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A novel ulvan lyase family with broad-spectrum activity from the ulvan utilisation loci of Formosa agariphila KMM 3901

Journal article
Authors V. R. Konasani
Chunsheng Jin
Niclas G. Karlsson
E. Albers
Published in Scientific Reports
Volume 8
ISSN 2045-2322
Publication year 2018
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Language en
Keywords persicivirga-ulvanivorans, sulfated polysaccharides, signal peptides, green seaweeds, uronic-acid, web server, algae, degradation, extracts, oligosaccharides, Science & Technology - Other Topics
Subject categories Biological Sciences


Ulvan, which is one of the major structural polysaccharides of the cell walls of green macroalgae, is degraded by ulvan lyases via the beta-elimination mechanism with the release of oligosaccharides that have unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (Delta) at the non-reducing end. These ulvan lyases belong to the PL24 or PL25 or PL28 family in the CAZy database. In this study, we identify and biochemically characterise a periplasmic novel broad-spectrum ulvan lyase from Formosa agariphila KMM 3901. The lyase was overexpressed in Escherichia coli, and the purified recombinant enzyme depolymerised ulvan in an endolytic manner with a K-m of 0.77 mg/ml, and displayed optimum activity at 40 degrees C and pH 8. This lyase also degraded heparan sulphate and chondroitin sulphate. Detailed analyses of the end-products of the enzymatic degradation of ulvan using H-1- and C-13-NMR and LC-MS revealed an unsaturated disaccharide (Delta Rha3S) and a tetrasaccharide (Delta Rha3S-Xyl-Rha) as the principal end-products. In contrast to the previously described ulvan lyases, this novel lyase is mostly composed of alpha-helices that form an (alpha/alpha)(6) incomplete toroid domain and displays a remarkably broad-spectrum activity. This novel lyase is the first member of a new family of ulvan lyases.

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Utskriftsdatum: 2020-08-06