Characterization of substrate binding to novel thermostable lipases/esterases and rational design to change their substrate specificity for biotechnological applications

• Grant number: 12/20490-0
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate
• Start date: August 12, 2013
• End date: February 11, 2014
• Field of knowledge: Biological Sciences - Biochemistry - Molecular Biology
• Principal Investigator: Eliana Gertrudes de Macedo Lemos
• Grantee: Mariana Rangel Pereira
• Supervisor: Marko Hyvönen
• Host Institution: Faculdade de Ciências Agrárias e Veterinárias (FCAV). Universidade Estadual Paulista (UNESP). Campus de Jaboticabal. Jaboticabal , SP, Brazil
• Institution abroad: University of Cambridge, England
• Associated to the scholarship: 11/09136-7 - Functional and Structural Characterization of Lipolitic Enzymes of Consortium Specialized on Diesel Oil Degradation, BP.DR

Abstract

Global trade industries enzymes is estimated at U.S 2.3 billion dollars, divided mainly in detergents ($ 789 million), food applications ($ 634 million), agriculture ($ 237 million). Within this trade, the lipolytic enzymes have been attracted enormous attention because of their potential biotechnological, and, most of this enzymes used in industries come from microbial origin.Because they are versatile and widely used is expected that lipase's future is as important as industrial catalysts, how much are currently proteases and carbohydrases. Lipases of microbial origin are economically attractive to be: easily biodegradable; usually act in mild conditions; and are chemo-selective, providing for the pharmaceutical industry to obtain drugs with reduced side effects. Aiming to identify enzymes with biotechnological potential, samples of a bacterial consortium degrading diesel oil, from a region greatly affected by chemical waste, were used as material for bioprospecting, using a metagenomics approach (master's student project, process number 2009/06991-0). From the analysis of the reading frames were identified five enzymes with function esterase/lipase which show low similarity with sequences deposited in major banks of known sequences. A preliminary characterization of these enzymes revealed its high biotechnological potential and in this context, this project aims to solve the crystal structures of these proteins, defining the regions of interaction with the substrate and using the technique of rational design of mutants to obtain proteins with high biotechnological potential. (AU)

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. (11/09136-7, 12/20490-0)