Non-Specific GH30_7 Endo-β-1,4-xylanase from Talaromyces leycettanus

This study describes the catalytic properties of a GH30_7 xylanase produced by the fungus Talaromyces leycettanus. The enzyme is an ando-beta-1,4-xylanase, showing similar specific activity towards glucuronoxylan, arabinoxylan, and rhodymenan (linear beta-1,3-beta-1,4-xylan). The heteroxylans are hydrolyzed to a mixture of linear as well as branched beta-1,4-xylooligosaccharides that are shorter than the products generated by GH10 and GH11 xylanases. In the rhodymenan hydrolyzate, the linear beta-1,4-xylooligosaccharides are accompanied with a series of mixed linkage homologues. Initial hydrolysis of glucuronoxylan resembles the action of other GH30_7 and GH30_8 glucuronoxylanases, resulting in a series of aldouronic acids of a general formula MeGlcA(2)Xyl(n). Due to the significant non-specific endoxylanase activity of the enzyme, these acidic products are further attacked in the unbranched regions, finally yielding MeGlcA(2)Xyl(2-3). The accommodation of a substituted xylosyl residue in the -2 subsite also applies in arabinoxylan depolymerization. Moreover, the xylose residue may be arabinosylated at both positions 2 and 3, without negatively affecting the main chain cleavage. The catalytic properties of the enzyme, particularly the great tolerance of the side-chain substituents, make the enzyme attractive for biotechnological applications. The enzyme is also another example of extraordinarily great catalytic diversity among eukaryotic GH30_7 xylanases.

Automated summary

This study explores the catalytic properties of a GH30_7 xylanase from the fungus Talaromyces leycettanus, demonstrating its specificity towards various types of xylans. The enzyme shows remarkable tolerance towards side-chain substituents, making it attractive for biotechnological applications. Its catalytic diversity reflects the wide range of enzymatic capabilities among eukaryotic GH30_7 xylanases.