Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities
Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identif...
| Autores principales: | , , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
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Karger
2020
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12123/7513 https://www.karger.com/Article/Abstract/491698 https://doi.org/10.1159/000491698 |
| _version_ | 1855035872345325568 |
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| author | Navas, Laura Emilce Florin-Christensen, Mónica Benintende, Graciela Beatriz Zandomeni, Ruben Berretta, Marcelo Facundo |
| author_browse | Benintende, Graciela Beatriz Berretta, Marcelo Facundo Florin-Christensen, Mónica Navas, Laura Emilce Zandomeni, Ruben |
| author_facet | Navas, Laura Emilce Florin-Christensen, Mónica Benintende, Graciela Beatriz Zandomeni, Ruben Berretta, Marcelo Facundo |
| author_sort | Navas, Laura Emilce |
| collection | INTA Digital |
| description | Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55–80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes. |
| format | info:ar-repo/semantics/artículo |
| id | INTA7513 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2020 |
| publishDateRange | 2020 |
| publishDateSort | 2020 |
| publisher | Karger |
| publisherStr | Karger |
| record_format | dspace |
| spelling | INTA75132020-07-03T12:21:51Z Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities Navas, Laura Emilce Florin-Christensen, Mónica Benintende, Graciela Beatriz Zandomeni, Ruben Berretta, Marcelo Facundo Fosfolipase Enzimas Aciltransferasa Fosfolípidos Phospholipases Enzymes Acyltransferases Phospholipids Thermus Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55–80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes. Instituto de Microbiología y Zoología Agrícola Fil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Florin-Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina Fil: Zandomeni, Ruben. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 2020-07-03T12:08:14Z 2020-07-03T12:08:14Z 2018 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/7513 https://www.karger.com/Article/Abstract/491698 1464-1801 1660-2412 https://doi.org/10.1159/000491698 eng info:eu-repo/semantics/restrictedAccess application/pdf Karger Journal of Molecular Microbiology and Biotechnology 28 (3) : 99–106 (2018) |
| spellingShingle | Fosfolipase Enzimas Aciltransferasa Fosfolípidos Phospholipases Enzymes Acyltransferases Phospholipids Thermus Navas, Laura Emilce Florin-Christensen, Mónica Benintende, Graciela Beatriz Zandomeni, Ruben Berretta, Marcelo Facundo Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
| title | Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
| title_full | Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
| title_fullStr | Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
| title_full_unstemmed | Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
| title_short | Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
| title_sort | characterization of a novel thermostable enzyme from thermus sp 2 9 with phospholipase and acyltransferase activities |
| topic | Fosfolipase Enzimas Aciltransferasa Fosfolípidos Phospholipases Enzymes Acyltransferases Phospholipids Thermus |
| url | http://hdl.handle.net/20.500.12123/7513 https://www.karger.com/Article/Abstract/491698 https://doi.org/10.1159/000491698 |
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