This study evaluates the activity of a recombinant chitinase from the leaf-cutting ant (AsChtII-C4B1) against colloidal and solid α- and β-chitin substrates. H NMR analyses of the reaction media showed the formation of N-acetylglucosamine (GlcNAc) as the hydrolysis product. Viscometry analyses revealed a reduction in the viscosity of chitin solutions, indicating that the enzyme decreases their molecular masses.
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