|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Fish-Derived Antifreeze Proteins and Antifreeze Glycoprotein Exhibit a Different Ice-Binding Property with Increasing Concentration
| Title: | Fish-Derived Antifreeze Proteins and Antifreeze Glycoprotein Exhibit a Different Ice-Binding Property with Increasing Concentration |
| Authors: | Tsuda, Sakae Browse this author →KAKEN DB | | Yamauchi, Akari Browse this author | | Khan, N. M. -Mofiz Uddin Browse this author | | Arai, Tatsuya Browse this author | | Mahatabuddin, Sheikh Browse this author | | Miura, Ai Browse this author | | Kondo, Hidemasa Browse this author |
| Keywords: | antifreeze protein | | hydration | | ice-binding | | thermal hysteresis | | solubility | | structure |
| Issue Date: | Mar-2020 |
| Publisher: | MDPI |
| Journal Title: | Biomolecules |
| Volume: | 10 |
| Issue: | 3 |
| Start Page: | 423 |
| Publisher DOI: | 10.3390/biom10030423 |
| Abstract: | The concentration of a protein is highly related to its biochemical properties, and is a key determinant for its biotechnological applications. Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) are structurally diverse macromolecules that are capable of binding to embryonic ice crystals below 0 degrees C, making them useful as protectants of ice-block formation. In this study, we examined the maximal solubility of native AFP I-III and AFGP with distilled water, and evaluated concentration dependence of their ice-binding property. Approximately 400 mg/mL (AFP I), 200 mg/mL (AFP II), 100 mg/mL (AFP III), and >1800 mg/mL (AFGP) of the maximal solubility were estimated, and among them AFGP's solubility is much higher compared with that of ordinary proteins, such as serum albumin (similar to 500 mg/mL). The samples also exhibited unexpectedly high thermal hysteresis values (2-3 degrees C) at 50-200 mg/mL. Furthermore, the analysis of fluorescence-based ice plane affinity showed that AFP II binds to multiple ice planes in a concentration-dependent manner, for which an oligomerization mechanism was hypothesized. The difference of concentration dependence between AFPs and AFGPs may provide a new clue to help us understand the ice-binding function of these proteins. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/78411 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
|
