Functional Analysis of Antifreeze Protein from Ascomycete

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  • FUKAMI Daichi
    Transdisciplinary Life Science Course, Graduate School of Life Science, Hokkaido University
  • HANADA Yuichi
    Transdisciplinary Life Science Course, Graduate School of Life Science, Hokkaido University
  • CHENG Jing
    Transdisciplinary Life Science Course, Graduate School of Life Science, Hokkaido University
  • TSUDA Sakae
    Transdisciplinary Life Science Course, Graduate School of Life Science, Hokkaido University:Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology(AIST)
  • KONDO Hidemasa
    Transdisciplinary Life Science Course, Graduate School of Life Science, Hokkaido University:Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology(AIST)

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Other Title
  • 子嚢菌由来不凍タンパク質の機能解析
  • シノウキン ユライ フトウタンパクシツ ノ キノウ カイセキ

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Antifreeze protein (AFP) specifically binds to ice crystal surface and inhibits its growth. In order to elucidate ice-binding mechanism of fungal AFPs, we performed measurements of thermal hysteresis (TH) activity and a recently developed method called "Fluorescence-based Ice Plane Affinity (FIPA)" analysis against AFP identified from Antarctic ascomycete, Antarctomyces psychrotrophicus (AnpAFP). AnpAFP showed a maximum TH of 0.8℃ and led to an ice growth along with the c-axis, which were typical for AFP with moderate antifreeze activity. In addition, FIPA analysis showed that AnpAFP bound to only prism planes of an ice crystal. Such an ice-binding manner of AnpAFP is different from that of the other known microbial AFPs, since they can bind to both prism and basal planes.

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