ArticleMarine biotechnology (New York, N.Y.)2014
Isolation and characterization of antifreeze proteins from the antarctic marine microalga Pyramimonas gelidicola.
Article in Marine biotechnology (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 30 citations in OpenAlex.
- Extremophilic Microalgae and Cyanobacteria as Platforms for Climate Resilience, Circular Resource Utilization and Bioprospecting.Microorganisms · 2026Review
- The Safety and Efficacy of 1-Monoeicosapentaenoin Isolated from the TrebouxiophyceaeJournal of clinical medicine · 2023Article
- Structural diversity of marine anti-freezing proteins, properties and potential applications: a review.Bioresources and bioprocessing · 2022Review
- Prediction and analysis of antifreeze proteins.Heliyon · 2021Article
- Co-production of biodiesel and bioethanol using psychrophilic microalgaBiotechnology for biofuels · 2020Article
- Review
- Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant.Marine drugs · 2017Review
- Physiological adaptations of yeasts living in cold environments and their potential applications.World journal of microbiology & biotechnology · 2015Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antifreeze proteins (AFPs) play an important role in the psychrophilic adaptation of polar organisms. AFPs encoded by an Antarctic chlorophyte, identified as Pyramimonas gelidicola, were isolated and characterized. Two AFP isoforms were found from cDNAs and their deduced molecular weights were estimated to be 26.4 kDa (Pg-1-AFP) and 27.1 kDa (Pg-2-AFP). Both AFP cDNAs were cloned and expressed in Escherichia coli. The purified recombinant Pg-1-rAFP and Pg-2-rAFP both showed antifreeze activity based on the measurement of thermal hysteresis (TH) and morphological changes to single ice crystals. Pg-1-rAFP shaped ice crystals into a snowflake pattern with a TH value of 0.6 ± 0.02 °C at ~15 mg/ml. Single ice crystals in Pg-2-rAFP showed a dendritic morphology with a TH value of 0.25 ± 0.02 °C at the same protein concentration. Based on in silico protein structure predictions, the three-dimensional structures of P. gelidicola AFPs match those of their homologs found in fungi and bacteria. They fold as a right-handed β-helix flanked by an α-helix. Unlike the hyperactive insect AFPs, the proposed ice-binding site on one of the flat β-helical surfaces is neither regular nor well-conserved. This might be a characteristic of AFPs used for freeze tolerance as opposed to freeze avoidance. A role for P. gelidicola AFPs in freeze tolerance is also consistent with their relatively low TH values.
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