Fish-Derived Antifreeze Proteins and Antifreeze Glycoprotein Exhibit a Different Ice-Binding Property with Increasing Concentration
| Autor: | Hidemasa Kondo, Tatsuya Arai, Sakae Tsuda, Sheikh Mahatabuddin, Akari Yamauchi, Ai Miura, N. M.-Mofiz Uddin Khan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Fish Proteins
0301 basic medicine thermal hysteresis Serum albumin lcsh:QR1-502 010402 general chemistry 01 natural sciences Biochemistry Article lcsh:Microbiology 03 medical and health sciences ice-binding Antifreeze protein Antifreeze Proteins Animals structure Solubility Molecular Biology chemistry.chemical_classification Chromatography biology solubility Ice Fishes 0104 chemical sciences 030104 developmental biology Ice binding chemistry Distilled water Antifreeze biology.protein Glycoprotein human activities antifreeze protein hydration Macromolecule |
| Zdroj: | Biomolecules, Vol 10, Iss 3, p 423 (2020) Biomolecules Volume 10 Issue 3 |
| Popis: | 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 ° C, making them useful as protectants of ice-block formation. In this study, we examined the maximal solubility of native AFP I&ndash 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&rsquo s solubility is much higher compared with that of ordinary proteins, such as serum albumin (~500 mg/mL). The samples also exhibited unexpectedly high thermal hysteresis values (2&ndash 3 ° C) at 50&ndash 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. |
| Databáze: | OpenAIRE |
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