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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Main Authors: Naoto Nishi, Takuya Miyamoto, Tomonori Waku, Naoki Tanaka, Yoshimichi Hagiwara
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2016-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4859470?pdf=render
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spelling 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
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