FREEZECONTROL BY IBP

Freeze Control in Food by Ice Binding Proteins

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 Obiettivo del progetto (Objective)

'The freezing processes play a main role in food science. The storage of food in a frozen form has become one of the most common ways to elongate the shelf-time of many food products. Nevertheless, during freezing and thawing, cell walls can be ruptured by the ice crystals or can be separated by extra-cellular ice growth during the recrystalization process. Ice binding proteins (IBP), which include antifreeze proteins, ice nucleating proteins, and recrystalization inhibitors, hold great promise for improvements in food supply and quality through the prevention of frost damage to crops and the enhancement of preservation technology. The interaction of IBPs with ice crystals suggests that these proteins can be use as a means of controlling ice in food in each level of its production and processing. I propose to investigate freeze control in food by ice binding proteins. My background includes a PhD in ice physics and in particular optical investigation of crystal growth, a post-doctorate work in biophysics and biotechnology and academic position in Ohio University in where I investigate IBPs. In my post-doctorate work at Caltech, I developed instrumentation that was the basis for the biotechnology company Helicos Bioscience, which led to the development of the first instrumentation that can sequence DNA at the single molecule level. In the past few years at Ohio University, I have combined the subjects of ice physics and biophysics and have developed methods for investigating antifreeze proteins in novel ways. I have developed unique instrumentation to assess the activity of the proteins, in particular microfluidics and fluorescence microscopy. At the Hebrew University Faculty of Agriculture, Food and Environment I intend to establish a Food Biophysics lab in which I will continue my basic research on the mechanism of freeze control and investigate the potential of IBPs to improve the quality of different food materials upon cooling, freezing and thawing.'

Introduzione (Teaser)

An EU-funded project has harnessed an antifreeze protein (AFP) to prevent ice damage caused by freezing, which increases the shelf-life of food.

Descrizione progetto (Article)

Advancements in frozen storage methods have significantly extended food shelf-life and increased supermarket access to global imports. Unfortunately though, the freezing and thawing process can create ice crystals that rupture cell walls, thus damaging products.

The aim of the 'Freeze control in food by ice binding proteins' (FREEZECONTROL BY IBP) project was to find out if such damage could be prevented using AFPs. The project advanced cryopreservation technologies that make use of AFPs to inhibit the growth of cell-damaging ice crystals, a mechanism known to help organisms survive sub-zero temperatures.

Researchers designed two new technologies for measuring AFP activity. The first is a custom-made computer-controlled cold microscope stage system; the second is a microfluidic device allowing temperature control of ice crystals in a microscopic environment.

They found that a specific class of AFP had a greater effect on ice recrystallisation and ice shaping, and that preventing these two processes could improve cryopreservation. The project also successfully up-scaled the production of large numbers of AFPs, which is necessary for cryopreservation research.

Overall, this research reveals the potential of ice-binding proteins, such as AFPs, to improve the quality of frozen food. Their application would improve cold chain management, decrease food wastage, and minimise the health risks associated with importing and exporting frozen products.