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- W4207035862 abstract "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 Abstract" @default.
- W4207035862 created "2022-01-26" @default.
- W4207035862 creator A5028878670 @default.
- W4207035862 creator A5035142978 @default.
- W4207035862 creator A5039782232 @default.
- W4207035862 creator A5076670984 @default.
- W4207035862 date "2022-01-22" @default.
- W4207035862 modified "2023-10-01" @default.
- W4207035862 title "Structural diversity of marine anti-freezing proteins, properties and potential applications: a review" @default.
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