A novel GH30 xylobiohydrolase from Acremonium alcalophilum releasing xylobiose from the non-reducing end

Publication date: Available online 30 November 2019Source: Enzyme and Microbial TechnologyAuthor(s): Katarína Šuchová, Vladimír Puchart, Nikolaj Spodsberg, Kristian B.R. Mørkeberg Krogh, Peter BielyAbstractXylanases of the GH30 family are grouped to subfamilies GH30-7 and GH30-8. The GH30-8 members are of bacterial origin and well characterized, while the GH30-7 members are from fungal sources and their properties are quite diverse. Here, a heterologous expression and characterization of the GH30-7 xylanase AaXyn30A from a cellulolytic fungus Acremonium alcalophilum is reported. From various polymeric and oligomeric substrates AaXyn30A generates xylobiose as the main product. It was proven that xylobiose is released from the non-reducing end of all tested substrates, thus the enzyme behaves as a typical non-reducing-end acting xylobiohydrolase. AaXyn30A is active on different types of xylan, exhibiting the highest activity on rhodymenan (linear β-1,3-β-1,4-xylan) from which also an isomeric xylotriose Xyl-β-1,3-Xyl-β-1,4-Xyl is formed. Production of xylobiose from glucuronoxylan is at later stage accompanied by a release of aldouronic acids differing from those liberated by the bacterial GH30-8 glucuronoxylanases.

Source: Enzyme and Microbial Technology - December 1, 2019 Category: Biotechnology Source Type: research