Earticle

초록

영어

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.

키워드

저자

• EonSeon JIN [ Department of Life Science, Hanyang University, 133-791 Seoul, South Korea. ]
• Yunho GWAK [ Department of Life Science, Hanyang University, 133-791 Seoul, South Korea. ]
• Woongsic JUNG [ Department of Life Science, Hanyang University, 133-791 Seoul, South Korea. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576