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Novel xylanolytic triple domain enzyme targeted at feruloylated arabinoxylan degradation.

Enzyme Microb Technol. 2019; 
Holck J, Djajadi DT, Brask J, Pilgaard B, Krogh KBRM, Meyer AS, Lange L, Wilkens C.
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Biochemicals … 29–371); GH62 (residues 407–716) and GH10 (residues 727–1077) were purchased and cloned into pET-22b (CE1-GH62-GH10; CE1-GH62; GH62-GH10 and GH62) or pET-28a (CE1 and GH10) using the restriction sites Nco1 and Xho1 (GenScript, Piscataway, NJ, USA) in … Get A Quote

摘要

A three catalytic domain multi-enzyme; a CE1 ferulic acid esterase, a GH62 α-l-arabinofuranosidase and a GH10 β-d-1,4-xylanase was identified in a metagenome obtained from wastewater treatment sludge. The capability of the CE1-GH62-GH10 multi-enzyme to degrade arabinoxylan was investigated to examine the hypothesis that CE1-GH62-GH10 would degrade arabinoxylan more efficiently than the corresponding equimolar mix of the individual enzymes. CE1-GH62-GH10 efficiently catalyzed the production of xylopyranose, xylobiose, xylotriose, arabinofuranose and ferulic acid (FA) when incubated with insoluble wheat arabinoxylan (WAX-I) (kcat = 20.8 ± 2.6 s-1). Surprisingly, in an equimolar mix of the individual en... More

关键词

Arabinofuranosidase; Arabinoxylan; Ferulic acid esterase; Multi-enzyme; Xylanase