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

Soudabeh Ghalamara, Sara Silva, Carla Brazinha, Manuela Pintado

Research output: Contribution to journalReview articlepeer-review

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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 Abstract: [Figure not available: see fulltext.].

Original languageEnglish
Article number5
JournalBioresources and Bioprocessing
Volume9
Issue number1
DOIs
Publication statusPublished - Dec 2022

Keywords

  • Function
  • Ice recrystallization inhibition (IRI)
  • Marine antifreeze proteins
  • Potential applications
  • Thermal hysteresis (TH)

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