Identification and Characterization of a Novel Mannanase from Klebsiella grimontii .

Konjac glucomannan (KGM) is a natural polysaccharide derived from konjac, which has been widely used in various fields due to its numerous beneficial properties. However, the high viscosity and water absorption of KGM limit its application. Compared with KGM, Konjac glucomannan oligosaccharides (KGMOS) have higher water solubility and stronger application value. In this paper, a novel mannanase ManA was cloned from to develop a new KGMOS-producing enzyme. Bioinformatic analysis shows that the structural similarity between ManA and other enzymes was less than 18.33%. Phylogenetic analysis shows that ManA shares different branches with the traditional mannanases containing the CMB35 domain, indicating that it is a novel mannanase. Then, the enzymatic properties were determined and substrate specificity was characterized. Surprisingly, ManA is stable in a very wide pH range of 3.0 to 10.0; it has a special substrate specificity and seems to be active only for mannans without galactose in the side chain. Additionally, the three-dimensional structure of the enzyme was simulated and molecular docking of the mannotetraose substrate was performed. As far as we know, this is the first report to characterize the enzymatic properties and to simulate the structure of mannanase from . This work will contribute to the development and characterization of novel -derived mannanases. The above results indicate that ManA is a promising tool for the production of KGMOS.