Certain organisms, including some bugs (both insects and microbes) are able to survive low
temperatures by the production of either ice nucleating proteins (INPs) or antifreeze proteins
(AFPs). INPs direct crystal growth by inducing rapid ice formation whereas AFPs adsorb to ice
embryos and decrease the temperature at which the ice grows. We have also shown that certain
AFPs can inhibit the crystallization of clathrate hydrates and eliminate more rapid
recrystallization or “memory effect”. Here we examine several bacterial species with iceassociating
properties for their effect on tetrahydrofuran (THF) hydrate crystallization. The
bacteria Chryseobacterium sp. C14, which shares the ice recrystallization inhibition ability of
AFPs, increased induction time to THF hydrate crystallization in isothermal experiments. In an
effort to understand the association between AFPs and THF hydrate we have produced
bacterially-expressed AFPs as probes for hydrate binding. Although the structure of hydrates is
clearly distinct from ice, the apparent potential for these products to perturb clathrate hydrate
growth compels us to explore new techniques to uncover “green inhibitors” for hydrate binding.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:BVAU.2429/1105 |
| Date | 07 1900 |
| Creators | Huva, Emily I., Gordienko, Raimond V., Ripmeester, John A., Zeng, Huang, Walker, Virginia K. |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | text |
Page generated in 0.0015 seconds