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Functional and Structural Characterization of Lipolitic Enzymes of Consortium Specialized on Diesel Oil Degradation

Grant number: 11/09136-7
Support type:Scholarships in Brazil - Doctorate
Effective date (Start): November 01, 2011
Effective date (End): March 31, 2015
Field of knowledge:Biological Sciences - Genetics - Molecular Genetics and Genetics of Microorganisms
Principal Investigator:Eliana Gertrudes de Macedo Lemos
Grantee:Mariana Rangel Pereira
Home Institution: Faculdade de Ciências Agrárias e Veterinárias (FCAV). Universidade Estadual Paulista (UNESP). Campus de Jaboticabal. Jaboticabal , SP, Brazil
Associated scholarship(s):12/20490-0 - Characterization of substrate binding to novel thermostable lipases/esterases and rational design to change their substrate specificity for biotechnological applications, BE.EP.DR

Abstract

The use of microorganisms for the processing of natural materials is carried through has decades and comes growing with the news discovered in terms of methods of isolation, characterization and culture of these. Studies of different microbians populations of habitats, using conserved sequences of the genes 16S rRNA and 18S rRNA sample that most of the microorganisms that compose the biosphere not yet was studied. This population and genetic diversity comes being object of study in different aspects, but mainly with the objective to identify microorganisms with potential of bioremediation and biotechnological industry. One of the used strategies more than offers an almost limitless combination to find new genes coders of excellent products is the metagenomic approach, from which the genomic DNA of microorganisms gifts in samples of the environment isolated and is clonated in specific vectors for the construction of libraries. In function of the enormous biotechnological potential, the lipolytics enzymes come attracting attention in the global market, as for example: in the enzymatic mixtures for formularization of detergents; in the leather industry, being able to be applied together with others hidrolases in the removal of the subcutaneous fats; in the cosmetic production; pharmaceutical applications; biodiesel, amongst others. Lipases microbial presents low toxicity, is easily biodegradable and works in mild conditions, being distinguished for the quimio-selectivity, what it reduces the collateral effect of the drugs. With the objective of if identifying enzymes with biotechnological potential, samples of a degrading bacterial oil trust diesel, proceeding from a region sufficiently affected by chemical residues, had been used as material for the bioprospection, using the metagenomic approach (mester project, process number 2009/06991-0). From the analysis, four enzymes with function of esterase/lipase had been identified that they present low similarity with sequences of orthologous deposited in the main banks of known sequences. The preliminary characterization of these enzymes disclosed to its high biotechnological potential and in this context, the present project has for objective to produce on a large scale, to characterize biochemically and to crystallize such lipolytics enzymes.

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
PEREIRA, MARIANA RANGEL; MAESTER, THAS CARVALHO; MERCALDI, GUSTAVO FERNANDO; DE MACEDO LEMOS, ELIANA GERTRUDES; HYVONEN, MARKO; BALAN, ANDREA. From a metagenomic source to a high-resolution structure of a novel alkaline esterase. Applied Microbiology and Biotechnology, v. 101, n. 12, p. 4935-4949, JUN 2017. Web of Science Citations: 10.
PEREIRA, MARIANA RANGEL; MERCALDI, GUSTAVO FERNANDO; MAESTER, THAIS CARVALHO; BALAN, ANDREA; DE MACEDO LEMOS, ELIANA GERTRUDES. Est16, a New Esterase Isolated from a Metagenomic Library of a Microbial Consortium Specializing in Diesel Oil Degradation. PLoS One, v. 10, n. 7 JUL 27 2015. Web of Science Citations: 15.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.