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Title: Investigations into the ice crystallization and freezing properties of the antifreeze protein ApAFP752
Authors: Asenath-Smith, Emily.
Jeng, Emily C.
Ambrogi, Emma K.
Hoch, Garrett R.
Olivier, Jason L.
Keywords: Antifreeze protein
Ice materials
Ice mechanics
Ice prevention and control
Ice recrystallization
Surface chemistry
Publisher: Engineer Research and Development Center (U.S.)
Series/Report no.: Technical Report (Engineer Research and Development Center (U.S.)) ; no. ERDC/CRREL TR-22-17
Abstract: Antifreeze proteins (AFPs) allow biological organisms, including insects, fish, and plants, to survive in freezing temperatures. While in solution, AFPs impart cryoprotection by creating a thermal hysteresis (TH), imparting ice recrystallization inhibition (IRI), and providing dynamic ice shaping (DIS). To leverage these ice-modulating effects of AFPs in other scenarios, a range of icing assays were performed with AFPs to investigate how AFPs interact with ice formation when tethered to a surface. In this work, we studied ApAFP752, an AFP from the beetle Anatolica polita, and first investigated whether removing the fusion protein attached during protein expression would result in a difference in freezing behavior. We performed optical microscopy to examine ice-crystal shape, micro-structure, and the recrystallization behavior of frozen droplets of AFP solutions. We developed a surface chemistry approach to tether these proteins to glass surfaces and conducted droplet-freezing experiments to probe the interactions of these proteins with ice formed on those surfaces. In solution, ApAFP752 did not show any DIS or TH, but it did show IRI capabilities. In surface studies, the freezing of AFP droplets on clean glass surfaces showed no dependence on concentration, and the results from freezing water droplets on AFP-decorated surfaces were inconclusive.
Description: Technical Report
Gov't Doc #: ERDC/CRREL TR-22-17
Rights: Approved for Public Release; Distribution is Unlimited
Size: 42 pages / 5.16 MB
Types of Materials: PDF
Appears in Collections:Technical Report

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