Skip to main content
Log in

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

  • Original Paper
  • Published:
Molecular Biotechnology Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  1. Natsch, A., Derrer, S., Flachsmann, F., & Schmid, J. (2006). A broad diversity of volatile carboxylic acids, released by a bacterial aminoacylase from axilla secretions, as candidate molecules for the determination of human-body odor type. Chemistry & Biodiversity,3, 1–20.

    Article  CAS  Google Scholar 

  2. Lenochova, P., Roberts, S. C., & Havlicek, J. (2009). Methods of human body odor sampling: The effect of freezing. Chemical Senses,34, 127–138.

    Article  Google Scholar 

  3. Haze, S., Gozu, Y., Nakamura, S., Kohno, Y., Sawano, K., Ohta, H., et al. (2001). 2-Nonenal newly found in human body odor tends to increase with aging. Journal of Investigative Dermatology,116, 520–524.

    Article  CAS  Google Scholar 

  4. Ishino, C., Wakita, T., Shibata, S., Toyokuni, S., Machida, S., Matsuda, T., et al. (2010). Lipid peroxidation generates body odor component trans-2-nonenal covalently bound to protein in vivo. Journal of Biological Chemistry,285, 15302–15313.

    Article  CAS  Google Scholar 

  5. de Duve, C. (1963). The lysosome concept, Ciba Foundation Symposium—Anterior Pituitary Secretion. Book I of Colloquia on Endocrinology, 1–35.

  6. Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000). Rab7: A key to lysosome biogenesis. Molecular Biology of the Cell,11, 467–480.

    Article  CAS  Google Scholar 

  7. Saftig, P., & Klumperman, J. (2009). Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function. Nature Reviews Molecular Cell Biology,10, 623–635.

    Article  CAS  Google Scholar 

  8. Dunn, W. A. (1994). Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends in Cell Biology,4, 139–143.

    Article  CAS  Google Scholar 

  9. Zhang, Y., Li, Y., Du, C., Liu, M., & Cao, Z. A. (2006). Inactivation of aldehyde dehydrogenase: A key factor for engineering 1, 3-propanediol production by Klebsiella pneumoniae. Metabolic Engineering,8, 578–586.

    Article  CAS  Google Scholar 

  10. Holmes, R. S. (1978). Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: Localization of Ahd-1 encoding the mitochondrial isozyme on chromosome 4. Biochemical Genetics,16, 1207–1218.

    Article  CAS  Google Scholar 

  11. Smith, H. E., & Lindahl, R. (1980). Peroxisome-associated aldehyde dehydrogenase in normal rat liver. Pharmacology Biochemistry and Behavior,13, 111–118.

    Article  CAS  Google Scholar 

  12. Bicknell, L. S., Farrington-Rock, C., Shafeghati, Y., Rump, P., Alanay, Y., Alembik, Y., et al. (2007). A molecular and clinical study of larsen syndrome caused by mutations in FLNB. Journal of Medical Genetics,44, 89–98.

    Article  CAS  Google Scholar 

  13. Xu, B., Gao, Y., Zhan, S., & Ge, W. (2017). Quantitative proteomic profiling for clarification of the crucial roles of lysosomes in microbial infections. Molecular Immunology,87, 122–131.

    Article  CAS  Google Scholar 

  14. Nguyen, N. T., Kim, Y. H., Bang, S. H., Hong, J. H., Kwon, S. D., & Min, J. (2014). Toxic detection in mine water based on proteomic analysis of lysosomal enzymes in Saccharomyces cerevisiae. Environmental Health and Toxicology. https://doi.org/10.5620/eht.e2014019.

    Article  PubMed  PubMed Central  Google Scholar 

  15. Yoon, J., Kim, K. J., Choi, Y. W., Shin, H. S., Kim, Y. H., & Min, J. (2010). The dependence of enhanced lysosomal activity on the cellular aging of bovine aortic endothelial cells. Molecular and Cellular Biochemistry,340, 175–178.

    Article  CAS  Google Scholar 

  16. Yamazaki, S., Hoshino, K., & Kusuhara, M. (2010). Odor associated with aging. Anti-Aging Medicine,7, 60–65.

    Article  Google Scholar 

  17. Graham, J. M. (2000). Isolation of peroxisomes from tissues and cells by differential and density gradient centrifugation. Current Protocols in Cell Biology,6, 3–5.

    Google Scholar 

Download references

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).

Author information

Authors and Affiliations

Authors

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.

Ethics declarations

Conflict of interest

All authors declare that they have no conflict of interest.

Research Involving Human Participants and/or Animals

This article does not contain any studies with human participants or animals performed by any of the authors.

Informed Consent

Informed consent was obtained from all individual participants included in the study.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

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

Download citation

  • Accepted:

  • Published:

  • Issue Date:

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

Keywords

Navigation