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- W2269439782 abstract "Antifreeze proteins (AFP) have an ability to bind ice crystals and cause thermal hysteresis (TH) which lowers the freezing temperature without affecting the melting point. Thereby, AFPs have already been applied in various areas (food, medical, cryopreservation and cold hardness of crop plant). Immunolocalization, western blot and antifreeze activity assay clearly showed that antartic diatom AFPs were located in the intracellular area, apoplastic region near to the membrane and flagella. When, the AFPs activities were measured, the maximum TH values of recombinant diatom AFP was measured as 1.28℃ at the protein concentration of 10 mg/ml protein. To predict the ice binding site, 3-dimensional structure of diatom AFP was simulated in silico. Amino acid substitution by point mutations was performed to verify the putative ice-binding surface. Mutant diatom AFPs which had substituted amino acids of the predicted ice binding site revealed 10% TH activity of that of the wild type AFP and exhibited changed ice crystal form at various protein concentrations compared to that of the wild type AFP. The possible explanation of the ice binding mechanism and its biotechnological application will be discussed." @default.
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- W2269439782 date "2013-04-01" @default.
- W2269439782 modified "2023-09-22" @default.
- W2269439782 title "Isolation and Biotechnological Application of Antifreeze Proteins from Antarctic Microalgae" @default.
- W2269439782 hasPublicationYear "2013" @default.
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