Scientists are aware that antifreeze proteins (AFPs) reduce the freezing point of bodily fluids and prevent ice recrystallisation. An adsorption-inhibition mechanism is believed to be responsible; however, the precise details are not yet fully understood. The EU-funded PRICE (Why and how do antifreeze proteins bind ice? An experimental study on the solution and adsorption behaviour of antifreeze proteins) initiative aimed to identify how AFPs work. The researchers would gain a better understanding of this mystery through a series of protein biosynthesis experiments. PRICE used Escherichia coli bacteria to make and study type I and type III AFPs in the laboratory. The researchers used X-ray scattering to study hyperactive type I AFPs in winter flounder. The research group also investigated the use of 2D infrared spectroscopy to work out the structure of fish type III AFPs. Results from the PRICE project regarding the natural cryoprotective ability of AFPs have important applications in the wider world. Real-world applications would include the preservation of organs and food products during freezing.
Antifreeze proteins, polar fish, freezing, adsorption, cryoprotective