy; differential scanning calorimetry (DSC); principal component analysis (PCA)
Issue Date
2018-12
Citation
Sanghwa Lee, et al. 2018. "Properties of phase transition of ice binding protein from Arctic yeast (LeIBP) utilizing differential scanning calorimetry (DSC) and Raman spectroscopy". CRYOBIOLOGY, 85(1): 33-38.
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.
URI
http://repository.kopri.re.kr/handle/201206/9526
DOI
http://dx.doi.org/10.1016/j.cryobiol.2018.10.005
ISSN
0011-2240
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