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Title: Bacillus sp JR3 esterase LipJ: A new mesophilic enzyme showing traces of a thermophilic past
Author: Ribera, Judit
Estupiñán Romero, Mónica
Fuentes, Alba
Fillet, Amanda
Martínez Martínez, Josefina
Díaz Lucea, Pilar
Keywords: Lipases
Bacillus (Bacteria)
Issue Date: 25-Jul-2017
Publisher: Public Library of Science (PLoS)
Abstract: A search for extremophile enzymes from ancient volcanic soils in El Hierro Island (Canary Islands, Spain) allowed isolation of a microbial sporulated strain collection from which several enzymatic activities were tested. Isolates were obtained after sample cultivation under several conditions of nutrient contents and temperature. Among the bacterial isolates, supernatants from the strain designated JR3 displayed high esterase activity at temperatures ranging from 30 to 100 degrees C, suggesting the presence of at least a hyper-thermophilic extracellular lipase. Sequence alignment of known thermophilic lipases allowed design of degenerated consensus primers for amplification and cloning of the corresponding lipase, named LipJ. However, the cloned enzyme displayed maximum activity at 30 degrees C and pH 7, showing a different profile from that observed in supernatants of the parental strain. Sequence analysis of the cloned protein showed a pentapeptide motif-GHSMG-distinct from that of thermophilic lipases, and much closer to that of esterases. Nevertheless, the 3D structural model of LipJ displayed the same folding as that of thermophilic lipases, suggesting a common evolutionary origin. A phylogenetic study confirmed this possibility, positioning LipJ as a new member of the thermophilic family of bacterial lipases 1.5. However, LipJ clusters in a clade close but separated from that of Geobacillus sp. thermophilic lipases. Comprehensive analysis of the cloned enzyme suggests a common origin of LipJ and other bacterial thermophilic lipases, and highlights the most probable divergent evolutionary pathway followed by LipJ, which during the harsh past times would have probably been a thermophilic enzyme, having lost these properties when the environment changed to more benign conditions.
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It is part of: PLoS One, 2017, vol. 12, num. 7, p. e0181029
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ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Genètica, Microbiologia i Estadística)

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