Winter Flounder “Antifreeze” Proteins:  Synthesis and Ice Growth Inhibition of Analogues that Probe the Relative Importance of Hydrophobic and Hydrogen-Bonding Interactions

1999 ◽  
Vol 121 (5) ◽  
pp. 941-948 ◽  
Author(s):  
A. D. J. Haymet ◽  
Leanne G. Ward ◽  
Margaret M. Harding
Keyword(s):  
Hydrogen Bonding ◽  
Growth Inhibition ◽  
Antifreeze Proteins ◽  
Winter Flounder ◽  
Relative Importance ◽  
Ice Growth ◽  
Hydrogen Bonding Interactions

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>

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.

Three-dimensional simulation of ice growth in the presence of antifreeze proteins

2003 ◽  
Vol 81 (1-2) ◽  
pp. 39-45 ◽  
Author(s):  
B Wathen ◽  
M J Kuiper ◽  
V K Walker ◽  
Z Jia
Keyword(s):  
Crystal Growth ◽  
Growth Inhibition ◽  
Antifreeze Proteins ◽  
Three Dimensional ◽  
Computational Method ◽  
Inhibition Mechanism ◽  
Ice Crystal ◽  
Ice Growth ◽  
Ice Binding ◽  
Dimensional Simulation

A Monte Carlo computational method for simulating the growth of entire ice crystals from the liquid phase has been developed specifically to study the inhibition of ice-crystal growth by antifreeze proteins (AFPs). AFPs are found in the fluids of certain organisms that inhabit freezing environments and constrain ice-crystal growth by adsorbtion to the ice surface, but their inhibition mechanism is still poorly understood. Thus, it was of interest to incorporate these molecules into the dynamic ice simulations to examine the inhibition phenomenon on a whole-crystal basis. We have undertaken simulations with AFPs from two different organisms that differ in activity; the insect AFP has up to 100 times the activity of the fish AFP on a molar basis. Simulations involving insect and fish AFPs have achieved ice-growth inhibition at simulation temperatures within reported activity ranges for both fish and insect AFPs, accompanied by resulting ice morphologies similar to those observed experimentally. These results, as well as other studies on ice-etching patterns and ice burst growth at temperatures below known AFP ice-growth inhibition abilities suggest that AFP activity is dominated by the AFP ice-binding position rather than AFP ice-binding strength. PACS No.: 07.05T

When Are Antifreeze Proteins in Solution Essential for Ice Growth Inhibition?

Langmuir ◽  
2015 ◽  
Vol 31 (21) ◽  
pp. 5805-5811 ◽  
Author(s):  
Ran Drori ◽  
Peter L. Davies ◽  
Ido Braslavsky
Keyword(s):  
Growth Inhibition ◽  
Antifreeze Proteins ◽  
Ice Growth

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>

Sign in / Sign up

Export Citation Format

Share Document