Antifreeze proteins from snow mold fungi

2003 ◽  
Vol 81 (12) ◽  
pp. 1175-1181 ◽  
Author(s):  
Tamotsu Hoshino ◽  
Michiko Kiriaki ◽  
Satoru Ohgiya ◽  
Mineko Fujiwara ◽  
Hidemasa Kondo ◽  
...  

The psychrophilic fungi Coprinus psychromorbidus and Typhula ishikariensis produced unique antifreeze proteins (AFPs) in the extracellular space. Molecular masses of purified fungal AFPs of C. psychromorbidus and T. ishikariensis were approximately 22 and 23 kDa, respectively. Cloned genes of AFPs from T. ishikariensis do not have any similarity with known proteins. Purified fungal AFPs from cultural filtrate of T. ishikariensis and recombinant fungal AFP from methylotrophic yeast formed specific ice crystals resembling "Stone Age knives". These observations indicate that fungal AFPs do not form proper hexagonal ice crystals to inhibit their growth and that fungal AFPs can probably bind to surfaces of ice crystals in an irregular manner.Key words: antifreeze protein, snow mold fungi, Coprinus psychromorbidus, Typhula ishikariensis.


Author(s):  
Jun Jie Liu ◽  
Yangzong Qin ◽  
Maya Bar Dolev ◽  
Yeliz Celik ◽  
J. S. Wettlaufer ◽  
...  

The melting of pure axisymmetric ice crystals has been described previously by us within the framework of so-called geometric crystal growth . Non-equilibrium ice crystal shapes evolving in the presence of hyperactive antifreeze proteins (hypAFPs) are experimentally observed to assume ellipsoidal geometries (‘lemon’ or ‘rice’ shapes). To analyse such shapes, we harness the underlying symmetry of hexagonal ice I h and extend two-dimensional geometric models to three-dimensions to reproduce the experimental dissolution process. The geometrical model developed will be useful as a quantitative test of the mechanisms of interaction between hypAFPs and ice.



CrystEngComm ◽  
2017 ◽  
Vol 19 (16) ◽  
pp. 2163-2167 ◽  
Author(s):  
Charles H. Z. Kong ◽  
Ivanhoe K. H. Leung ◽  
Vijayalekshmi Sarojini

Synthetic antifreeze peptides based on the hyperactive antifreeze protein modify the shape of ice crystals and show enhanced antifreeze activity with the addition of a small molecule.



1999 ◽  
Author(s):  
Edward I. Naats ◽  
Anatoli G. Borovoi ◽  
Ulrich G. Oppel
Keyword(s):  


1985 ◽  
Vol 2 (4) ◽  
pp. 446-454
Author(s):  
Qiming Cai ◽  
Kuo-Nan Liou


Author(s):  
Alexander V. Konoshonkin ◽  
Natalia V. Kustova ◽  
Andrey P. Lyulyakin ◽  
Anatoli G. Borovoi ◽  
Victor Shishko


Crystals ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 352 ◽  
Author(s):  
Adiel F. Perez ◽  
Kyle R. Taing ◽  
Justin C. Quon ◽  
Antonia Flores ◽  
Yong Ba

Antifreeze proteins (AFPs) protect organisms living in subzero environments from freezing injury, which render them potential applications for cryopreservation of living cells, organs, and tissues. Cryoprotective agents (CPAs), such as glycerol and propylene glycol, have been used as ingredients to treat cellular tissues and organs to prevent ice crystal’s formation at low temperatures. To assess AFP’s function in CPA solutions, we have the applied site-directed spin labeling technique to a Type I AFP. A two-step process to prevent bulk freezing of the CPA solutions was observed by the cryo-photo microscopy, i.e., (1) thermodynamic freezing point depression by the CPAs; and (2) inhibition to the growth of seed ice crystals by the AFP. Electron paramagnetic resonance (EPR) experiments were also carried out from room temperature to 97 K, and vice versa. The EPR results indicate that the spin labeled AFP bound to ice surfaces, and inhibit the growths of ice through the bulk freezing processes in the CPA solutions. The ice-surface bound AFP in the frozen matrices could also prevent the formation of large ice crystals during the melting processes of the solutions. Our study illustrates that AFPs can play an active role in CPA solutions for cryopreservation applications.



1999 ◽  
Vol 38 (9) ◽  
pp. 1626 ◽  
Author(s):  
Michael I. Mishchenko ◽  
Andreas Macke
Keyword(s):  


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