Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins

L.L.C. Olijve, K. Meister, A.L. DeVries, J.G. Duman, S. Guo, H.J. Bakker, I.K. Voets

Research output: Contribution to journalArticleAcademicpeer-review

90 Citations (Scopus)
173 Downloads (Pure)


Antifreeze proteins (AFPs) are a unique class of proteins that bind to growing ice crystal surfaces and arrest further ice growth. AFPs have gained a large interest for their use in antifreeze formulations for water-based materials, such as foods, waterborne paints, and organ transplants. Instead of commonly used colligative antifreezes such as salts and alcohols, the advantage of using AFPs as an additive is that they do not alter the physicochemical properties of the water-based material. Here, we report the first comprehensive evaluation of thermal hysteresis (TH) and ice recrystallization inhibition (IRI) activity of all major classes of AFPs using cryoscopy, sonocrystallization, and recrystallization assays. The results show that TH activities determined by cryoscopy and sonocrystallization differ markedly, and that TH and IRI activities are not correlated. The absence of a distinct correlation in antifreeze activity points to a mechanistic difference in ice growth inhibition by the different classes of AFPs: blocking fast ice growth requires rapid nonbasal plane adsorption, whereas basal plane adsorption is only relevant at long annealing times and at small undercooling. These findings clearly demonstrate that biomimetic analogs of antifreeze (glyco)proteins should be tailored to the specific requirements of the targeted application.

Original languageEnglish
Pages (from-to)3740-3745
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America (PNAS)
Issue number14
Publication statusPublished - 5 Apr 2016


  • Antifreeze protein
  • Ice recrystallization inhibition
  • Thermal hysteresis


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