Ice recrystallization inhibition activity varies with ice-binding protein type and does not correlate with thermal hysteresis

Cryobiology ◽  
2021 ◽  
Author(s):  
Audrey K. Gruneberg ◽  
Laurie A. Graham ◽  
Robert Eves ◽  
Prashant Agrawal ◽  
Richard D. Oleschuk ◽  
...  
Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 274 ◽  
Author(s):  
Aneta Białkowska ◽  
Edyta Majewska ◽  
Aleksandra Olczak ◽  
Aleksandra Twarda-Clapa

More than 80% of Earth’s surface is exposed periodically or continuously to temperatures below 5 °C. Organisms that can live in these areas are called psychrophilic or psychrotolerant. They have evolved many adaptations that allow them to survive low temperatures. One of the most interesting modifications is production of specific substances that prevent living organisms from freezing. Psychrophiles can synthesize special peptides and proteins that modulate the growth of ice crystals and are generally called ice binding proteins (IBPs). Among them, antifreeze proteins (AFPs) inhibit the formation of large ice grains inside the cells that may damage cellular organelles or cause cell death. AFPs, with their unique properties of thermal hysteresis (TH) and ice recrystallization inhibition (IRI), have become one of the promising tools in industrial applications like cryobiology, food storage, and others. Attention of the industry was also caught by another group of IBPs exhibiting a different activity—ice-nucleating proteins (INPs). This review summarizes the current state of art and possible utilizations of the large group of IBPs.


2012 ◽  
Vol 33 (11) ◽  
pp. 3565-3570 ◽  
Author(s):  
Mija Ahn ◽  
Ravichandran N. Murugan ◽  
Song Yub Shin ◽  
Eunjung Kim ◽  
Jun Hyuck Lee ◽  
...  

2019 ◽  
Vol 62 (7) ◽  
pp. 909-915 ◽  
Author(s):  
Shenglin Jin ◽  
Lingkang Yin ◽  
Bin Kong ◽  
Shuwang Wu ◽  
Zhiyuan He ◽  
...  

2018 ◽  
Vol 24 (31) ◽  
pp. 7834-7839 ◽  
Author(s):  
Madeleine K. Adam ◽  
Charles Jarrett-Wilkins ◽  
Michael Beards ◽  
Emiliyan Staykov ◽  
Liam R. MacFarlane ◽  
...  

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