Quantitative study on the antifreeze protein mimetic ice growth inhibition properties of poly(ampholytes) derived from vinyl-based polymers

2014 ◽  
Vol 2 (12) ◽  
pp. 1787-1795 ◽  
Author(s):  
Daniel E. Mitchell ◽  
Mary Lilliman ◽  
Sebastian G. Spain ◽  
Matthew I. Gibson
Keyword(s):  
Growth Inhibition ◽  
Quantitative Study ◽  
Fish Species ◽  
Antifreeze Protein ◽  
Natural Sources ◽  
Ice Recrystallization ◽  
Ice Growth ◽  
Polar Fish

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.

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
Keyword(s):  
Growth Inhibition ◽  
Antifreeze Protein ◽  
Type Iii ◽  
Ice Growth

scholarly journals Effects of Winter Flounder Antifreeze Protein on the Growth of Ice Particles in an Ice Slurry Flow in Mini-Channels

Biomolecules ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 70 ◽  
Author(s):  
Yuki Takeshita ◽  
Tomonori Waku ◽  
Peter W. Wilson ◽  
Yoshimichi Hagiwara
Keyword(s):  
Growth Inhibition ◽  
Antifreeze Protein ◽  
Winter Flounder ◽  
Ice Slurry ◽  
Protein Solution ◽  
Fresh Fish ◽  
Ice Growth ◽  
Ice Particles ◽  
Mini Channels ◽  
Ice Surfaces

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.

scholarly journals Ice-recrystallization inhibiting polymers protect proteins against freeze-stress and enable glycerol-free cryostorage

2019 ◽  
Vol 6 (2) ◽  
pp. 364-368 ◽  
Author(s):  
Daniel E. Mitchell ◽  
Alice E. R. Fayter ◽  
Robert C. Deller ◽  
Muhammad Hasan ◽  
Jose Gutierrez-Marcos ◽  
...  
Keyword(s):  
Antifreeze Protein ◽  
Solvent Free ◽  
Ice Recrystallization ◽  
Ice Growth ◽  
Freeze Stress

Antifreeze-protein mimic polymers are shown to enable solvent-free storage of important proteins for therapy and biotechnology by modulating ice growth.

scholarly journals Kinetics of antifreeze protein-induced ice growth inhibition

FEBS Letters ◽  
1997 ◽  
Vol 412 (1) ◽  
pp. 241-244 ◽  
Author(s):  
Lars Chapsky ◽  
Boris Rubinsky
Keyword(s):  
Growth Inhibition ◽  
Antifreeze Protein ◽  
Ice Growth ◽  
Kinetics Of

scholarly journals Ice Growth Suppression in the Solution Flows of Antifreeze Protein and Sodium Chloride in a Mini-Channel

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 306
Author(s):  
Kazuya Taira ◽  
Tomonori Waku ◽  
Yoshimichi Hagiwara
Keyword(s):  
Sodium Chloride ◽  
Synergistic Effects ◽  
Pure Water ◽  
Interface Velocity ◽  
Antifreeze Protein ◽  
Layer Growth ◽  
Mixed Solution ◽  
Solution Flow ◽  
Ice Growth ◽  
Cold Energy

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.

Intracellular oxygen diffusion: the roles of myoglobin and lipid at cold body temperature.

1998 ◽  
Vol 201 (8) ◽  
pp. 1119-1128 ◽  
Author(s):  
B D Sidell
Keyword(s):  
Body Temperature ◽  
Fish Species ◽  
Oxygen Diffusion ◽  
Mechanical Performance ◽  
Muscle Cells ◽  
Cold Temperature ◽  
Oxygen Binding ◽  
Mitochondrial Density ◽  
Polar Fish ◽  
The Mean

Cold temperature can constrain the rate of oxygen movement through muscle cells of ectothermic animals because the kinetic energy of the solvent-solute system decreases and the viscosity of the aqueous cytoplasm increases during cooling within the physiological range of body temperatures. These factors affect the movement of both dissolved oxygen and oxymyoglobin, the two predominant routes of intracellular oxygen diffusion in vertebrate oxidative muscles. In addition, reductions in temperature have been shown to increase the affinity of myoglobin for oxygen and to slow the rate of Mb O2-dissociation, compromising the ability of this oxygen-binding protein to facilitate intracellular oxygen diffusion. Experiments with both seasonally cold-bodied fishes and polar fish species suggest that several factors combine to overcome these limitations in delivery of oxygen from the blood to the mitochondria. First, reductions in body temperature induce increases in mitochondrial density of oxidative muscle cells, reducing the mean diffusional pathlength for oxygen between capillaries and mitochondria. Second, cold body temperature in both temperate-zone and polar fishes is frequently correlated with a high content of neutral lipid in oxidative muscles, providing an enhanced diffusional pathway for oxygen through the tissue. Third, recent data indicate that myoglobins from fish species bind and release oxygen more rapidly at cold temperature than do those from mammals. Data from both oxidative skeletal muscle and cardiac muscle of fishes suggest that these factors in various combinations contribute to enhance the aerobically supported mechanical performance of the tissues at cold cellular temperatures.

scholarly journals Ice Growth Acceleration by Antifreeze Proteins Leads to Higher Thermal Hysteresis Activity

2020 ◽  
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori
Keyword(s):  
Crystal Growth ◽  
Growth Inhibition ◽  
Growth Velocity ◽  
Crystal Morphology ◽  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Ice Crystal ◽  
Ice Growth ◽  
Thermal Hysteresis Activity ◽  
Adsorption Rates

<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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