Abstract
Abstract Loosenin is a protein recently described which presents amorphogenic activity on cellulose. It was isolated from the Basidiomycete Bjerkandera adusta and it enhances sugar release from cellulosic fibers treated previously with it and then subjected to cellulase treatment. It can also bind to other polysaccharides like chitin and xylans but presents no hydrolytic activity itself. Blast analysis using the loosenin amino acid sequence retrieved a sequence from the Neurospora crassa genome that showed 59% similarity. In this work, we cloned, expressed and partially characterized a putative loosenin from N. crassa, since these proteins have a potential for pretreatment of lignocellulosic materials.
Highlights
Lignocellulose is the most abundant biomass source; its degradation to simple sugars has been considered a viable way to produce bioethanol (Gray et al 2006)
In our group we previously described a novel protein with expansin-like activity from the Basidiomycete Bjerkandera adusta, it was called loosenin (LOOS1)
We found one sequence of Neurospora crassa, denominated N2, with 59% of similitude to LOOS1
Summary
Lignocellulose is the most abundant biomass source; its degradation to simple sugars has been considered a viable way to produce bioethanol (Gray et al 2006). Between the members of these families, only 20 to 40% of identity is shared at the level of amino acid sequence, and the highest conservation is found in the DPBB domain (Sampedro and Cosgrove 2005) Another group of expansins was described of organisms that are not plants; this group was called EXLX. In our group we previously described a novel protein with expansin-like activity from the Basidiomycete Bjerkandera adusta, it was called loosenin (LOOS1). This protein binds to polysaccharides and has only one domain with a DPBB fold. Because N. crassa is considered a model organism, with a lot of genetic and molecular tools, we cloned and expressed this sequence (N2) in Kluyveromyces lactis, to evaluate its amorphogenic activity
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