Structural diversity of marine anti-freezing proteins, properties and potential applications: a review
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 mem...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
SpringerOpen
2022-01-01
|
| Series: | Bioresources and Bioprocessing |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s40643-022-00494-7 |
| _version_ | 1818954025354133504 |
|---|---|
| author | Soudabeh Ghalamara Sara Silva Carla Brazinha Manuela Pintado |
| author_facet | Soudabeh Ghalamara Sara Silva Carla Brazinha Manuela Pintado |
| author_sort | Soudabeh Ghalamara |
| collection | DOAJ |
| description | 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 |
| first_indexed | 2024-12-20T10:15:36Z |
| format | Article |
| id | doaj.art-f9f9bc09a58448428533fbdd96437c8c |
| institution | Directory Open Access Journal |
| issn | 2197-4365 |
| language | English |
| last_indexed | 2024-12-20T10:15:36Z |
| publishDate | 2022-01-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Bioresources and Bioprocessing |
| spelling | doaj.art-f9f9bc09a58448428533fbdd96437c8c2022-12-21T19:44:04ZengSpringerOpenBioresources and Bioprocessing2197-43652022-01-019112410.1186/s40643-022-00494-7Structural diversity of marine anti-freezing proteins, properties and potential applications: a reviewSoudabeh Ghalamara0Sara Silva1Carla Brazinha2Manuela Pintado3Universidade Católica Portuguesa, CBQF – Centro de Biotecnologia e Química Fina – Laboratório Associado, Escola Superior de BiotecnologiaUniversidade Católica Portuguesa, CBQF – Centro de Biotecnologia e Química Fina – Laboratório Associado, Escola Superior de BiotecnologiaLAQV/Requimte, Faculdade de Ciências E Tecnologia, Universidade Nova de LisboaUniversidade Católica Portuguesa, CBQF – Centro de Biotecnologia e Química Fina – Laboratório Associado, Escola Superior de BiotecnologiaAbstract 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 Abstracthttps://doi.org/10.1186/s40643-022-00494-7Marine antifreeze proteinsIce recrystallization inhibition (IRI)Thermal hysteresis (TH)FunctionPotential applications |
| spellingShingle | Soudabeh Ghalamara Sara Silva Carla Brazinha Manuela Pintado Structural diversity of marine anti-freezing proteins, properties and potential applications: a review Bioresources and Bioprocessing Marine antifreeze proteins Ice recrystallization inhibition (IRI) Thermal hysteresis (TH) Function Potential applications |
| title | Structural diversity of marine anti-freezing proteins, properties and potential applications: a review |
| title_full | Structural diversity of marine anti-freezing proteins, properties and potential applications: a review |
| title_fullStr | Structural diversity of marine anti-freezing proteins, properties and potential applications: a review |
| title_full_unstemmed | Structural diversity of marine anti-freezing proteins, properties and potential applications: a review |
| title_short | Structural diversity of marine anti-freezing proteins, properties and potential applications: a review |
| title_sort | structural diversity of marine anti freezing proteins properties and potential applications a review |
| topic | Marine antifreeze proteins Ice recrystallization inhibition (IRI) Thermal hysteresis (TH) Function Potential applications |
| url | https://doi.org/10.1186/s40643-022-00494-7 |
| work_keys_str_mv | AT soudabehghalamara structuraldiversityofmarineantifreezingproteinspropertiesandpotentialapplicationsareview AT sarasilva structuraldiversityofmarineantifreezingproteinspropertiesandpotentialapplicationsareview AT carlabrazinha structuraldiversityofmarineantifreezingproteinspropertiesandpotentialapplicationsareview AT manuelapintado structuraldiversityofmarineantifreezingproteinspropertiesandpotentialapplicationsareview |