scholarly journals Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

10.3791/55302 ◽  
2017 ◽  
Author(s):  
Melissa Bredow ◽  
Heather E. Tomalty ◽  
Virginia K. Walker
Keyword(s):  
Binding Proteins ◽  
Affinity Purification ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Ice Binding ◽  
Recrystallization Inhibition

scholarly journals Protection of Alcohol Dehydrogenase against Freeze–Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Property

Marine Drugs ◽  
2020 ◽  
Vol 18 (12) ◽  
pp. 638
Author(s):  
Young Hoon Lee ◽  
Kitae Kim ◽  
Jun Hyuck Lee ◽  
Hak Jun Kim
Keyword(s):  
Alcohol Dehydrogenase ◽  
Binding Proteins ◽  
Residual Activity ◽  
Fluorescence Emission ◽  
Fluorescence Emission Spectra ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Freeze Thaw ◽  
Ice Binding ◽  
Recrystallization Inhibition

Ice-binding proteins (IBPs) have ice recrystallization inhibition (IRI) activity. IRI property has been extensively utilized for the cryopreservation of different types of cells and tissues. Recent reports demonstrated that IRI can also play a significant role in protecting proteins from freezing damage during freeze–thaw cycles. In this study, we hypothesized that the protective capability of IBPs on proteins against freeze–thaw damage is proportional to their IRI activity. Hence we used two IBPs: one with higher IRI activity (LeIBP) and the other with lower activity (FfIBP). Yeast alcohol dehydrogenase (ADH) was used as a freeze-labile model protein. IBPs and ADH were mixed, frozen at −20 °C, and thawed repeatedly. The structure of ADH was assessed using fluorescence emission spectra probed by 1-anilinonaphthalene-8-sulfonate over the repeated freeze–thaw cycles. The activity was monitored at 340 nm spectrophotometrically. Fluorescence data and activity clearly indicated that ADH without IBP was freeze-labile. However, ADH maintained about 70% residual activity after five repeated cycles at a minimal concentration of 0.1 mg mL-1 of high IRI-active LeIBP, but only 50% activity at 4 mg mL−1 of low active FfIBP. These results showed that the protection of proteins from freeze–thaw stress by IBPs is proportional to their IRI activity.

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.

Ice recrystallization inhibition activity varies with ice-binding protein type and does not correlate with thermal hysteresis

Cryobiology ◽  
2021 ◽  
Author(s):  
Audrey K. Gruneberg ◽  
Laurie A. Graham ◽  
Robert Eves ◽  
Prashant Agrawal ◽  
Richard D. Oleschuk ◽  
...  
Keyword(s):  
Thermal Hysteresis ◽  
Binding Protein ◽  
Inhibition Activity ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Ice Binding ◽  
Recrystallization Inhibition ◽  
Ice Binding Protein

Ice recrystallization inhibition mediated by a nuclear-expressed and -secreted recombinant ice-binding protein in the microalga Chlamydomonas reinhardtii

2013 ◽  
Vol 97 (22) ◽  
pp. 9763-9772 ◽  
Author(s):  
Kyle J. Lauersen ◽  
Tara L. Vanderveer ◽  
Hanna Berger ◽  
Isabell Kaluza ◽  
Jan H. Mussgnug ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Binding Protein ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Ice Binding ◽  
Recrystallization Inhibition ◽  
Ice Binding Protein

19. Determining the Ice-binding Face of an Antifreeze Protein from the Grass, Brachypodium distachyon

2018 ◽  
Author(s):  
Lindsay Smith
Keyword(s):  
New Technologies ◽  
Brachypodium Distachyon ◽  
Ice Crystals ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Left Handed ◽  
Subzero Temperatures ◽  
Ice Binding ◽  
Recrystallization Inhibition ◽  
The One

At subzero temperatures extracellular ice growth can kill plants by dehydrating cells and rupturing their membranes. Some grasses can protect themselves from this damage by producing antifreeze proteins (AFPs). These AFPs irreversibly adsorb to growing ice crystals and prevent further gowth. This is measured by ice-recrystallization inhibition (IRI), whereby ice crystals remain small at high sub-zero temperatures. An AFP from Brachypodium distachyon, a temperate grass, has been structurally modelled as a left-handed beta helix with two flat ‘faces’ on either side of the molecule. I am trying to determine which ‘face’ is important for ice adsorption. I have made mutations in the sequence encoding the AFP so that a small, flat amino acid is replaced by a bulky residue, which will likely interfere with the “fit” of the protein to ice. A mutation on one of the flat ‘faces’ of the protein seems to retain all AFP activity, whereas mutations on the opposite ‘face’ appear to cause a loss in activity. Therefore, I believe that this latter ‘face’ is the one important for ice-binding. By understanding how proteins interact with ice, it may be possible to develop new technologies such as environmentally-friendly de-icing agents.

scholarly journals Polymer Self-Assembly Induced Enhancement of Ice Recrystallization Inhibition

2021 ◽  
Author(s):  
Panagiotis G. Georgiou ◽  
Huba L. Marton ◽  
Alexander N. Baker ◽  
Thomas R. Congdon ◽  
Thomas F. Whale ◽  
...  
Keyword(s):  
Self Assembly ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Recrystallization Inhibition

scholarly journals Molecular Dynamics at the Interface between Ice and Poly(vinyl alcohol) and Ice Recrystallization Inhibition

Langmuir ◽  
2017 ◽  
Vol 34 (17) ◽  
pp. 5116-5123 ◽  
Author(s):  
Lindong Weng ◽  
Shannon L. Stott ◽  
Mehmet Toner
Keyword(s):  
Molecular Dynamics ◽  
Vinyl Alcohol ◽  
Poly Vinyl Alcohol ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Recrystallization Inhibition

scholarly journals Ice recrystallization inhibition proteins (IRIPs) and freeze tolerance in the cryophilic Antarctic hair grassDeschampsia antarcticaE. Desv.

2009 ◽  
Vol 32 (4) ◽  
pp. 336-348 ◽  
Author(s):  
ULRIK P. JOHN ◽  
RENATA M. POLOTNIANKA ◽  
KAILAYAPILLAI A. SIVAKUMARAN ◽  
ORINDA CHEW ◽  
LEANNE MACKIN ◽  
...  
Keyword(s):  
Freeze Tolerance ◽  
Ice Recrystallization Inhibition ◽  
Ice Recrystallization ◽  
Recrystallization Inhibition
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