ArticleExtremophiles : life under extreme conditions2013
Characterization of Afp1, an antifreeze protein from the psychrophilic yeast Glaciozyma antarctica PI12.
Article in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 76 citations in OpenAlex.
- Crystal structure of a cold-active arginase from Glaciozyma antarctica.Acta crystallographica. Section F, Structural biology communications · 2026Article
- An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- The genome of the polyextremophilic yeast, Naganishia friedmannii, reveals adaptations involved in stress response pathways, carbohydrate metabolism expansion, and a limited DNA repair repertoire.FEMS yeast research · 2025Article
- Antifreeze proteins produced by Antarctic yeast from the genus Glaciozyma as cryoprotectants in food storage.PloS one · 2025Article
- Freezing and thawing in Antarctica: characterization of antifreeze protein (AFP) producing microorganisms isolated from King George Island, Antarctica.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Biochemical and in silico structural characterization of a cold-active arginase from the psychrophilic yeast, Glaciozyma antarctica PI12.Extremophiles : life under extreme conditions · 2024Article
- Comparative genome analysis of the freshwater fungus Filosporella fistucella indicates potential for plant-litter degradation at cold temperatures.G3 (Bethesda, Md.) · 2023Article
- High-quality genome of the basidiomycete yeast Dioszegia hungarica PDD-24b-2 isolated from cloud water.G3 (Bethesda, Md.) · 2022Article
- The Effects of Different Doses of ROCK Inhibitor, Antifreeze Protein III, and Boron Added to Semen Extender on Semen Freezeability of Ankara Bucks.Molecules (Basel, Switzerland) · 2022Article
- Structural diversity of marine anti-freezing proteins, properties and potential applications: a review.Bioresources and bioprocessing · 2022Review
- A genomic approach to analyze the cold adaptation of yeasts isolated from Italian Alps.Frontiers in microbiology · 2022Article
- Characterization of Inducible HSP70 Genes in an Antarctic Yeast,Microorganisms · 2021Article
- Prediction and analysis of antifreeze proteins.Heliyon · 2021Article
- Basidiomycetous Yeast,Microorganisms · 2021Article
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Stress-induced expression is enriched for evolutionarily young genes in diverse budding yeasts.Nature communications · 2020Article
- Ice Binding Proteins: Diverse Biological Roles and Applications in Different Types of Industry.Biomolecules · 2020Review
- Review
- Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica.Cell stress & chaperones · 2019Article
- Computational discovery and annotation of conserved small open reading frames in fungal genomes.BMC bioinformatics · 2019Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The psychrophilic yeast Glaciozyma antarctica demonstrated high antifreeze activity in its culture filtrate. The culture filtrate exhibited both thermal hysteresis (TH) and ice recrystallization inhibition (RI) properties. The TH of 0.1 °C was comparable to that previously reported for bacteria and fungi. A genome sequence survey of the G. antarctica genome identified a novel antifreeze protein gene. The cDNA encoded a 177 amino acid protein with 30 % similarity to a fungal antifreeze protein from Typhula ishikariensis. The expression levels of AFP1 were quantified via real time-quantitative polymerase chain reaction (RT-qPCR), and the highest expression levels were detected within 6 h of growth at -12 °C. The cDNA of the antifreeze protein was cloned into an Escherichia coli expression system. Expression of recombinant Afp1 in E. coli resulted in the formation of inclusion bodies that were subsequently denatured by treatment with urea and allowed to refold in vitro. Activity assays of the recombinant Afp1 confirmed the antifreeze protein properties with a high TH value of 0.08 °C.
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