Structural and functional studies of the glycoside hydrolase family 3 β-glucosidase Cel3A from the moderately thermophilic fungus Rasamsonia emersonii
Autor: | Mikael Gudmundsson, Mats Sandgren, Thijs Kaper, Saeid Karkehabadi, Henrik Hansson, Edmund A. Larenas, Steve Kim, Sergio Sunux, Meredith K. Fujdala, Anna L. E. Larsson, Ingeborg Stals |
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Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
TALAROMYCES-EMERSONII
MECHANISM 0301 basic medicine Models Molecular Glycosylation Protein Conformation Disaccharide Crystallography X-Ray Lignin biodegradation chemistry.chemical_compound SUBSTRATE Structural Biology Hypocrea CRYSTAL-STRUCTURES Glycoside hydrolase glycoside hydrolase CELLULOSE HYDROLYSIS glycoproteins Fungal protein ANALYSIS REFINEMENT biology Rasamsonia emersonii Hydrolysis beta-Glucosidase fungus Biochemistry and Molecular Biology Eurotiales thermophilic fungus thermophilic Research Papers HYPOCREA-JECORINA Biochemistry β-glucosidase ENZYMES EXPRESSION crystal structure Technology and Engineering Cellulase crystal Fungal Proteins 03 medical and health sciences TRICHODERMA-REESEI CELLULASES beta-glucosidase Hydrolase structure Cel3A 030102 biochemistry & molecular biology Glycoside hydrolase family 3 biology.organism_classification 030104 developmental biology chemistry biology.protein Protein Multimerization Biokemi och molekylärbiologi |
Zdroj: | 'Acta Crystallographica D ', vol: 72, pages: 860-870 (2016) Acta Crystallographica. Section D, Structural Biology ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY |
ISSN: | 0907-4449 2059-7983 |
Popis: | Cel3A from the thermophilic fungus R. emersonii has proven to be more efficient in the hydrolysis of β-glycosidic linkages than Cel3A from H. jecorina. The filamentous fungus Hypocrea jecorina produces a number of cellulases and hemicellulases that act in a concerted fashion on biomass and degrade it into monomeric or oligomeric sugars. β-Glucosidases are involved in the last step of the degradation of cellulosic biomass and hydrolyse the β-glycosidic linkage between two adjacent molecules in dimers and oligomers of glucose. In this study, it is shown that substituting the β-glucosidase from H. jecorina (HjCel3A) with the β-glucosidase Cel3A from the thermophilic fungus Rasamsonia emersonii (ReCel3A) in enzyme mixtures results in increased efficiency in the saccharification of lignocellulosic materials. Biochemical characterization of ReCel3A, heterologously produced in H. jecorina, reveals a preference for disaccharide substrates over longer gluco-oligosaccharides. Crystallographic studies of ReCel3A revealed a highly N-glycosylated three-domain dimeric protein, as has been observed previously for glycoside hydrolase family 3 β-glucosidases. The increased thermal stability and saccharification yield and the superior biochemical characteristics of ReCel3A compared with HjCel3A and mixtures containing HjCel3A make ReCel3A an excellent candidate for addition to enzyme mixtures designed to operate at higher temperatures. |
Databáze: | OpenAIRE |
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