Penicillium sp J39 lipase immobilization by different strategies, stabilization and characterization of derivatives

• Grant number: 14/04925-1
• Support Opportunities: Scholarships abroad - Research Internship - Master's degree
• Start date: June 12, 2014
• End date: December 11, 2014
• Field of knowledge: Agronomical Sciences - Food Science and Technology - Food Science
• Principal Investigator: Eleonora Cano Carmona
• Grantee: Daniela Flavia Machado Turati
• Supervisor: Jose Manuel Guisán Seijas
• Host Institution: Instituto de Biociências (IB). Universidade Estadual Paulista (UNESP). Campus de Rio Claro. Rio Claro , SP, Brazil
• Institution abroad: Consejo Superior de Investigaciones Científicas (CSIC), Spain
• Associated to the scholarship: 13/15157-2 - Purification, immobilization and biochemical characterization of lipase produced by Penicillium sp J39 in submerged fermentation, BP.MS

Abstract

Lipases (triacylglycerol acyl hydrolase, EC 3.1.1.3) constitute a class of enzymes that catalyze the hydrolysis of ester bonds of triacylglycerol, operating at oil/water interface. These enzymes emerge in industrial processes, being used in the production of detergents, pulp and paper, dairy, cosmetics, among others. In spite of their excellent catalytic properties, the use of soluble enzymes in industrial processes is often costly and economically unviable, due to their disposal after use, poor stability and efficiency in various process conditions. Enzyme immobilization is an alternative, since it increases enzymatic efficiency, improves stability and is capable of reuse, besides allowing that only products are withdrawn in multiple steps processes. The type of enzyme immobilization has been associated with the degree of modification and stabilization of protein structure, which determines characteristics such as enzyme activity and stability at different conditions of temperature, pH, organic solvents, etc. In this context, this work aims to immobilize Penicillium sp J39 lipase produced under submerged fermentation by different strategies, in order to obtain derivatives to be used in aqueous media (adsorption on octyl-agarose and MANAE-agarose and multipoint covalent attachment to glyoxyl-agarose) and in organic media (octadecyl Sepabeads®), as well as to characterize immobilization derivatives on its ability to reuse, stability at different pH and organic media, hydrolysis of fish oil in aqueous medium and ethanolysis of fish oil in organic medium. (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)

TURATI, DANIELA F. M.; MORAIS JUNIOR, WILSON G.; TERRASAN, CESAR R. F.; MORENO-PEREZ, SONIA; PESSELA, BENEVIDES C.; FERNANDEZ-LORENTE, GLORIA; GUISAN, JOSE M.; CARMONA, ELEONORA C.. Immobilization of Lipase from Penicillium sp Section Gracilenta (CBMAI 1583) on Different Hydrophobic Supports: Modulation of Functional Properties. Molecules, v. 22, n. 2, FEB 2017. (14/04925-1)

MORENO-PEREZ, SONIA; MACHADO TURATO, DANIELA FLAVIA; BORGES, JANAINA PIRES; LUNA, PILAR; JAVIER SENORANS, FRANCISCO; GUISAN, JOSE M.; FERNANDEZ-LORENTE, GLORIA. Critical Role of Different Immobilized Biocatalysts of a Given Lipase in the Selective Ethanolysis of Sardine Oil. Journal of Agricultural and Food Chemistry, v. 65, n. 1, p. 117-122, JAN 11 2017. (14/04925-1)