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Fish-Derived Antifreeze Proteins and Antifreeze Glycoprotein Exhibit a Different Ice-Binding Property with Increasing Concentration

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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)

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