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The Survival Secrets of the Arctic Springtail
14/02/25, 13:48
Last updated:
21/09/24, 16:09
Published:
Antifreeze proteins and frozen foods
Introduction
Approximately 450 million years ago, during the Ordovician period, the Earth was characterised by a hot and humid globe. The sea was teeming with life, with early squids, eel-like fish, and sea worms hunting smaller animals. However, there was no sign of movement above ground as the animals had not yet crawled ashore. This period of warmth created ideal living conditions for wildlife, but it was about to change dramatically.
Shortly after, the land masses began to freeze, and an ice cap started to spread. The once warm and accommodating waters turned cold and inhospitable, leading to the second-worst mass extinction in the history of the planet. Many species succumbed to the harsh conditions, but one animal survived - the springtail.
The springtail, a small insect-like animal, had developed a special strategy to combat the cold. Its cells started producing proteins that could protect them from freezing. This discovery challenges the previous belief that animals did not develop antifreeze proteins until much later. Research from Aarhus University has shown that the springtail might have been the first animal to develop such proteins.
Applications in the Food Industry
Since then, scientists have found antifreeze proteins in various animals, plants, and microorganisms. These proteins have also found applications in different industries. One of the industries utilising antifreeze proteins is the food industry, especially in producing frozen foods.
Frozen foods often suffer from changes in taste and texture due to the formation of ice crystals. However, by incorporating antifreeze proteins, these undesirable effects can be prevented. Industrial yeast cell cultures have been engineered to produce antifreeze proteins derived from fish genes. These proteins can then be added to different foods, including ice cream, to improve texture and prevent the formation of ice crystals.
Exploring Arctic Fish
Aside from their contribution to the food industry, springtails have also fascinated scientists due to their ability to survive in extremely cold regions. The discovery of antifreeze proteins explained how arctic fish could swim in icy seawater. The proteins prevent ice from forming in the cells and blood of the fish, allowing them to survive in freezing conditions.
Martin Holmstrup, a researcher at Aarhus University, oversees colonies of springtails in his laboratory. These small animals require minimal space and can be easily maintained in Petri dishes with a base of moist plaster and a feed of dry yeast. Researchers have determined that springtails developed these proteins long before other animals by studying the DNA sequences responsible for building antifreeze proteins.
The discovery of antifreeze proteins in springtails opens up possibilities for various applications, including in the food industry. These proteins have been found to prevent ice crystal formation, which can affect the taste and texture of frozen foods. The genes responsible for their production have been copied into industrial yeast cell cultures to utilise these proteins. This allows the yeast to produce the antifreeze proteins, which can then be added to different foods. One example is the use of these proteins in ice cream, where they help create a delightful texture and allow the ice cream to be thawed and refrozen without compromising its quality.
Conclusion
The discovery of antifreeze proteins in springtails has revolutionised various industries, particularly the food industry. These proteins have been found to prevent ice crystal formation, improving the taste and texture of frozen foods. Incorporating antifreeze proteins derived from fish genes into yeast cell cultures can produce and add these proteins to different foods, such as ice cream, ensuring a delightful texture and the ability to thaw and refreeze without compromising quality. This remarkable adaptation of springtails has provided insight into their survival in extremely cold regions and opened up possibilities for further applications of antifreeze proteins in various fields.
Written by Sara Maria Majernikova
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

