9. Cooperative ice growth inhibition of the isoforms of type III antifreeze protein

Cryobiology ◽  
2009 ◽  
Vol 59 (3) ◽  
pp. 372
Author(s):  
Manabu Takamichi ◽  
Yoshiyuki Nishimiya ◽  
Ai Miura ◽  
Sakae Tsuda
Biomolecules ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 70 ◽  
Author(s):  
Yuki Takeshita ◽  
Tomonori Waku ◽  
Peter W. Wilson ◽  
Yoshimichi Hagiwara

The control of ice growth in ice slurry is important for many fields, including (a) the cooling of the brain during cardiac arrest, (b) the storage and transportation of fresh fish and fruits, and (c) the development of distributed air-conditioning systems. One of the promising methods for the control is to use a substance such as antifreeze protein. We have observed and report here growth states of ice particles in both quiescent and flowing aqueous solutions of winter flounder antifreeze proteins in mini-channels with a microscope. We also measured ice growth rates. Our aim was to improve the levels of ice growth inhibition by subjecting the antifreeze protein solution both to preheating and to concentrating by ultrafiltration. We have found that the ice growth inhibition by the antifreeze protein decreased in flowing solutions compared with that in quiescent solutions. In addition, unlike unidirectional freezing experiments, the preheating of the antifreeze protein solution reduced the ice growth inhibition properties. This is because the direction of flow, containing HPLC6 and its aggregates, to the ice particle surfaces can change as the ice particle grows, and thus the probability of interaction between HPLC6 and ice surfaces does not increase. In contrast to this, ultrafiltration after preheating the solution improved the ice growth inhibition. This may be due to the interaction between ice surfaces and many aggregates in the concentrates.


1996 ◽  
Vol 71 (5) ◽  
pp. 2346-2355 ◽  
Author(s):  
C.I. DeLuca ◽  
H. Chao ◽  
F.D. Sönnichsen ◽  
B.D. Sykes ◽  
P.L. Davies

FEBS Letters ◽  
1997 ◽  
Vol 412 (1) ◽  
pp. 241-244 ◽  
Author(s):  
Lars Chapsky ◽  
Boris Rubinsky

2014 ◽  
Vol 2 (12) ◽  
pp. 1787-1795 ◽  
Author(s):  
Daniel E. Mitchell ◽  
Mary Lilliman ◽  
Sebastian G. Spain ◽  
Matthew I. Gibson

Antifreeze (glyco) proteins (AF(G)Ps) from the blood of polar fish species are extremely potent ice recrystallization inhibitors (IRI), but are difficult to synthesise or extract from natural sources.


Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 306
Author(s):  
Kazuya Taira ◽  
Tomonori Waku ◽  
Yoshimichi Hagiwara

The control of ice growth inside channels of aqueous solution flows is important in numerous fields, including (a) cold-energy transportation plants and (b) the preservation of supercooled human organs for transplantation. A promising method for this control is to add a substance that influences ice growth in the flows. However, limited results have been reported on the effects of such additives. Using a microscope, we measured the growth of ice from one sidewall toward the opposite sidewall of a mini-channel, where aqueous solutions of sodium chloride and antifreeze protein flowed. Our aim was to considerably suppress ice growth by mixing the two solutes. Inclined interfaces, the overlapping of serrated interfaces, and interfaces with sharp and flat tips were observed in the cases of the protein-solution, salt-solution, and mixed-solution flows, respectively. In addition, it was found that the average interface velocity in the case of the mixed-solution flow was the lowest and decreased by 64% compared with that of pure water. This significant suppression of the ice-layer growth can be attributed to the synergistic effects of the ions and antifreeze protein on the diffusion of protein.


2020 ◽  
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori

<p>Since some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all crystal planes, they change ice crystal morphology by minimizing the area of the crystal planes to which they cannot bind until crystal growth is halted. Previous studies found that growth along the <i>c</i>-axis (perpendicular to the basal plane, the crystal plane to which these AF(G)Ps cannot bind) is accelerated by some AF(G)Ps, while growth of other planes is inhibited. The effects of this growth acceleration on crystal morphology and on the thermal hysteresis activity are unknown to date. Understanding these effects will elucidate the mechanism of ice growth inhibition by AF(G)Ps. Using cold stages and an Infrared laser, ice growth velocities and crystal morphologies in AF(G)P solutions were measured. Three types of effects on growth velocity were found: concentration-dependent acceleration, concentration-independent acceleration, and concentration-dependent deceleration. Quantitative crystal morphology measurements in AF(G)P solutions demonstrated that adsorption rate of the proteins to ice plays a major role in determining the morphology of the bipyramidal crystal. These results demonstrate that faster adsorption rates generate bipyramidal crystals with diminished basal surfaces at higher temperatures compared to slower adsorption rates. The acceleration of growth along the <i>c</i>-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a></p>


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