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Journal of Microbiology and Biotechnology. 2025 Dec; 35(0): 8508904. doi: 10.4014/jmb.2504.04022

Cloning, Expression, and Characterization of GDSL-Type Lipolytic Enzyme Genes from Epidermidibacterium keratini EPI-7 Isolated from Human Skin

Seok-Yun Jeong , Seok Kyun Yun , Suhyeon Cho , Seyeol Baek , Hee-Jae Shin , Seokmuk Park , Sugyeong Jeong , Gayoung Kim , Seunghyun Kang , Seunghee Bae*
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  • Abstract



    This study investigated seven putative lipolytic enzymes (EstEk01-07) from the skin microbiome bacterium Epidermidibacterium keratini EPI-7, focusing on their properties relevant to industrial applications. Sequence analysis revealed conserved GDSL motifs and four conserved blocks, characteristic of the GDSL/SGNH superfamily, with predicted α/β/α folds consistent with these enzymes. Significant variations in the number of α-helices and β-sheets among the EstEk enzymes suggested diverse substrate specificities and catalytic efficiencies. The enzymes exhibited a strong preference for short-chain fatty acids (C2-C4), classifying them as carboxylesterases, a novel finding within the skin microbiome. Optimal enzyme activity was observed at alkaline pH (8.0-9.0) and thermophilic condition (50-60°C), with substantial thermostability retained after heating at 50°C for three hours. Metal ion analysis revealed a significant stimulatory effect of Ca2+ and Fe3+, while other transition metals were inhibitory. The enzymes were stable in a range of non-ionic detergents, but sensitive to SDS. Moreover, they exhibited notable tolerance to various organic solvents, particularly methanol and isopropanol, suggesting potential applications in cosmetics and pharmaceutical industries. This study identifies a novel library of thermostable, alkaline carboxylesterases from the skin microbiome, highlighting their potential for industrial biocatalysis and further investigation into their role in skin lipid metabolism.

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