scholarly journals Ice-binding proteins and the applicability and limitations of the kinetic pinning model

2019 ◽  
Vol 377 (2146) ◽  
pp. 20180391 ◽  
Author(s):  
Michael Chasnitsky ◽  
Ido Braslavsky
Keyword(s):  
Binding Proteins ◽  
Thermal Hysteresis ◽  
Freezing Point ◽  
Ice Crystal ◽  
Water Ice ◽  
Ice Binding ◽  
Production Technologies ◽  
Seeding Time ◽  
Two Phases ◽  
Key Parameter

Ice-binding proteins (IBPs) are unique molecules that bind to and are active on the interface between two phases of water: ice and liquid water. This property allows them to affect ice growth in multiple ways: shaping ice crystals, suppressing the freezing point, inhibiting recrystallization and promoting nucleation. Advances in the protein's production technologies make these proteins promising agents for medical applications among others. Here, we focus on a special class of IBPs that suppress freezing by causing thermal hysteresis (TH): antifreeze proteins (AFPs). The kinetic pinning model describes the dynamics of a growing ice face with proteins binding to it, which eventually slow it down to a halt. We use the kinetic pinning model, with some adjustments made, to study the TH dependence on the solution's concentration of AFPs by fitting the model to published experimental data. We find this model describes the activity of (moderate) type III AFPs well, but is inadequate for the (hyperactive) Tenebrio molitor AFPs. We also find the engulfment resistance to be a key parameter, which depends on the protein's size. Finally, we explain intuitively how TH depends on the seeding time of the ice crystal in the protein solution. Using this insight, we explain the discrepancy in TH measurements between different assays. This article is part of the theme issue ‘The physics and chemistry of ice: scaffolding across scales, from the viability of life to the formation of planets’.

scholarly journals Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics

2014 ◽  
Vol 11 (98) ◽  
pp. 20140526 ◽  
Author(s):  
Ran Drori ◽  
Yeliz Celik ◽  
Peter L. Davies ◽  
Ido Braslavsky
Keyword(s):  
Basal Plane ◽  
Binding Proteins ◽  
Thermal Hysteresis ◽  
Freezing Point ◽  
Ice Crystal ◽  
Ice Binding ◽  
Time Sensitivity ◽  
Custom Made ◽  
Order Of Magnitude ◽  
Accumulation Kinetics

Ice-binding proteins that aid the survival of freeze-avoiding, cold-adapted organisms by inhibiting the growth of endogenous ice crystals are called antifreeze proteins (AFPs). The binding of AFPs to ice causes a separation between the melting point and the freezing point of the ice crystal (thermal hysteresis, TH). TH produced by hyperactive AFPs is an order of magnitude higher than that produced by a typical fish AFP. The basis for this difference in activity remains unclear. Here, we have compared the time dependence of TH activity for both hyperactive and moderately active AFPs using a custom-made nanolitre osmometer and a novel microfluidics system. We found that the TH activities of hyperactive AFPs were time-dependent, and that the TH activity of a moderate AFP was almost insensitive to time. Fluorescence microscopy measurement revealed that despite their higher TH activity, hyperactive AFPs from two insects (moth and beetle) took far longer to accumulate on the ice surface than did a moderately active fish AFP. An ice-binding protein from a bacterium that functions as an ice adhesin rather than as an antifreeze had intermediate TH properties. Nevertheless, the accumulation of this ice adhesion protein and the two hyperactive AFPs on the basal plane of ice is distinct and extensive, but not detectable for moderately active AFPs. Basal ice plane binding is the distinguishing feature of antifreeze hyperactivity, which is not strictly needed in fish that require only approximately 1°C of TH. Here, we found a correlation between the accumulation kinetics of the hyperactive AFP at the basal plane and the time sensitivity of the measured TH.

scholarly journals Ice Nucleation Properties of Ice-binding Proteins from Snow Fleas

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 532 ◽  
Author(s):  
Akalabya Bissoyi ◽  
Naama Reicher ◽  
Michael Chasnitsky ◽  
Sivan Arad ◽  
Thomas Koop ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Thermal Hysteresis ◽  
Ice Nucleation ◽  
Ice Crystals ◽  
Nucleation Theory ◽  
Classical Nucleation Theory ◽  
Ice Binding ◽  
Nucleation Activity ◽  
Ice Shell ◽  
Ice Nucleation Activity

Ice-binding proteins (IBPs) are found in many organisms, such as fish and hexapods, plants, and bacteria that need to cope with low temperatures. Ice nucleation and thermal hysteresis are two attributes of IBPs. While ice nucleation is promoted by large proteins, known as ice nucleating proteins, the smaller IBPs, referred to as antifreeze proteins (AFPs), inhibit the growth of ice crystals by up to several degrees below the melting point, resulting in a thermal hysteresis (TH) gap between melting and ice growth. Recently, we showed that the nucleation capacity of two types of IBPs corresponds to their size, in agreement with classical nucleation theory. Here, we expand this finding to additional IBPs that we isolated from snow fleas (the arthropod Collembola), collected in northern Israel. Chemical analyses using circular dichroism and Fourier-transform infrared spectroscopy data suggest that these IBPs have a similar structure to a previously reported snow flea antifreeze protein. Further experiments reveal that the ice-shell purified proteins have hyperactive antifreeze properties, as determined by nanoliter osmometry, and also exhibit low ice-nucleation activity in accordance with their size.

Annealing condition influences thermal hysteresis of fungal type ice-binding proteins

Cryobiology ◽  
2014 ◽  
Vol 68 (1) ◽  
pp. 159-161 ◽  
Author(s):  
Nan Xiao ◽  
Yuichi Hanada ◽  
Haruhiko Seki ◽  
Hidemasa Kondo ◽  
Sakae Tsuda ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Thermal Hysteresis ◽  
Annealing Condition ◽  
Ice Binding

scholarly journals Growth suppression of ice crystal basal face in the presence of a moderate ice-binding protein does not confer hyperactivity

2018 ◽  
Vol 115 (29) ◽  
pp. 7479-7484 ◽  
Author(s):  
Maddalena Bayer-Giraldi ◽  
Gen Sazaki ◽  
Ken Nagashima ◽  
Sepp Kipfstuhl ◽  
Dmitry A. Vorontsov ◽  
...  
Keyword(s):  
Crystal Growth ◽  
Heat Dissipation ◽  
Freezing Point ◽  
Binding Protein ◽  
Ice Crystals ◽  
Ice Crystal ◽  
Freezing Point Depression ◽  
Basal Face ◽  
Ice Binding ◽  
Ice Binding Protein

Ice-binding proteins (IBPs) affect ice crystal growth by attaching to crystal faces. We present the effects on the growth of an ice single crystal caused by an ice-binding protein from the sea ice microalga Fragilariopsis cylindrus (fcIBP) that is characterized by the widespread domain of unknown function 3494 (DUF3494) and known to cause a moderate freezing point depression (below 1 °C). By the application of interferometry, bright-field microscopy, and fluorescence microscopy, we observed that the fcIBP attaches to the basal faces of ice crystals, thereby inhibiting their growth in the c direction and resulting in an increase in the effective supercooling with increasing fcIBP concentration. In addition, we observed that the fcIBP attaches to prism faces and inhibits their growth. In the event that the effective supercooling is small and crystals are faceted, this process causes an emergence of prism faces and suppresses crystal growth in the a direction. When the effective supercooling is large and ice crystals have developed into a dendritic shape, the suppression of prism face growth results in thinner dendrite branches, and growth in the a direction is accelerated due to enhanced latent heat dissipation. Our observations clearly indicate that the fcIBP occupies a separate position in the classification of IBPs due to the fact that it suppresses the growth of basal faces, despite its moderate freezing point depression.

scholarly journals Falling Water Ice Purification of Ice-Binding Proteins

2018 ◽  
Author(s):  
Chen Adar ◽  
Vera Sirotinskaya ◽  
Maya Bar Dolev ◽  
Tomer Friehmann ◽  
Ido Braslavsky
Keyword(s):  
Binding Proteins ◽  
Vertical Surface ◽  
Ice Crystals ◽  
New Method ◽  
Food Storage ◽  
High Quality ◽  
Natural Sources ◽  
Water Ice ◽  
Ice Binding ◽  
Commercial Applications

Ice-binding proteins (IBPs) have several functions that permit their hosts to thrive in the presence of ice. The ability of IBPs to control ice growth makes them potential additives in various industries ranging from food storage and cryopreservation to anti-icing systems. For IBPs to be used in commercial applications, however, methods are needed to produce sufficient quantities of high-quality proteins. Here, we describe a new method for IBP purification, termed falling water ice purification (FWIP). The method is based on the affinity of IBPs for ice. A crude IBP solution is allowed to flow continuously over the large chilled vertical surface of a commercial ice machine. The temperature of the surface is lowered gradually until ice crystals are produced, to which the IBPs bind but other solutes do not. As in other ice affinity methods, FWIP does not require molecular tags and is suitable for purifying recombinant IBPs as well as IBPs from natural sources. The advantage of FWIP over other ice affinity methods is that it exploits an ice machine designed to produce large volumes of clear ice daily. This system can be easily scaled up and suits the purification of industrial quantities of IBPs. The FWIP method significantly advances the use of IBPs in research and industry.

scholarly journals Falling water ice affinity purification of ice-binding proteins

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Chen Adar ◽  
Vera Sirotinskaya ◽  
Maya Bar Dolev ◽  
Tomer Friehmann ◽  
Ido Braslavsky
Keyword(s):  
Binding Proteins ◽  
Affinity Purification ◽  
Water Ice ◽  
Ice Binding

scholarly journals Systematic Affiliation and Genome Analysis of Subtercola vilae DB165T with Particular Emphasis on Cold Adaptation of an Isolate from a High-Altitude Cold Volcano Lake

2019 ◽  
Vol 7 (4) ◽  
pp. 107 ◽  
Author(s):  
Alvaro S. Villalobos ◽  
Jutta Wiese ◽  
Johannes F. Imhoff ◽  
Cristina Dorador ◽  
Alexander Keller ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Cold Shock ◽  
Extreme Environment ◽  
Crystal Formation ◽  
Ice Crystal ◽  
Cold Environments ◽  
Ice Binding ◽  
Shock Proteins ◽  
Harsh Conditions ◽  
Insight Into

Among the Microbacteriaceae the species of Subtercola and Agreia form closely associated clusters. Phylogenetic analysis demonstrated three major phylogenetic branches of these species. One of these branches contains the two psychrophilic species Subtercola frigoramans and Subtercola vilae, together with a larger number of isolates from various cold environments. Genomic evidence supports the separation of Agreia and Subtercola species. In order to gain insight into the ability of S. vilae to adapt to life in this extreme environment, we analyzed the genome with a particular focus on properties related to possible adaptation to a cold environment. General properties of the genome are presented, including carbon and energy metabolism, as well as secondary metabolite production. The repertoire of genes in the genome of S. vilae DB165T linked to adaptations to the harsh conditions found in Llullaillaco Volcano Lake includes several mechanisms to transcribe proteins under low temperatures, such as a high number of tRNAs and cold shock proteins. In addition, S. vilae DB165T is capable of producing a number of proteins to cope with oxidative stress, which is of particular relevance at low temperature environments, in which reactive oxygen species are more abundant. Most important, it obtains capacities to produce cryo-protectants, and to combat against ice crystal formation, it produces ice-binding proteins. Two new ice-binding proteins were identified which are unique to S. vilae DB165T. These results indicate that S. vilae has the capacity to employ different mechanisms to live under the extreme and cold conditions prevalent in Llullaillaco Volcano Lake.

Ice-binding proteins: a remarkable ice crystal regulator for frozen foods

2020 ◽  
pp. 1-14
Author(s):  
Xu Chen ◽  
Xiaodan Shi ◽  
Xixi Cai ◽  
Fujia Yang ◽  
Ling Li ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Ice Crystal ◽  
Frozen Foods ◽  
Ice Binding

scholarly journals Ice Binding Proteins: Diverse Biological Roles and Applications in Different Types of Industry

Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 274 ◽  
Author(s):  
Aneta Białkowska ◽  
Edyta Majewska ◽  
Aleksandra Olczak ◽  
Aleksandra Twarda-Clapa
Keyword(s):  
Binding Proteins ◽  
Thermal Hysteresis ◽  
Industrial Applications ◽  
Food Storage ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Current State ◽  
Ice Binding ◽  
Recrystallization Inhibition ◽  
Living Organisms

More than 80% of Earth’s surface is exposed periodically or continuously to temperatures below 5 °C. Organisms that can live in these areas are called psychrophilic or psychrotolerant. They have evolved many adaptations that allow them to survive low temperatures. One of the most interesting modifications is production of specific substances that prevent living organisms from freezing. Psychrophiles can synthesize special peptides and proteins that modulate the growth of ice crystals and are generally called ice binding proteins (IBPs). Among them, antifreeze proteins (AFPs) inhibit the formation of large ice grains inside the cells that may damage cellular organelles or cause cell death. AFPs, with their unique properties of thermal hysteresis (TH) and ice recrystallization inhibition (IRI), have become one of the promising tools in industrial applications like cryobiology, food storage, and others. Attention of the industry was also caught by another group of IBPs exhibiting a different activity—ice-nucleating proteins (INPs). This review summarizes the current state of art and possible utilizations of the large group of IBPs.

scholarly journals Basidiomycetous Yeast, Glaciozyma antarctica, Forming Frost-Columnar Colonies on Frozen Medium

2021 ◽  
Vol 9 (8) ◽  
pp. 1679
Author(s):  
Seiichi Fujiu ◽  
Masanobu Ito ◽  
Eriko Kobayashi ◽  
Yuichi Hanada ◽  
Midori Yoshida ◽  
...  
Keyword(s):  
Crystal Growth ◽  
Binding Proteins ◽  
East Antarctica ◽  
Basidiomycetous Yeast ◽  
Extracellular Polysaccharides ◽  
Unfrozen Water ◽  
Ice Crystal ◽  
Ice Binding

The basidiomycetous yeast, Glaciozyma antarctica, was isolated from various terrestrial materials collected from the Sôya coast, East Antarctica, and formed frost-columnar colonies on agar plates frozen at −1 °C. Thawed colonies were highly viscous, indicating that the yeast produced a large number of extracellular polysaccharides (EPS). G. antarctica was then cultured on frozen media containing red food coloring to observe the dynamics of solutes in unfrozen water; pigments accumulated in frozen yeast colonies, indicating that solutes were concentrated in unfrozen water of yeast colonies. Moreover, the yeast produced a small quantity of ice-binding proteins (IBPs) which inhibited ice crystal growth. Solutes in unfrozen water were considered to accumulate in the pore of frozen colonies. The extracellular IBPs may have held an unfrozen state of medium water after accumulation in the frost-columnar colony.

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