Antifreeze Proteins and Their Practical Utilization in Industry, Medicine, and Agriculture

Abstract

Antifreeze proteins (AFPs) are specific proteins, glycopeptides, and peptides made by different organisms to allow cells to survive in sub-zero conditions. AFPs function by reducing the water’s freezing point and avoiding ice crystals’ growth in the frozen stage. Their capability in modifying ice growth leads to the stabilization of ice crystals within a given temperature range and the inhibition of ice recrystallization that decreases the drip loss during thawing. This review presents the potential applications of AFPs from different sources and types. AFPs can be found in diverse sources such as fish, yeast, plants, bacteria, and insects. Various sources reveal different α-helices and β-sheets structures. Recently, analysis of AFPs has been conducted through bioinformatics tools to analyze their functions within proper time. AFPs can be used widely in various aspects of application and have significant industrial functions, encompassing the enhancement of foods’ freezing and liquefying properties, protection of frost plants, enhancement of ice cream’s texture, cryosurgery, and cryopreservation of cells and tissues. In conclusion, these applications and physical properties of AFPs can be further explored to meet other industrial players. Designing the peptide-based AFP can also be done to subsequently improve its function.

Antifreeze Proteins: A Tale of Evolution From Origin to Energy Applications

“…Antifreeze proteins are important antifreeze materials that have been widely used in the industry. The economic impact of using antifreeze proteins is significant, and therefore over the last decades, they have been studied extensively to optimize their large-scale production from various sources of organisms for improvement in various applications (Eskandari et al, 2020). Genetic engineering combined with large-scale culturing has succeeded in the production of commercial quantities of several proteins such as cold temperature active enzymes used in laundry detergents, diagnostic antibodies, and pharmaceutical proteins (Nomoto, 1993).…”

Psychrophilic Bacterial Phosphate-Biofertilizers: A Novel Extremophile for Sustainable Crop Production under Cold Environment

“…The cold-active enzymes, which are heat labile, preserve the proper movement of the active site even at temperatures at which the molecular motions of mesophilic and thermophilic counterparts are critically limited [67,68]. In addition, psychrophiles/psychrotrophs bacteria enduringly synthesize one set of ice-binding proteins (AFP) at low temperatures whose concentration increases with rising low temperatures [69,70]. The AFPs reduce the freezing point of water without altering its melting point and eluding the formation of ice crystals [69,71].…”

“…In addition, psychrophiles/psychrotrophs bacteria enduringly synthesize one set of ice-binding proteins (AFP) at low temperatures whose concentration increases with rising low temperatures [69,70]. The AFPs reduce the freezing point of water without altering its melting point and eluding the formation of ice crystals [69,71]. Conclusively, the AFPs and accumulation of other compatible solutes, for example, glycine betaine as produced by Bacillus subtilis, prohibit ice-crystallization and as an effective cold stress protectant, respectively, and therefore allow bacteria to grow normally at growth-inhibiting temperatures [12,13,62].…”

Biolocomotion and premelting in ice

“…Moreover, surface properties are central to the fact that extremophile organisms in Earth's cryosphere-glaciers, sea ice and permafrost-develop strategies to persist in challenging environments. Indeed, many biological organisms secrete exopolymeric substance (EPS) [17] or harness antifreeze glycoproteins (AFP) [18,19] to maintain interfacial liquidity. For example, sea ice houses an array of algae and bacteria, some of which produce EPS to protect them at low temperature and high salinity [20,21].…”