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Removal of Trans-2-nonenal Using Hen Egg White Lysosomal-Related Enzymes

Molecular Biotechnology volume 62, pages 380–386 (2020)Cite this article

Abstract

2-Nonenal is a long-chain aliphatic aldehyde containing nine carbons and an unsaturated bond. 2-Nonenal is the primary cause of odor associated with aging, with an unpleasant greasy and grassy odor. Lysosome, mitochondria, and peroxisome are significant organelles in eukaryotic cells that contain various hydrolases that degrade biomolecules. Proteins in mitochondria and peroxisome also contain aldehyde dehydrogenase. We performed trans-2-nonenal treatment using lysosomal-related enzymes extracted from hen egg white (HEW). As trans-2-nonenal is more structurally stable than cis-2-nonenal, it was selected as the target aldehyde. HEW contains various biologically active proteins and materials such as albumin, ovotransferrin, lysosome, peroxisome, and mitochondria. Here, complementary experiments were conducted to evaluate the role of lysosomal-related enzymes in the treatment of trans-2-nonenal. The activity of lysosomal-related enzymes was confirmed via antimicrobial test against E. coli. HPLC analysis was used to determine the reduction of trans-2-nonenal. The trans-2-nonenal treatment depended on the reaction time and enzyme concentration. Materials considered as an intermediate from trans-2-nonenal treatment were detected by GC/MS spectrometer. Under acidic conditions (pH 6), lysosomal-related enzymes were the most efficient in the treatment of trans-2-nonenal. Furthermore, based on differential pH testing, we found the conditions under which all the 50 ppm trans-2-nonenal was removed. Therefore, our results suggest that the lysosomal-related enzymes reduced trans-2-nonenal, suggesting clinical application as anti-aging deodorants.

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Acknowledgements

This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT & Future Planning (2017R1A2B4009775).

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Author notes

  1. Seyoung Lee, Ji Hun Kim and Ngoc-Tu Nguyen have contributed equally to this work.

Authors and Affiliations

  1. Graduate School of Semiconductor and Chemical Engineering, Jeonbuk National University, 567 Baekje-daero, deokjin-gu, Jeonju-si, Jeollabuk-do, 54896, Republic of Korea

    Seyoung Lee, Ngoc-Tu Nguyen, Ra-Mi Park, Su-Min Lee, Seung Hyuck Bang, Gyeongchan Jeon, Jaewoong Lee & Jiho Min

  2. Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Yuseong-gu, Daejeon, 34141, South Korea

    Ji Hun Kim, Sunchang Kim & Byung-Kwan Cho

  3. School of Biological Science, Chungbuk National University, Chungdae-ro 1, Seowon-Gu, Cheongju, Chungbuk, 28644, Republic of Korea

    Yang-Hoon Kim

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  1. Seyoung Lee
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Contributions

SL, NTN, R-MP, SHB, JL, GJ, Y-HK and JM designed the experiments and analyzed the results. SYK analyzed the experimental data, J-HW conducted the HPLC analysis. All authors contributed to writing of the manuscript.

Corresponding authors

Correspondence to Byung-Kwan Cho, Yang-Hoon Kim or Jiho Min.

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Lee, S., Kim, J.H., Nguyen, NT. et al. Removal of Trans-2-nonenal Using Hen Egg White Lysosomal-Related Enzymes. Mol Biotechnol 62, 380–386 (2020). https://doi.org/10.1007/s12033-020-00256-w

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  • DOI: https://doi.org/10.1007/s12033-020-00256-w

Keywords

  • 2-Nonenal
  • Long-chain aliphatic aldehyde
  • Hen’s egg white lysosomes
  • Lysosomal-related enzymes