Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 act differently toward soluble and insoluble xylans.

Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 (C1), Xyl7 and Xyl8, were purified and the influence of solubility and molecular structure of various xylans on their efficiency was investigated. Both endo-xylanases were hindered by a high degree of substitution of a xylan. The two GH11 xylanases released different products from the xylans, in which Xyl7 displayed a degradation product composition closer to GH10 xylanases.

Efficient plant biomass degradation by thermophilic fungus Myceliophthora heterothallica.

Rapid and efficient enzymatic degradation of plant biomass into fermentable sugars is a major challenge for the sustainable production of biochemicals and biofuels. Enzymes that are more thermostable (up to 70°C) use shorter reaction times for the complete saccharification of plant polysaccharides compared to hydrolytic enzymes of mesophilic fungi such as Trichoderma and Aspergillus species. The genus Myceliophthora contains four thermophilic fungi producing industrially relevant thermostable enzymes.

Two GH10 endo-xylanases from Myceliophthora thermophila C1 with and without cellulose binding module act differently towards soluble and insoluble xylans.

Xylanases are mostly classified as belonging to glycoside hydrolase (GH) family 10 and 11, which differ in catalytic properties and structures. However, within one family, differences may also be present. The influence of solubility and molecular structure of substrates towards the efficiency of two GH10 xylanases from Myceliophthora thermophila C1 was investigated.

Enzymatic production and characterization of konjac glucomannan oligosaccharides.

Enzymes from a balanced human gut flora are promising tools to design prebiotic oligosaccharides. In this study, we investigated the action of enzymes from fecal bacteria on the complex polysaccharide konjac glucomannan (KGM). The oligosaccharides produced were compared to oligosaccharides from KGM digests with fungal endo-β-(1,4)-glucanase (EG) or endo-β-(1,4)-mannanase (EM).

Introducing capillary electrophoresis with laser-induced fluorescence detection (CE-LIF) for the characterization of konjac glucomannan oligosaccharides and their in vitro fermentation behavior.

The application of capillary electrophoresis with laser-induced fluorescence detection (CE-LIF) as a tool for the characterization of complex carbohydrate structures was investigated for konjac glucomannan (KGM) oligosaccharide mixtures and the monitoring of their structural changes during 72 h of in vitro fermentation with human gut flora. Different types of KGM oligosaccharide mixtures were produced from a KGM polysaccharide using endo-beta-(1,4)-mannanase and endo-beta-(1,4)-glucanase. Distinction of structures emerging from different enzymatic KGM digests and detection of acetylated oligosaccharides were possible by both CE-LIF and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS).