Loosenin, a novel protein with cellulose-disrupting activity from Bjerkandera adusta

Expansins and expansin-like proteins loosen cellulose microfibrils, possibly through the rupture of intramolecular hydrogen bonds. Together with the use of lignocellulolytic enzymes, these proteins are potential molecular tools to treat plant biomass to improve saccharification yields. Here we descr...

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Bibliographic Details
Published in:Microbial cell factories 2011-02, Vol.10 (1), p.8-8, Article 8
Main Authors: Quiroz-Castañeda, Rosa E, Martínez-Anaya, Claudia, Cuervo-Soto, Laura I, Segovia, Lorenzo, Folch-Mallol, Jorge L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteria
Cellulase
Cellulose
Cellulose - chemistry
Cellulose - metabolism
Chemical bonds
Chitin - chemistry
Chitin - metabolism
Cloning
Cloning, Molecular
Coriolaceae - metabolism
Enzymes
Fungal Proteins - genetics
Fungal Proteins - metabolism
Hydrogen-Ion Concentration
Molecular Sequence Data
Mushrooms
Physiological aspects
Protein Binding
Proteins
Saccharomyces cerevisiae - metabolism
Temperature
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Summary:Expansins and expansin-like proteins loosen cellulose microfibrils, possibly through the rupture of intramolecular hydrogen bonds. Together with the use of lignocellulolytic enzymes, these proteins are potential molecular tools to treat plant biomass to improve saccharification yields. Here we describe a new type of expansin-related fungal protein that we have called loosenin. Its corresponding gene, loos1, from the basidiomycete Bjerkandera adusta, was cloned and heterologously expressed in Saccharomyces cerevisiae. LOOS1 is distantly related to plant expansins through the shared presence of a DPBB domain, however domain II found in plant expansins is absent. LOOS1 binds tightly to cellulose and chitin, and we demonstrate that cotton fibers become susceptible to the action of a commercial cellulase following treatment with LOOS1. Natural fibers of Agave tequilana also become susceptible to hydrolysis by cellulases after loosenin treatment. LOOS1 is a new type of protein with disrupting activity on cellulose. LOOS1 binds polysaccharides, and given its enhancing properties on the action of hydrolytic enzymes, LOOS1 represents a potential additive in the production of fermentable sugars from lignocellulose.
ISSN:1475-2859
1475-2859
DOI:10.1186/1475-2859-10-8