IDENTIFICATION OF A GENE SEQUENCE ENCODING AN ENDOGLUCANASE FROM Irpex lacteus (BASIDIOMYCOTA)

GIORGIO, M.; MARIO CARLOS NAZARENO SAPARRAT; ZAPATA, P.; VILLALBA, L.

Mar del Plata

Otro; LI Reunión SAIB 2015; 2015

SAIB

Endo-β-1,4-glucanases are enzymes that hydrolyze beta-1,4 bonds between two glucose units in the cellulose chain, having key role in several biotechnological processes such as cellulosic bioethanol production. The aim of this study was to identify DNA sequences encoding enzymes with endoglucanase activity from the fungus Irpex lacteus (Basidiomycota) LBM 034, isolated from the subtropical rain-forest of the province of Misiones, by PCR amplification using a pair of degenerate primers. The primers were designed based on the endoglucanase sequences from other fungi belonging to Phylum Basidiomycota. A fragment of ~2000 pb was found in the genomic DNA of I. lacteus LBM 034 when the PCR amplification was performed using the degenerate primers. The putative endoglucanase ORF identified, excluding signal peptide, encoded a fragment of 384 amino acid residues, interrupted by 14 introns. This deduced amino acid sequence revealed a multidomain structure composed of a Carbohydrate-Binding Module belonging to the Family 1, a Ser-/Thr-rich linker and a catalytic domain from the N-terminus. This putative endoglucanase showed high similitude compared to those belonging to family 5 of glycosyl hydrolases. Future studies will involve cloning and expression of this endoglucanase gene from I. lacteus LBM 034 as promising target in the uncovering of new recombinant enzymes of industrial application.