Structural characterization of an endoglucanase from Serpula lacrymans var. lacrymans S7.9

Abstract

Lately cellulase enzymes from fungi and also bacteria, have received much attention due to their application in bioethanol production from lignocellulosic feedstock. Dry rot fungus (Serpula lacrymans) is known to be the most damaging destroyer of indoor wood construction materials in temperate regions. Therefore the very recent sequencing of this fungus genome has opened new possibilities. We describe here the analysis of the primary, secondary and tertiary structure of a 255 amino acid sequence endoglucanase, from S. lacrymans var. lacrymans S7.9, having a molecular weight of 26746. We also provide the amino acids from the active site.