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Biomolecules
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Article

Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (HaHSL) from Halocynthiibacter Arcticus

by
Ly Thi Huong Luu Le
1,
Wanki Yoo
1,2,
Changwoo Lee
3,4,
Ying Wang
1,
Sangeun Jeon
1,
Kyeong Kyu Kim
2,
Jun Hyuck Lee
3,4 and
T. Doohun Kim
1,*
1
Department of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Korea
2
Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea
3
Department of Polar Sciences, University of Science and Technology (UST), Incheon 21990, Korea
4
Unit of Research for Practical Application, Korea Polar Research Institute (KOPRI), Incheon 21990, Korea
*
Author to whom correspondence should be addressed.
Biomolecules 2019, 9(11), 704; https://doi.org/10.3390/biom9110704
Submission received: 14 October 2019 / Revised: 30 October 2019 / Accepted: 31 October 2019 / Published: 5 November 2019
(This article belongs to the Special Issue Biology, Biotechnology and Bioprospecting of Microbial Biomolecules)
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Abstract

Bacterial hormone-sensitive lipases (bHSLs), which are homologous to the catalytic domains of human HSLs, have received great interest due to their uses in the preparation of highly valuable biochemicals, such as drug intermediates or chiral building blocks. Here, a novel cold-active HSL from Halocynthiibacter arcticus (HaHSL) was examined and its enzymatic properties were investigated using several biochemical and biophysical methods. Interestingly, HaHSL acted on a large variety of substrates including tertiary alcohol esters and fish oils. Additionally, this enzyme was highly tolerant to high concentrations of salt, detergents, and glycerol. Furthermore, immobilized HaHSL retained its activity for up to six cycles of use. Homology modeling suggested that aromatic amino acids (Trp23, Tyr74, Phe78, Trp83, and Phe245) in close proximity to the substrate-binding pocket were important for enzyme activity. Mutational analysis revealed that Tyr74 played an important role in substrate specificity, thermostability, and enantioselectivity. In summary, the current study provides an invaluable insight into the novel cold-active HaHSL from H. arcticus, which can be efficiently and sustainably used in a wide range of biotechnological applications.
Keywords: hormone-sensitive lipase; substrate specificity; enantioselectivity; immobilization; Halocynthiibacter arcticus hormone-sensitive lipase; substrate specificity; enantioselectivity; immobilization; Halocynthiibacter arcticus

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MDPI and ACS Style

Le, L.T.H.L.; Yoo, W.; Lee, C.; Wang, Y.; Jeon, S.; Kim, K.K.; Lee, J.H.; Kim, T.D. Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (HaHSL) from Halocynthiibacter Arcticus. Biomolecules 2019, 9, 704. https://doi.org/10.3390/biom9110704

AMA Style

Le LTHL, Yoo W, Lee C, Wang Y, Jeon S, Kim KK, Lee JH, Kim TD. Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (HaHSL) from Halocynthiibacter Arcticus. Biomolecules. 2019; 9(11):704. https://doi.org/10.3390/biom9110704

Chicago/Turabian Style

Le, Ly Thi Huong Luu, Wanki Yoo, Changwoo Lee, Ying Wang, Sangeun Jeon, Kyeong Kyu Kim, Jun Hyuck Lee, and T. Doohun Kim. 2019. "Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (HaHSL) from Halocynthiibacter Arcticus" Biomolecules 9, no. 11: 704. https://doi.org/10.3390/biom9110704

APA Style

Le, L. T. H. L., Yoo, W., Lee, C., Wang, Y., Jeon, S., Kim, K. K., Lee, J. H., & Kim, T. D. (2019). Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (HaHSL) from Halocynthiibacter Arcticus. Biomolecules, 9(11), 704. https://doi.org/10.3390/biom9110704

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