Análise in silico de uma pirofosfatase e de uma tiosterase de uma biblioteca metagenômica de solo de Eucalipto spp
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Data
2014-05-06
Autores
Rodrigues, Gisele Regina [UNESP]
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Universidade Estadual Paulista (Unesp)
Resumo
Os microrganismos apresentam uma imensa diversidade genética e desempenham funções únicas e cruciais na manutenção dos ecossistemas, uma dessas funções é a produção de enzimas extracelulares que ajudam na mineralização da matéria orgânica, liberação de carbono e nutrientes na forma de serem assimilados. Devido a esses importantes fatores cada vez mais aumenta a busca por enzimas que possam ser utilizadas nos diversos setores industriais a fim de diminuir o impacto ambiental e obter maior eficiência e menor custo durante os processos de catalise. Mas esse potencial biocatalítico ainda é pouco explorado. As hidrolases pertencem ao grupo de maior interesse para o mercado de enzimas sendo amplamente utilizadas em processos industriais tais como, a aplicação de aditivos em alimentos para animais, têxteis, para a produção de biodiesel e biossíntese de novos antibióticos. Nesse sentido, o objetivo do trabalho foi o de encontrar novas enzimas hidrolíticas. Para isso, foi utilizada biblioteca metagenômica de solo sob Eucalyptus spp. (EAA) realizando uma busca para identificar clone positivo e a construção da biblioteca “shotgun”. Os dados gerados pelo sequêciamento foram utilizados para a montagem do mapa com sequencis conservadas que permitiu identificação de genes codificadores de pirofosfatase inorgânica (PPase) e tioesterase (TEs). A pirofosfatase inorgânica tem um papel importante no metabolismo do fósforo, além de controlar a concentração celular de pirofosfato (PPi) e processo de biossíntese. Tioesterases (TEs) são responsáveis pela hidrólise de um grupo tioéster carboxílico e um átomo de enxofre em ácidos graxos. A metagenômica revelou-se como uma ferramenta inovadora para explorar novos biocatalisadores na microbiota presente no solo. A análise dos dados in silico permitiu a predição da estrutura tridimensional e possível função das proteínas, assim os resultados sugerem que MetaPPase ...
The soil diversity of microorganisms with potential to select new genes, enzymes and compounds able to supply the high demand of biotechnology industry. In this sense, an immense diversity of microorganisms, yet most remains unexplored. Thus, soil diversity it is stimulated the search for new biocatalyst to high efficiency and stability, has been a constant pursuit of enzymologists, biochemists and chemical engineers. One of that biocatalyst is the hydrolases group, which are great interest to market for enzymes that cleavage of chemical structure by the addition of water. The hydrolases are widely used in industrial processes such as the application of additives in animal feed, textile, biodiesel production and biosynthesis of new antibiotics. Thus, the aim of this work was to find new hydrolases genes. In this paper, we used metagenomic library of soil under Eucalyptus spp. arboretum (EAA), was performed screening to identify a positive clone and construct the shotgun library. The data was analyzed using bioinformatics tools, to assemble the functional map and identify a hydrolase gene as possible novel inorganic (PPase) a thioesterase (TEs). The inorganic pyrophosphatase that has an important role in phosphorus metabolism controlling the cellular concentration of pyrophosphate (PPi) and biosynthetic process. Thioesterase (TEs) responsible for the hydrolysis of a carboxylic thioester group and a sulfur atom in fatty acids. The metagenomic revealed itself as an innovative tool for exploring novel biocatalysts in the microbiota present in the soil. The data analyses provide three-dimensional structure and protein function and the results suggest that MetaPPase is M- PPase and perchance an H+_PPase transporting subfamilies and TEs_ Meta possibly a new thioesterase
The soil diversity of microorganisms with potential to select new genes, enzymes and compounds able to supply the high demand of biotechnology industry. In this sense, an immense diversity of microorganisms, yet most remains unexplored. Thus, soil diversity it is stimulated the search for new biocatalyst to high efficiency and stability, has been a constant pursuit of enzymologists, biochemists and chemical engineers. One of that biocatalyst is the hydrolases group, which are great interest to market for enzymes that cleavage of chemical structure by the addition of water. The hydrolases are widely used in industrial processes such as the application of additives in animal feed, textile, biodiesel production and biosynthesis of new antibiotics. Thus, the aim of this work was to find new hydrolases genes. In this paper, we used metagenomic library of soil under Eucalyptus spp. arboretum (EAA), was performed screening to identify a positive clone and construct the shotgun library. The data was analyzed using bioinformatics tools, to assemble the functional map and identify a hydrolase gene as possible novel inorganic (PPase) a thioesterase (TEs). The inorganic pyrophosphatase that has an important role in phosphorus metabolism controlling the cellular concentration of pyrophosphate (PPi) and biosynthetic process. Thioesterase (TEs) responsible for the hydrolysis of a carboxylic thioester group and a sulfur atom in fatty acids. The metagenomic revealed itself as an innovative tool for exploring novel biocatalysts in the microbiota present in the soil. The data analyses provide three-dimensional structure and protein function and the results suggest that MetaPPase is M- PPase and perchance an H+_PPase transporting subfamilies and TEs_ Meta possibly a new thioesterase
Descrição
Palavras-chave
Solos, Microorganismos, Biologia molecular, Bioinformática, Proteínas, Genômica, Molecular biology
Como citar
RODRIGUES, Gisele Regina. Análise in silico de uma pirofosfatase e de uma tiosterase de uma biblioteca metagenômica de solo de Eucalipto spp. 2014. xv, 89 p. Tese (doutorado) - Universidade Estadual Paulista Júlio de Mesquita Filho, Faculdade de Ciências Agrárias e Veterinárias, 2014.