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

Tsuda, Sakae; Yamauchi, Akari; Khan, N. M. -Mofiz Uddin; Arai, Tatsuya; Mahatabuddin, Sheikh; Miura, Ai; Kondo, Hidemasa

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

Tsuda, Sakae; Yamauchi, Akari; Khan, N. M. -Mofiz Uddin et al.

Biomolecules, 2020, 10(3), 423

Permalink : https://hdl.handle.net/2115/78411

このアイテムのアクセス数:651件（2026-08-08 07:46 集計）

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論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/78411
タイトル	Fish-Derived Antifreeze Proteins and Antifreeze Glycoprotein Exhibit a Different Ice-Binding Property with Increasing Concentration
著者	Tsuda, Sakae ; Yamauchi, Akari ; Khan, N. M. -Mofiz Uddin ; Arai, Tatsuya ; Mahatabuddin, Sheikh ; Miura, Ai ; Kondo, Hidemasa
e-Rad_Researcher 70211381 著者名 Tsuda, Sakae
著者名 Yamauchi, Akari
著者名 Khan, N. M. -Mofiz Uddin
著者名 Arai, Tatsuya
著者名 Mahatabuddin, Sheikh
著者名 Miura, Ai
著者名 Kondo, Hidemasa
言語	英語
キーワード	antifreeze protein
	hydration
	ice-binding
	thermal hysteresis
	solubility
	structure
発行日	2020-03
出版者	MDPI
収録物名	Biomolecules
巻(号)	10(3)
ページ	423
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.3390/biom10030423