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Abstract
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 [ver mas...]
dc.contributor.authorNavas, Laura Emilce
dc.contributor.authorFlorin-Christensen, Mónica
dc.contributor.authorBenintende, Graciela Beatriz
dc.contributor.authorZandomeni, Ruben
dc.contributor.authorBerretta, Marcelo Facundo
dc.date.accessioned2020-07-03T12:08:14Z
dc.date.available2020-07-03T12:08:14Z
dc.date.issued2018
dc.identifier.issn1464-1801
dc.identifier.issn1660-2412
dc.identifier.otherhttps://doi.org/10.1159/000491698
dc.identifier.urihttp://hdl.handle.net/20.500.12123/7513
dc.identifier.urihttps://www.karger.com/Article/Abstract/491698
dc.description.abstractPhospholipases 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.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherKargeres_AR
dc.rightsinfo:eu-repo/semantics/restrictedAccesses_AR
dc.sourceJournal of Molecular Microbiology and Biotechnology 28 (3) : 99–106 (2018)es_AR
dc.subjectFosfolipasees_AR
dc.subjectPhospholipaseseng
dc.subjectEnzimases_AR
dc.subjectEnzymeseng
dc.subjectAciltransferasaes_AR
dc.subjectAcyltransferaseseng
dc.subjectFosfolípidoses_AR
dc.subjectPhospholipidseng
dc.subject.otherThermuses_AR
dc.titleCharacterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activitieses_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Microbiología y Zoología Agrícolaes_AR
dc.description.filFil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Florin-Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentinaes_AR
dc.description.filFil: Zandomeni, Ruben. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.subtypecientifico


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