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Phoenix666 [soylentnews.org] writes:

This week Dutch, American and Canadian researchers present a major step in understanding antifreeze proteins [phys.org], the proteins that hinder the growth of ice crystals. Artificial forms of these proteins are interesting for a whole range of applications – from de-icing spray and road salt to improved preservation of frozen food and organs. The team, led by TU/e researcher Ilja Voets, will publish its findings this week in the leading journal PNAS on how we need a different type of antifreeze protein than previously thought for most applications.
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Roughly speaking, antifreeze proteins work in two ways. On the one hand, they reduce the temperature whereby ice crystals begin to grow rapidly (the scientific term being 'thermal hysteresis', or TH). On the other hand, they combat so-call recrystallization, the process by which, in simple terms, small ice crystals cluster into larger chunks (scientific term: 'ice recrystallization inhibition', or IRI). However, the relationship between these two activities of antifreeze proteins has long been unclear.
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TU/e researcher Ilja Voets and her team of Dutch, American and Canadian researchers now reveal that there is no clear relationship between these activities and that there are also significant differences per protein. This also means that it is not so easy, as had long been thought, to determine how 'active' a protein is – an important consideration in its suitability in applications. "Sometimes the TH activity is important but more often than not it is the IRI activity that appears to be the determining factor," says Voets.

Anti-freeze proteins are considered for a variety of applications from de-icing aircraft wings to keeping roads ice-free to producing better-quality frozen food.

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