Characterization of a Pyranose Oxidase/-Glycoside Oxidase from sp. 3H14, Belonging to the Unexplored Clade II of Actinobacterial POx/CGOx.

Pyranose oxidase (POx) is an FAD-dependent oxidoreductase and belongs to the glucose-methanol-choline (GMC) superfamily of oxidoreductases. As recently reported, POxs and FAD-dependent -glycoside oxidases (CGOxs) share the same sequence space, and phylogenetic analysis of actinobacterial sequences belonging to this shared sequence space showed that it can be divided into four clades. Here, we report the biochemical characterization of a POx/CGOx from sp.

Value creation of copra meal mannan into functional manno-oligosaccharides (β-MOS) using the mannanase Bacillus man B (BlMan26B).

Agricultural wastes rich in β-mannan are an important environmental problem in tropical and sub-tropical countries. This research aims at dealing with this and investigates the valorization of mannan-rich copra meal from virgin coconut oil manufacturing into mannan-oligosaccharides (β-MOS) by enzymatic hydrolysis using β-mannanase from Bacillus licheniformis (BlMan26B). Lab-scale process, involving pre-treatment and bioconversion steps, were conducted and evaluated.

Surface-Displayed Mannanolytic and Chitinolytic Enzymes Using Peptidoglycan Binding LysM Domains.

Using as a food-grade carrier to create non-GMO whole-cell biocatalysts is gaining popularity. This work evaluates the immobilization yield of a chitosanase (CsnA, 30 kDa) from and a mannanase (ManB, 40 kDa) from on the surface of WCFS1 using either a single LysM domain derived from the extracellular transglycosylase Lp_3014 or a double LysM domain derived from the muropeptidase Lp_2162. ManB and CsnA were fused with the LysM domains of Lp_3014 or Lp_2162, produced in and anchored to the cell surface of .