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beta-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides

Rohman, 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 journalReview articleAcademicpeer-review

  • Ali Rohman
  • Bauke W. Dijkstra
  • Ni Nyoman Tri Puspaningsih

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.

Original languageEnglish
Article number5524
Number of pages26
JournalInternational Journal of Molecular Sciences
Volume20
Issue number22
Publication statusPublished - Nov-2019

    Keywords

  • 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

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