A thermophilic hormone-sensitive lipase family esterase Est1404 identified from an Antarctic bacterium Pseudomonas sp. E2-15

Yuanfang  He; Rui  Deng; Xiaoyu  Liu; Shu  Xing; Xiying  Zhang; Hailun  He; John Kevin  Bielicki; Mingyang Zhou

doi:10.33265/polar.v45.10747

Yuanfang He School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, PR China
Rui Deng School of Bioengineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, PR China
Xiaoyu Liu School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, PR China
Shu Xing School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, PR China;
Xiying Zhang State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao, PR China
Hailun He State Key Laboratory of Medical Genetics, School of Life Sciences, Central South University, Changsha, PR China
John Kevin Bielicki School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, PR China
Mingyang Zhou School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, PR China https://orcid.org/0000-0003-1624-3827

DOI: https://doi.org/10.33265/polar.v45.10747

Keywords: Antarctica, bacteria, enzyme, HSL family

Abstract

Esterases are a group of enzymes with a diverse range of uses in industry. We identified a novel hormone-sensitive lipase (HSL) in the esterase family, Est1404, through cloning and expression from the Antarctic bacterium Pseudomonas sp. E2–15, from soil collected on King George Island. Investigations showed that the Est1404 enzyme is a thermophilic esterase that maintains 90–100% activity throughout the temperature range of 60–90 °C. It exhibits the highest catalytic activity towards p-nitrophenol butyrate at 70 °C and pH 8.5. Est1404 was inhibited by the serine-modifying reagent phenylmethylsulfonyl fluoride, but thiol reagents such as dithiolthreitol stimulated its activity. Metal chelating chemicals, such as ethylenediaminetetraacetic acid, did not affect its activity. Phylogenetic analysis indicated that Est1404 is in the GDSAG subfamily of HSL. The enzyme contains a GDSAG motif with an active serine (S) positioned within a catalytic triad consisting of highly conserved Ser¹⁵⁶, Asp²⁵⁰ and His²⁸⁰ residues. The thermal stability of the Est1404 esterase makes it potentially useful in industrial catalysis.

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