Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating.
The objective of this study is to enhance the inhibition of ice growth in the aqueous solution of a polypeptide, which is inspired by winter flounder antifreeze protein. We carried out measurements on unidirectional freezing of the polypeptide solution. The thickness of the solution was 0.02 mm, and...
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2016-01-01
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doaj-d56f8803c27b49738c29b67f3c32fc5f2020-11-24T21:09:55ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01115e015478210.1371/journal.pone.0154782Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating.Naoto NishiTakuya MiyamotoTomonori WakuNaoki TanakaYoshimichi HagiwaraThe objective of this study is to enhance the inhibition of ice growth in the aqueous solution of a polypeptide, which is inspired by winter flounder antifreeze protein. We carried out measurements on unidirectional freezing of the polypeptide solution. The thickness of the solution was 0.02 mm, and the concentration of polypeptide was varied from 0 to 2 mg/mL. We captured successive microscopic images of ice/solution interfaces, and measured the interface velocity from the locations of tips of the pectinate interface in the images. We also simultaneously measured the temperature by using a small thermocouple. The ice/solution interface temperature was defined by the temperature at the tips. It was found that the interface temperature was decreased with an increasing concentration of polypeptide. To try varying the activity of the polypeptide, we preheated the polypeptide solution and cooled it before carrying out the measurements. Preheating for 1-5 hours was found to cause a further decrease in the interface temperature. Furthermore, wider regions of solution and ice with inclined interfaces in the pectinate interface structure were observed, compared with the case where the solution was not preheated. Thus, the ice growth inhibition was enhanced by this preheating. To investigate the reason for this enhancement, we measured the conformation and aggregates of polypeptide in the solution. We also measured the local concentration of polypeptide. It was found that the polypeptide aggregates became larger as a result of preheating, although the polypeptide conformation was unchanged. These large aggregates caused both adsorption to the interface and the wide regions of supercooled solution in the pectinate interface structure.http://europepmc.org/articles/PMC4859470?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Naoto Nishi Takuya Miyamoto Tomonori Waku Naoki Tanaka Yoshimichi Hagiwara |
spellingShingle |
Naoto Nishi Takuya Miyamoto Tomonori Waku Naoki Tanaka Yoshimichi Hagiwara Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating. PLoS ONE |
author_facet |
Naoto Nishi Takuya Miyamoto Tomonori Waku Naoki Tanaka Yoshimichi Hagiwara |
author_sort |
Naoto Nishi |
title |
Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating. |
title_short |
Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating. |
title_full |
Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating. |
title_fullStr |
Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating. |
title_full_unstemmed |
Ice Growth Inhibition in Antifreeze Polypeptide Solution by Short-Time Solution Preheating. |
title_sort |
ice growth inhibition in antifreeze polypeptide solution by short-time solution preheating. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2016-01-01 |
description |
The objective of this study is to enhance the inhibition of ice growth in the aqueous solution of a polypeptide, which is inspired by winter flounder antifreeze protein. We carried out measurements on unidirectional freezing of the polypeptide solution. The thickness of the solution was 0.02 mm, and the concentration of polypeptide was varied from 0 to 2 mg/mL. We captured successive microscopic images of ice/solution interfaces, and measured the interface velocity from the locations of tips of the pectinate interface in the images. We also simultaneously measured the temperature by using a small thermocouple. The ice/solution interface temperature was defined by the temperature at the tips. It was found that the interface temperature was decreased with an increasing concentration of polypeptide. To try varying the activity of the polypeptide, we preheated the polypeptide solution and cooled it before carrying out the measurements. Preheating for 1-5 hours was found to cause a further decrease in the interface temperature. Furthermore, wider regions of solution and ice with inclined interfaces in the pectinate interface structure were observed, compared with the case where the solution was not preheated. Thus, the ice growth inhibition was enhanced by this preheating. To investigate the reason for this enhancement, we measured the conformation and aggregates of polypeptide in the solution. We also measured the local concentration of polypeptide. It was found that the polypeptide aggregates became larger as a result of preheating, although the polypeptide conformation was unchanged. These large aggregates caused both adsorption to the interface and the wide regions of supercooled solution in the pectinate interface structure. |
url |
http://europepmc.org/articles/PMC4859470?pdf=render |
work_keys_str_mv |
AT naotonishi icegrowthinhibitioninantifreezepolypeptidesolutionbyshorttimesolutionpreheating AT takuyamiyamoto icegrowthinhibitioninantifreezepolypeptidesolutionbyshorttimesolutionpreheating AT tomonoriwaku icegrowthinhibitioninantifreezepolypeptidesolutionbyshorttimesolutionpreheating AT naokitanaka icegrowthinhibitioninantifreezepolypeptidesolutionbyshorttimesolutionpreheating AT yoshimichihagiwara icegrowthinhibitioninantifreezepolypeptidesolutionbyshorttimesolutionpreheating |
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