beta-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by MonosaccharidesRohman, A., Dijkstra, B. W. & Puspaningsih, N. N. T., Nov-2019, In : International Journal of Molecular Sciences. 20, 22, 26 p., 5524.
Research output: Contribution to journal › Review article › Academic › peer-review
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, beta-xylosidases are crucial, because they hydrolyze more glycosidic bonds than any of the other xylanolytic enzymes. They also enhance the efficiency of the process by degrading xylooligosaccharides, which are potent inhibitors of other hemicellulose-/xylan-converting enzymes. On the other hand, the beta-xylosidase itself is also inhibited by monosaccharides that may be generated in high concentrations during the saccharification process. Structurally, beta-xylosidases are diverse enzymes with different substrate specificities and enzyme mechanisms. Here, we review the structural diversity and catalytic mechanisms of beta-xylosidases, and discuss their inhibition by monosaccharides.
|Number of pages||26|
|Journal||International Journal of Molecular Sciences|
|Publication status||Published - Nov-2019|
- biomass, hemicellulose, bioethanol, xylanolytic enzyme, hemicellulase, glycoside hydrolase, ALPHA-L-ARABINOFURANOSIDASE, HYDROLASE FAMILY 3, BIOCHEMICAL-CHARACTERIZATION, TRICHODERMA-REESEI, CRYSTAL-STRUCTURE, XYLOSE-TOLERANT, SELENOMONAS-RUMINANTIUM, ASPERGILLUS-NIGER, THERMOANAEROBACTERIUM-SACCHAROLYTICUM, KINETIC-ANALYSIS