Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom

Antifreeze proteins (AFPs) from polar and cold-tolerant organisms are able to control ice growth as a result of their adsorption on the ice crystal surface. The proteins bind to selected crystallographic planes, which are characteristic for each kind of AFP. As a consequence of the adsorption, the f...

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Main Authors: Bayer-Giraldi, Maddalena, Kipfstuhl, Sepp, Weikusat, Ilka, Dieckmann, Gerhard
Format: Conference Object
Language:unknown
Published: 2014
Subjects:
Online Access:https://epic.awi.de/id/eprint/35515/
https://epic.awi.de/id/eprint/35515/1/Bayer-Giraldi_The_Physics_and_Chemistry_of_Ice.pdf
https://hdl.handle.net/10013/epic.44144
https://hdl.handle.net/10013/epic.44144.d001
id ftawi:oai:epic.awi.de:35515
record_format openpolar
spelling ftawi:oai:epic.awi.de:35515 2024-09-15T18:35:23+00:00 Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom Bayer-Giraldi, Maddalena Kipfstuhl, Sepp Weikusat, Ilka Dieckmann, Gerhard 2014 application/pdf https://epic.awi.de/id/eprint/35515/ https://epic.awi.de/id/eprint/35515/1/Bayer-Giraldi_The_Physics_and_Chemistry_of_Ice.pdf https://hdl.handle.net/10013/epic.44144 https://hdl.handle.net/10013/epic.44144.d001 unknown https://epic.awi.de/id/eprint/35515/1/Bayer-Giraldi_The_Physics_and_Chemistry_of_Ice.pdf https://hdl.handle.net/10013/epic.44144.d001 Bayer-Giraldi, M. orcid:0000-0002-7158-5478 , Kipfstuhl, S. , Weikusat, I. orcid:0000-0002-3023-6036 and Dieckmann, G. (2014) Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom , 13th International Conference on the Physics and Chemistry of Ice, Hanover, NH (USA), 16 March 2014 - 20 March 2014 . hdl:10013/epic.44144 EPIC313th International Conference on the Physics and Chemistry of Ice, Hanover, NH (USA), 2014-03-16-2014-03-20 Conference notRev 2014 ftawi 2024-06-24T04:09:53Z Antifreeze proteins (AFPs) from polar and cold-tolerant organisms are able to control ice growth as a result of their adsorption on the ice crystal surface. The proteins bind to selected crystallographic planes, which are characteristic for each kind of AFP. As a consequence of the adsorption, the freezing point of the solution is locally lowered below the melting point, following the Gibbs-Thomson equation. Within the difference between the melting and the freezing point (hysteresis gap), the macroscopic growth of the crystals is arrested. Below the freezing point, crystals grow with a burst of determined shapes. Their habit is dominated by the crystallographic planes inhibited by the proteins, due to the geometric adsorption selectivity as well as to the adsorption rate of the proteins. Most of the well-studied fish AFPs do not bind to the basal plane, therefore crystals burst as needles parallel to the c-axis. At strong supercoolings the protein adsorption rate is not fast enough to balance radial growth due to heat dissipation, and crystals develop dendrites. However, data about the shape of the crystals after the burst, and well below the freezing point, are still scarce, resulting in an incomplete understanding of the growth inhibition mechanisms by the different AFP types. Here we present ice growth experiments in the presence of AFPs from the polar diatom Fragilariopsis cylindrus, a dominant microalga in sea ice assemblages. The protein was recombinantely expressed and purified from E. coli. Ice grain habit was observed at light microscopy in a dish, from the hysteresis gap until growth into a solid sample of polycrystalline ice. Crystals grew with an expansion of the basal plane area, but a suppressed development parallel to the c-axis compared to negative controls, resulting in thin ice “sheets”. A slow three- dimensional growth was revealed by the formation of characteristic features as pits and groves. Dendritic growth was limited, presumably among others an effect of the rapid heat dissipation ... Conference Object Sea ice Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center)
institution Open Polar
collection Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center)
op_collection_id ftawi
language unknown
description Antifreeze proteins (AFPs) from polar and cold-tolerant organisms are able to control ice growth as a result of their adsorption on the ice crystal surface. The proteins bind to selected crystallographic planes, which are characteristic for each kind of AFP. As a consequence of the adsorption, the freezing point of the solution is locally lowered below the melting point, following the Gibbs-Thomson equation. Within the difference between the melting and the freezing point (hysteresis gap), the macroscopic growth of the crystals is arrested. Below the freezing point, crystals grow with a burst of determined shapes. Their habit is dominated by the crystallographic planes inhibited by the proteins, due to the geometric adsorption selectivity as well as to the adsorption rate of the proteins. Most of the well-studied fish AFPs do not bind to the basal plane, therefore crystals burst as needles parallel to the c-axis. At strong supercoolings the protein adsorption rate is not fast enough to balance radial growth due to heat dissipation, and crystals develop dendrites. However, data about the shape of the crystals after the burst, and well below the freezing point, are still scarce, resulting in an incomplete understanding of the growth inhibition mechanisms by the different AFP types. Here we present ice growth experiments in the presence of AFPs from the polar diatom Fragilariopsis cylindrus, a dominant microalga in sea ice assemblages. The protein was recombinantely expressed and purified from E. coli. Ice grain habit was observed at light microscopy in a dish, from the hysteresis gap until growth into a solid sample of polycrystalline ice. Crystals grew with an expansion of the basal plane area, but a suppressed development parallel to the c-axis compared to negative controls, resulting in thin ice “sheets”. A slow three- dimensional growth was revealed by the formation of characteristic features as pits and groves. Dendritic growth was limited, presumably among others an effect of the rapid heat dissipation ...
format Conference Object
author Bayer-Giraldi, Maddalena
Kipfstuhl, Sepp
Weikusat, Ilka
Dieckmann, Gerhard
spellingShingle Bayer-Giraldi, Maddalena
Kipfstuhl, Sepp
Weikusat, Ilka
Dieckmann, Gerhard
Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
author_facet Bayer-Giraldi, Maddalena
Kipfstuhl, Sepp
Weikusat, Ilka
Dieckmann, Gerhard
author_sort Bayer-Giraldi, Maddalena
title Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
title_short Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
title_full Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
title_fullStr Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
title_full_unstemmed Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
title_sort ice crystal habit in the presence of an antifreeze protein from a sea ice diatom
publishDate 2014
url https://epic.awi.de/id/eprint/35515/
https://epic.awi.de/id/eprint/35515/1/Bayer-Giraldi_The_Physics_and_Chemistry_of_Ice.pdf
https://hdl.handle.net/10013/epic.44144
https://hdl.handle.net/10013/epic.44144.d001
genre Sea ice
genre_facet Sea ice
op_source EPIC313th International Conference on the Physics and Chemistry of Ice, Hanover, NH (USA), 2014-03-16-2014-03-20
op_relation https://epic.awi.de/id/eprint/35515/1/Bayer-Giraldi_The_Physics_and_Chemistry_of_Ice.pdf
https://hdl.handle.net/10013/epic.44144.d001
Bayer-Giraldi, M. orcid:0000-0002-7158-5478 , Kipfstuhl, S. , Weikusat, I. orcid:0000-0002-3023-6036 and Dieckmann, G. (2014) Ice crystal habit in the presence of an antifreeze protein from a sea ice diatom , 13th International Conference on the Physics and Chemistry of Ice, Hanover, NH (USA), 16 March 2014 - 20 March 2014 . hdl:10013/epic.44144
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