Abstract
Icing and formation of ice crystals is a major obstacle against applications ranging from energy systems to transportation and aviation. Icing not only introduces excess thermal resistance, but it also reduces the safety in operating systems. Many organisms living under harsh climate and subzero temperature conditions have developed extraordinary survival strategies to avoid or delay ice crystal formation. There are several types of antifreeze glycoproteins with ice-binding ability to hamper ice growth, ice nucleation, and recrystallization. Scientists adopted similar approaches to utilize a new generation of engineered antifreeze and ice-binding proteins as bio cryoprotective agents for preservation and industrial applications. There are numerous types of antifreeze proteins (AFPs) categorized according to their structures and functions. The main challenge in employing such biomolecules on industrial surfaces is the stabilization/coating with high efficiency. In this review, we discuss various classes of antifreeze proteins. Our particular focus is on the elaboration of potential industrial applications of anti-freeze polypeptides.
Highlights
Ice crystallization and ice formation are major drawbacks that considerably hinder the productivity of industrial machinery and equipment with a cooling system
While icenucleation proteins (INP) contribute to the generation of ice crystals at the freezing temperature, antifreeze proteins (AFP) effectively mitigate freezing around the organism’s body fluids, and Recrystallization Inhibition Proteins (RIPs) inhibit the recrystallization of ice in freeze-tolerant organisms that could freeze and yet survive the freezing temperature (Ramløv and Friis, 2020a)
A successful immobilization on Aluminum coated surface using Aluminum-binding peptide (ABP)-Cn-AFPG124Y fusion proteins Stable antifreeze activity up to 12 days at room temperature Selection of the repeating polypeptides consisting of 14–28 identical residues with metal binding capacity to gold or chromium among five million various polypeptides Biosynthesis of Ag nanoparticles using metal binding peptides which are able to associate to metal cluster using “memory effect” factor Employing Poly l lysine for microbial biocoating on metal surfaces resulted in an energy conservation for more than 10%
Summary
Ice crystallization and ice formation are major drawbacks that considerably hinder the productivity of industrial machinery and equipment with a cooling system. While INPs contribute to the generation of ice crystals at the freezing temperature, AFPs effectively mitigate freezing around the organism’s body fluids, and RIPs inhibit the recrystallization of ice in freeze-tolerant organisms that could freeze and yet survive the freezing temperature (Ramløv and Friis, 2020a) According to their primary and tertiary structures, AFPs of antarctic and arctic inhabitants are classified into four groups as I, II, III, and IV (Figure 2). In a series of structural studies on Leucosporidium sp., an arctic yeast, Lee and his team demonstrated that various classes of AFPs from fish (I-IV), plants, and insects shared similar icebinding domains, which were adequately consistent and hydrophobic; the distinct folds in each one were significant (Hanada et al, 2014) These studies provided sufficient evidence in showing different family species possessing ice-binding properties, which shared the essential common domain of right-handed beta helical structure for ice-binding activity. The intracellular IRI proteins in these species control the formation
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