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

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 c-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 c-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a>

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

10.26434/chemrxiv.12915878 ◽

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

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 c-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 c-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a>

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Discovery of an antifreeze protein in the leaves of Ammopiptanthus nanus

Canadian Journal of Plant Science ◽

10.4141/cjps09060 ◽

2010 ◽

Vol 90 (1) ◽

pp. 35-40 ◽

Cited By ~ 7

Author(s):

S. Yu ◽

L. Yin ◽

S. Mu

Keyword(s):

Differential Scanning Calorimetry ◽

Thermal Hysteresis ◽

Large Subunit ◽

Antifreeze Proteins ◽

Cold Climate ◽

High Definition ◽

Scanning Calorimetry ◽

Bisphosphate Carboxylase ◽

Thermal Hysteresis Activity ◽

Ammopiptanthus Nanus

Overwintering plants produce antifreeze proteins (AFPs) that allow plants to survive under freezing or sub-freezing conditions. Ammopiptanthus nanus (M. Pop.) Cheng f. grows in the desert of Xinjiang, P.R. China, and our objective was to determine if its survival was dependent on AFP and to identify the protein. Using anion exchange and gel filtration, the AFP was extracted, isolated and purified from cold-acclimated A. nanus leaves. The thermal hysteresis activity (THA) of the antifreeze proteins was measured by differential scanning calorimetry. The THA of the AFP was 0.46°C when the concentration of the protein was 20 mg mL-1. The molecular weight of a band was about 119.24 kDa in SDS-PAGE gel. We detected (P < 0.05) the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit by analyzing the 119.24 kDa protein using the Waters SYNAPT™ high definition mass spectrometry (HDMS™) System. Our results indicate that there is an AFP in A. nanus leaves, and that it may play a vital role as a defence against the cold climate, thus increasing the chances for survival of A. nanus in its desert habitat.Key words: Thermal hysteresis activity, differential scanning calorimetry, extraction, purification, cold climate, desert habitat

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Experimental correlation between thermal hysteresis activity and the distance between antifreeze proteins on an ice surface

RSC Advances ◽

10.1039/c4ra12638f ◽

2015 ◽

Vol 5 (11) ◽

pp. 7848-7853 ◽

Cited By ~ 25

Author(s):

Ran Drori ◽

Peter L. Davies ◽

Ido Braslavsky

Keyword(s):

Fluorescence Microscopy ◽

Thermal Hysteresis ◽

Freezing Point ◽

Antifreeze Proteins ◽

Microfluidic Devices ◽

Freezing Point Depression ◽

Thermal Hysteresis Activity ◽

Ice Surface ◽

Experimental Correlation ◽

Temperature Controlled

Temperature-controlled microfluidic devices and fluorescence microscopy illustrate the correlation between freezing-point depression and the distance between antifreeze proteins on an ice surface.

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A two-dimensional adsorption kinetic model for thermal hysteresis activity in antifreeze proteins

The Journal of Chemical Physics ◽

10.1063/1.2186309 ◽

2006 ◽

Vol 124 (20) ◽

pp. 204702 ◽

Cited By ~ 12

Author(s):

Q. Z. Li ◽

Y. Yeh ◽

J. J. Liu ◽

R. E. Feeney ◽

V. V. Krishnan

Keyword(s):

Kinetic Model ◽

Thermal Hysteresis ◽

Antifreeze Proteins ◽

Adsorption Kinetic ◽

Two Dimensional ◽

Thermal Hysteresis Activity ◽

Adsorption Kinetic Model

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Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1524109113 ◽

2016 ◽

Vol 113 (14) ◽

pp. 3740-3745 ◽

Cited By ~ 78

Author(s):

Luuk L. C. Olijve ◽

Konrad Meister ◽

Arthur L. DeVries ◽

John G. Duman ◽

Shuaiqi Guo ◽

...

Keyword(s):

Thermal Hysteresis ◽

Comprehensive Evaluation ◽

Antifreeze Proteins ◽

Ice Crystal ◽

Crystal Surfaces ◽

Ice Recrystallization Inhibition ◽

Ice Growth ◽

Recrystallization Inhibition ◽

Water Based ◽

Fast Ice

Antifreeze proteins (AFPs) are a unique class of proteins that bind to growing ice crystal surfaces and arrest further ice growth. AFPs have gained a large interest for their use in antifreeze formulations for water-based materials, such as foods, waterborne paints, and organ transplants. Instead of commonly used colligative antifreezes such as salts and alcohols, the advantage of using AFPs as an additive is that they do not alter the physicochemical properties of the water-based material. Here, we report the first comprehensive evaluation of thermal hysteresis (TH) and ice recrystallization inhibition (IRI) activity of all major classes of AFPs using cryoscopy, sonocrystallization, and recrystallization assays. The results show that TH activities determined by cryoscopy and sonocrystallization differ markedly, and that TH and IRI activities are not correlated. The absence of a distinct correlation in antifreeze activity points to a mechanistic difference in ice growth inhibition by the different classes of AFPs: blocking fast ice growth requires rapid nonbasal plane adsorption, whereas basal plane adsorption is only relevant at long annealing times and at small undercooling. These findings clearly demonstrate that biomimetic analogs of antifreeze (glyco)proteins should be tailored to the specific requirements of the targeted application.

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