Improvement of arabinoxylan degradation in Clostridium saccharobutylicum DSM 13864<sup>T</sup> fermentations by heterologous glycoside hydrolase supplementation and expression. [PDF]
Edelmann H +4 more
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Advances in Lignocellulose-Degrading Enzyme Discovery from Anaerobic Rumen Fungi. [PDF]
Dhakal R +4 more
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Genome-scale metabolic modeling of Ruminiclostridium cellulolyticum: a microbial cell factory for valorization of lignocellulosic biomass. [PDF]
Burgos I +4 more
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Alterations of mouse gut microbiome in alveolar echinococcosis. [PDF]
Cui Z +10 more
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Phage-encoded depolymerases as a strategy for combating multidrug-resistant Acinetobacter baumannii. [PDF]
Islam MM, Mahbub NU, Shin WS, Oh MH.
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Cellulolytic and hemicellulolytic capacity of Acetivibrio clariflavus. [PDF]
Šuchová K, Puchart V.
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Unveiling a classical mutant in the context of the GH3 β-glucosidase family in Neurospora crassa. [PDF]
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Structures, Biochemical Characteristics, and Functions of β-Xylosidases
Journal of Agricultural and Food Chemistry, 2023The complete degradation of abundant xylan derived from plants requires the participation of β-xylosidases to produce the xylose which can be converted to xylitol, ethanol, and other valuable chemicals. Some phytochemicals can also be hydrolyzed by β-xylosidases into bioactive substances, such as ginsenosides, 10-deacetyltaxol, cycloastragenol, and ...
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β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides [PDF]
Xylan, a prominent component of cellulosic biomass, has a high potential for degradation into reducing sugars, and subsequent conversion into bioethanol. This process requires a range of xylanolytic enzymes. Among them, β-xylosidases are crucial, because they hydrolyze more glycosidic bonds than any of the other xylanolytic enzymes.
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Immobilization and Stabilization of Beta-Xylosidases from Penicillium janczewskii [PDF]
β-Xylosidases are critical for complete degradation of xylan, the second main constituent of plant cell walls. A minor β-xylosidase (BXYL II) from Penicillium janczewskii was purified by ammonium sulfate precipitation (30% saturation) followed by DEAE-Sephadex chromatography in pH 6.5 and elution with KCl.
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