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Updated: Jul 3, 2026

Elucidating β-1,3-Glucanase and Peroxidase Physicochemical Properties of Wheat Cell Wall Defense Mechanism Against Diuraphis noxia Infestation
Published on: July 26, 2024
Three carbohydrate-binding modules of laminarinase LA-Lam recognize β-1,3-glucan and enhance hydrolytic activity
Masahiko Okai1, Nozomi Ohki2, Kengo Nagase2
1Department of Ocean Sciences, Tokyo University of Marine Science and Technology, 4-5-7 Konan, Minato-ku, Tokyo 108-8477, Japan.
Abstract:
Carbohydrate-binding modules (CBMs) promote enzyme-substrate association, enhancing catalytic activity toward soluble and insoluble substrates. In this study, we characterized the three tandem domains of laminarinase LA-Lam from Pseudoalteromonas sp. LA as the first members of the CBM115 family. Affinity gel electrophoresis (AGE) showed that the three domains bound Laminaria digitata laminarin. Depletion isotherm assays revealed that binding affinity for curdlan followed the order CBM115_C > CBM115_M > CBM115_N, whereas CBM115_C exhibited the highest affinity for yeast β-glucan. Kinetic analyses demonstrated that the CBMs enhanced laminarin hydrolysis, but the number of CBMs had little additional effect on catalytic efficiency. The predicted structural models of the three CBMs indicated similarities to CBMs in families 4, 6, and 102. The differing binding affinities for curdlan and yeast β-glucan among the three CBMs may reflect variations in the region surrounding the substrate-binding cleft.
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