Preprint Article Version 1 This version is not peer-reviewed

Falling Water Ice Purification of Ice-Binding Proteins

Version 1 : Received: 15 January 2018 / Approved: 16 January 2018 / Online: 16 January 2018 (07:56:40 CET)

How to cite: Adar, C.; Sirotinskaya, V.; Bar Dolev, M.; Friehmann, T.; Braslavsky, I. Falling Water Ice Purification of Ice-Binding Proteins. Preprints 2018, 2018010137 (doi: 10.20944/preprints201801.0137.v1). Adar, C.; Sirotinskaya, V.; Bar Dolev, M.; Friehmann, T.; Braslavsky, I. Falling Water Ice Purification of Ice-Binding Proteins. Preprints 2018, 2018010137 (doi: 10.20944/preprints201801.0137.v1).

Abstract

Ice-binding proteins (IBPs) have several functions that permit their hosts to thrive in the presence of ice. The ability of IBPs to control ice growth makes them potential additives in various industries ranging from food storage and cryopreservation to anti-icing systems. For IBPs to be used in commercial applications, however, methods are needed to produce sufficient quantities of high-quality proteins. Here, we describe a new method for IBP purification, termed falling water ice purification (FWIP). The method is based on the affinity of IBPs for ice. A crude IBP solution is allowed to flow continuously over the large chilled vertical surface of a commercial ice machine. The temperature of the surface is lowered gradually until ice crystals are produced, to which the IBPs bind but other solutes do not. As in other ice affinity methods, FWIP does not require molecular tags and is suitable for purifying recombinant IBPs as well as IBPs from natural sources. The advantage of FWIP over other ice affinity methods is that it exploits an ice machine designed to produce large volumes of clear ice daily. This system can be easily scaled up and suits the purification of industrial quantities of IBPs. The FWIP method significantly advances the use of IBPs in research and industry.

Subject Areas

ice-binding proteins; antifreeze proteins, cold finger, ice affinity purification.

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