FOOD SCIENCE

• Reviews • Previous Articles     Next Articles

Relationship between Structure and Antifreeze Activity in Fish Antifreeze Proteins

JI Ruiqing1, LIU Aiguo1,*, CHEN Long1, WU Zijian1, HU Zhaobo2, LIU Bin3   

  1. 1. Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce,
    Tianjin 300134, China; 2. Tianjin Food Research Institute, Tianjin 301609, China; 3. Tianjin Key Laboratory of Refrigeration
    Technology, Tianjin University of Commerce, Tianjin 300134, China
  • Online:2015-03-15 Published:2015-03-17

Abstract:

Antifreeze proteins, which possess strong antifreeze activity, can effectively inhibit ice growth and
recrystallization by binding irreversibly to the ice crystal surface. The structural characteristics (including amino acid
residues, specific sequences, secondary structure contents and protein spatial configuration) of six representative kinds of fish
antifreeze proteins, important factors involved in stabilizing protein structure and amino-acid residue sites involved in ice
binding are discussed in this paper. Much attention is focused on revealing the potential relationship between structure and
antifreeze activity, and the purpose is to provide a theoretical basis for its widespread application in the future.

Key words: fish antifreeze proteins, structure, antifreeze activity, ice-binding property

CLC Number: