Structural diversity of marine anti-freezing proteins, properties and potential applications: a review

Soudabeh Ghalamara,Manuela Pintado,Sara Silva,Carla Brazinha

doi:10.1186/s40643-022-00494-7

Soudabeh Ghalamara, Manuela Pintado + Show 2 more

Open Access

https://doi.org/10.1186/s40643-022-00494-7

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Abstract

Cold-adapted organisms, such as fishes, insects, plants and bacteria produce a group of proteins known as antifreeze proteins (AFPs). The specific functions of AFPs, including thermal hysteresis (TH), ice recrystallization inhibition (IRI), dynamic ice shaping (DIS) and interaction with membranes, attracted significant interest for their incorporation into commercial products. AFPs represent their effects by lowering the water freezing point as well as preventing the growth of ice crystals and recrystallization during frozen storage. The potential of AFPs to modify ice growth results in ice crystal stabilizing over a defined temperature range and inhibiting ice recrystallization, which could minimize drip loss during thawing, improve the quality and increase the shelf-life of frozen products. Most cryopreservation studies using marine-derived AFPs have shown that the addition of AFPs can increase post-thaw viability. Nevertheless, the reduced availability of bulk proteins and the need of biotechnological techniques for industrial production, limit the possible usage in foods. Despite all these drawbacks, relatively small concentrations are enough to show activity, which suggests AFPs as potential food additives in the future. The present work aims to review the results of numerous investigations on marine-derived AFPs and discuss their structure, function, physicochemical properties, purification and potential applications.Graphical

Highlights

Cold habitats are crucial to the planet with temperatures of about 85% of the earth being below 5 °C (Hassan et al 2016)
The ice binding site (IBS) of ColAFP lacks the repeated sequences found in hyperactive anti-freezing proteins/peptides (AFPs). These findings show that ColAFP exhibits antifreeze activity via a compound IBS distinct from the IBSs shared by other hyperactive AFPs
Over the past 50 years, studies have revealed on a number of specific AFPs that seemed to have diverse structures and functions

Summary

Graphical Abstract

Introduction Cold habitats are crucial to the planet with temperatures of about 85% of the earth being (permanent or seasonal) below 5 °C (from the deep sea to the alpine and the Antarctic to the Arctic) (Hassan et al 2016). AFP from winter flounder can inhibit crystallization in ice when enough amount of liquid is present and the system contains salts and the temperature is not so low In this case, the AFP binds to the ice surface at the ice solution interfaces in grain boundaries, avoiding migration of the solution and effectively immobilizing the boundaries, since the concentration of salt required to induce recrystallization inhibition effects; AFPs could play a role in the survival of organisms by preventing damages due to recrystallization. Winter flounder AFP has the power to block ice crystallization when there is enough liquid, and the device contains salts, so the temperature is not so low In this case, the AFP links to the ice surface at the ice fluid interfaces in grain boundaries, avoiding migration of the solution and effectively inactivating the boundaries, because the salt concentration needed to cause recrystallization inhibition effects; AFPs might play a role in organism survival by preventing recrystallization loss (Knight et al 1995). 0.53 (50 μM) 0.2 (0.04 mM) 0.32 (140 μM) 2 (180 μM) 0.35 (370 μM) 0.80 (40 μM) 3.8 (0.14 mM) 2.5 (50 μM) 0.08 (200 μM) 0.56 (150 μM) 3.20 (1.6 mM) 0.90 (350 μM)

I III AFGP III AFGP

III I II III AFGP

Findings

Conclusions