open access

https://doi.org/10.14943/lowtemsci.81.51

https://hdl.handle.net/2115/89118

Structure and Function of antifreeze protein

日本語

ice-like waters

2023-03-20

低温科学第81巻編集委員会

Low Temperature Science

81

51-60

第一章：変温動物

A general block of ice is composed of an infinite number of single ice crystals, which is called ice polycrystalline state. Antifreeze protein (AFP) is a macromolecule that locates regularly organized hydration waters on its surface, whose arrangement is also adopted in a single ice crystal. As the consequence, AFP can specifically bind to single ice crystals, which prevents the ice polycrystalline state formation. We have been performed exploration of AFP against various cold-adapted organisms since the late 1990s, and found that many edible fishes available in the general Japanese food markets contain AFP in their body fluid. This finding enabled us to develop a mass-preparation technique of fish-derived AFPs, for which we have been performed structural and functional analyses and technological applications for many years. The advanced knowledge obtained from our results may ultimately realize a new AFP-technology that may prevent water freezing though the binding to single ice crystals, which may keep alive cells, tissues, and animals in the supercooled environment. The present review describes the overview of the waterfreezing mechanism and our research findings on the fish AFPs including their structure, function, and applicability for both industry and medical fields.

紀要論文

Version of Record

1880-7593