Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System

• Published in: Applied and Environmental Microbiology
• Main Authors: Fredriksen, L., Stokke, R., Jensen, M. S., Westereng, B., Jameson, J.-K., Steen, I. H., Eijsink, V. G. H.
• Other Authors: Stabb, Eric V., Research Council of Norway, NorBioLab
• Format: Article in Journal/Newspaper
• Language: English
• Published: American Society for Microbiology 2019
• Subjects: Ecology; Applied Microbiology and Biotechnology; Food Science; Biotechnology; Arctic
• Online Access: http://dx.doi.org/10.1128/aem.02970-18; https://journals.asm.org/doi/pdf/10.1128/AEM.02970-18

Hot springs at the sea bottom harbor unique biodiversity and are a promising source of enzymes with interesting properties. We describe the functional characterization of a thermophilic and halophilic multidomain xylanase originating from the Arctic Mid-Ocean Ridge vent system, belonging to the well-studied family 10 of glycosyl hydrolases (GH10). This xylanase, AMOR_GH10A, has a surprisingly wide substrate range and is more active toward cellopentaose than toward xylopentaose. This substrate promiscuity is unique for the GH10 family and could prove useful in industrial applications. Emphasizing the versatility of AMOR_GH10A, its N-terminal domain binds to both xylans and glycans, while not showing significant sequence similarities to any known carbohydrate-binding module (CBM) in the CAZy database. Thus, this N-terminal domain lays the foundation for the new CBM85 family.