Antifreeze protection from freezing in cold environments (Mondal

Antifreeze protein is a sequence of amino acid that
can prevent the formation of ice crystal growth by lowering the water freezing
point. However, it do not changing the water melting point. The large growth of
ice crystal can burst the organism’s cells at low temperature. The uses of
antifreeze protein is to control the growth of ice crystal. However the ice is
not fully stop growth, it only can limit the ice growth to manageable sizes. It
can be called as ice-restructuring proteins. When the cells is at low
temperature, water molecule inside the cell slowly begins to freeze. However,
when many crystal start to form and dominate inside the cell, it called as
recrystallization. Antifreeze protein can overcome the recrystallization by
binding to the surface of the small ice crystals and prevent the large ice
growth. Antifreeze protein can protect the cell from cold damage.

Hyperactive antifreeze protein has affinity for the
basal plane as its characteristics, which prevent ice crystal growth, thus it
will protect the crystal from growth down to lower freezing temperatures (Middleton et al., 2012). Ewart, Lin, and Hew (1999) illustrate that
the antifreeze proteins and glycoproteins AF(G)P were first identified in c
as the causative agents of serum freezing point depression. Jia and Davies (2002) show that binding
of AFP must be almost irreversible because any significant off-rate would lead
to ice growth. Irreversibility could stem from the extent of the surface area
in contact once the AFP has docked to ice, thus a large interaction between ice
crystal growth need an effort to release the ligand. Griffith and Ewart (1995) propose that
antifreeze proteins (AFPs), antifreeze glycoproteins (AFGPs) and thermal
hysteresis proteins (THPs) can attach to ice and control the normal growth of
ice crystal. The antifreeze proteins were effective at very low concentrations (Payne, Sandford, Harris, & Young, 1994). Antifreeze
proteins (AFPs) refer to a polypeptides found in organisms or microorganisms
especially in fish inhabitants of ice-laden sea water, which have protection
from freezing in cold environments (Mondal & Pai, 2014).

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Antifreeze protein prevent water  molecules from binding to the ice surface at
the bound location, which is energetically unfavourable for ice growth (Hakim et al., 2013). Antifreeze
proteins (AFPs) were characterized in marine fishes, where they protect their
cells from freezing by binding to ice crystal growth and avoid the growth (Guo, Garnham, Whitney, Graham, & Davies, 2012). Lee et al. (2010) state that AFPs
have ice recrystallization inhibition (RI) activity which prevents growth of
large ice at the expense of smaller grains. Because recrystallization can
damage cell membranes, RI activity can increase the freeze-thaw survival of
cells. Gilbert, Davies, and Laybourn-Parry (2005) report on an
uncharacteristically powerful bacterial AFP found in an Antarctica strain of
the bacterium Marinomonas primaryonesis which
is Ca2+ dependent, shows evidence of cooperativity, and can produces
over 2? freezing point depression. Ice crystal grown in the presence of high
concentrations of AFPs acquire unusual faceted or needle-like morphologies (Griffith and Ewart,1995). Warren et al.
(1992) showed that antifreeze proteins reduce recrystallization in foods and
were granted a United States patent on the use of their synthetic antifreeze
proteins in frozen products. 

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