A University Student Made Waves... Pukyong National University Undergraduate's Paper Published in International Journal 'Marine Drugs'

4th Year Chemistry Student Lee Younghoon Studies Protein Freeze Resistance Using Ice-Binding Proteins from Polar Organisms

Lee Young-hoon, a senior in the Department of Chemistry at Pukyong National University.

[Asia Economy Yeongnam Reporting Headquarters Reporter Kim Yong-woo] An undergraduate student at Pukyong National University has created a remarkable impact by publishing a paper in an SCI-level international academic journal.

Lee Young-hoon (25), a senior in the Department of Chemistry at Pukyong National University (President Jang Young-soo), recently had his paper published in the international journal in the field of marine pharmaceuticals, Marine Drugs.

Lee Young-hoon published the paper titled “Protection of Alcohol Dehydrogenase against Freeze-thaw Stress by Ice-Binding Proteins is Proportional to their Ice-Recrystallization Inhibition Property” (supervised by Professor Kim Hak-jun) as the first author in this journal.

Marine Drugs is an SCI-level international journal with an impact factor (IF) of 4.073, published by the large Swiss publisher MDPI.

In this paper, Lee revealed research results on conferring freeze resistance to enzymes using ice-binding proteins.

Ice-binding proteins are proteins mainly found in organisms living in polar regions. They prevent the formation of ice crystals, thus providing resistance to freezing.

By using these proteins, various substances can be given freeze resistance, allowing the preservation of their properties even after multiple freeze-thaw cycles.

In this study, Lee repeatedly froze and thawed alcohol dehydrogenase along with two types of ice-binding proteins with different ice recrystallization inhibition properties, observing structural changes using the fluorescent substance ANS.

The results showed that ice-binding proteins with higher ice recrystallization inhibition properties exhibited smaller structural changes due to freezing and thawing, whereas the general protein ADH showed relatively larger structural changes.

He also identified the concentration of ice-binding proteins that practically preserve activity. By varying the concentrations of alcohol dehydrogenase and ice-binding proteins and measuring changes in the enzyme’s activity, it was found that using the ice-binding protein with high ice recrystallization inhibition property (LeIBP) at concentrations above 500 μg/ml had a significant effect.

Lee said, “Through this research, we were able to identify the types and concentrations of ice-binding proteins that can maximize the preservation of protein activity during freezing and thawing. We will conduct follow-up studies to apply these results to freezing preservation methods for other various proteins in pharmaceuticals and food.”

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