Ice binding proteins (IBP), also known as antifreeze proteins and ice structuring proteins interfere with or modify ice crystal growth. These proteins have evolved in several organisms living in climates that include low temperatures and have potentially important in a host of health, geophysical, environmental, and industrial contexts. The interaction of IBPs with ice crystals suggests that these proteins can be used as a means for controlling ice in food during each stage of production and processing. It was found that IBPs can change the morphology of ice growth that influences the stability and structure of frozen desserts significantly. This include the inhibition of ice recrystallization, and structuring of ice crystals into bipyramidal shapes. IBPs change the growth habits of ice by binding to ice surfaces. Still many aspects of their operation remain unknown. Answering questions regarding the basic operation of the interaction of these special proteins with ice will assist in the investigation and development of procedures that will allow for better preservation of food materials and might control the final food texture. We investigate IBP by several means. Fluorescently labeled IBPs in combination with fluorescence microscopy and microfluidic devices were used in order to detect the binding planes of different IBPs to ice surfaces and the kinetics of ice protein interaction1. These methods allow for comparison of the interactions of different type of IBPs with ice crystals and to gain better understanding of their ice modification activity2. Controlling ice growth with these natural materials will enable for improved chilled and frozen food preservation by increasing the food materials stability and reduce their freezing damage.
Supported by NSF, ISF and ERC.
Principal Investigator: Dr. Ido Braslavsky Ido.braslavsky@mail.huji.ac.il
References:
1) "Microfluidic experiments reveal that antifreeze proteins bound to ice crystals suffice to prevent their growth", Celik, et.al, PNAS, 2013,110:1309-1314.
2) "New Insights into Ice Growth and Melting Modifications by Antifreeze Proteins", Bar-Dolev, et.al, J. Royal Society Interface, 2012, 9:3249-59.
