Ice recrystallization is strongly inhibited when antifreeze proteins bind to multiple ice planes.

ABSTRACT: Ice recrystallization is a phenomenon observed as the increase in ice crystal size within an already frozen material. Antifreeze proteins (AFPs), a class of proteins capable of arresting ice crystal growth, are known to inhibit this phenomenon even at sub milli-molar concentrations. A tremendous range in the possible applications of AFPs is hence expected in both medical and industrial fields, while a key determinant of the ice recrystallization inhibition (IRI) is hardly understood. Here, IRI efficiency and ice plane affinity were examined for the wild-type AFPI-III, a defective AFPIII isoform, and a fungal AFP isoform. To simplify the IRI analysis using the formal representation of Ostwald-ripening (r³ = r₀³ + kt), we monitored specific ice grains exhibit

SUBMITTER: Rahman AT 

PROVIDER: S-EPMC6374469 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature