İnternational Agricultural Science Conress, Van, Türkiye, 9 - 12 Mayıs 2018, ss.289, (Özet Bildiri)
Antifreeze proteins (AFP) were first discovered by De Vries et al.
in blood plasmas of Antarctic fish (Notohenioides). Antifreeze proteins
show a great diversity in their structure, and they are identified in a variety
of organisms including bacteria, insects, plants and fish. They are
glycopeptide structures formed by the attachment of a third amino acid
disaccharide molecule of a three amino acid peptide chain and their
repetition (Ala-Ala-Thr-galactosyl-N-acetyl galactosamine). Antifreeze
proteins have special relevance to ice crystals. Because of this interest
Antifreeze proteins have the ability to bind ice crystals and control the
growth and recrystallization of ice crystals. AFPs are very important in
preserving quality and texture by keeping the heat away from frost. These
special proteins, which have important functional properties for the food
industry, are now being used effectively in the medical, food and industrial
fields.