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
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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