Abstract
Chondroitin B lyase is a typical enzyme that catalyzes dermatan sulfate (DS) to produce oligosaccharides mainly 4,5-unsaturated dermatan sulfate disaccharides. It has been widely used in fields of medicine, functional food, and cosmetics because of its high selectivity. Here, a novel chondroitin B lyase from Pedobacter schmidteae (PsChonB) was cloned and heterologously expressed in Escherichia coli. The recombinant chondroitin B lyase had the highest activity in Tris-HCl buffer (100 mM, pH 8.0) at 40 °C. Characterization of the enzyme showed high stability of PsChonB, and its half-lives were 693 and 7949 min at 40 and 25 °C, and there was no significant decrease in activity after 30 days of storage at 4 °C. The specific activity, Km, Kcat, and Vmax of PsChonB were 395 U mg−1, 0.36 mg mL−1, 240.66 s−1, and 406.72 U mg−1. Molecular docking analysis of the enzyme indicated that the conserved residues Arg364, Arg363, His334, Arg318, Arg271, and Glu245 play vital roles in substrate binding. Compared with the previously reported chondroitin B lyases, PsChonB had the advantages of high activity and stability which indicated that it could be favorable for industrial production, clinic trials, and analytical the structures of glycosaminoglycans.
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