AI Article Synopsis
- Microbial endo-beta-1,4-xylanases from glycanase families 10 and 11 exhibit different efficiencies in hydrolyzing water-unextractable arabinoxylan (WU-AX).
- The enzyme from Thermoascus aurantiacus (family 10) achieves half-maximal hydrolysis rates at a lower concentration (4.4 nM) than the enzyme from Sporotrichum thermophile (family 11) (7.1 nM), making it about twice as efficient.
- Different xylanases produce varying lengths of feruloylated products, with the T. aurantiacus enzyme releasing a shorter feruloyl arabinoxylodisaccharide (FAX2) compared to the S. thermophile enzyme
Article Abstract
Microbial endo-beta-1,4-xylanases (EXs, EC 3.2.1.8) belonging to glycanase families 10 and 11 differ in their action on water-unextractable arabinoxylan (WU-AX). WU-AX was incubated with different levels of a Thermoascus aurantiacus family 10 and a Sporotrichum thermophile family 11 endoxylanases. At 10 g l(-1) arabinoxylan, enzyme concentrations (KE values) needed to obtain half-maximal hydrolysis rates (V(max) values) were 4.4 nM for the xylanase from T. aurantiacus and 7.1 nM for the xylanase from S. thermophile. Determination of Vmax/KE revealed that the family 10 enzyme hydrolysed two times more efficiently WU-AX than the family 11 enzyme. Molecular weights of the products formed were assessed and separation of feruloyl-oligosaccharides was achieved by anion-exchange and size-exclusion chromatography (SEC). The main difference between the feruloylated products by xylanases of family 10 and 11 concerned the length of the products containing feruloyl-arabinosyl substitution. The xylanase from T. aurantiacus liberated from WU-AX a feruloyl arabinoxylodisaccharide (FAX2) as the shortest feruloylated fragment in contrast with the enzyme from S. thermophile, which liberated a feruloyl arabinoxylotrisaccharide (FAX3). These results indicated that different factors govern WU-AX breakdown by the two endoxylanases.
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| http://dx.doi.org/10.1016/s0141-8130(03)00077-1 | DOI Listing |
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