Activity of a Recombinant Chitinase of the Atta sexdens Ant on Different Forms of Chitin and Its Fungicidal Effect against Lasiodiplodia theobromae.

Abstract: This study evaluates the activity of a recombinant chitinase from the leaf-cutting ant Atta sexdens (AsChtII-C4B1) against colloidal and solid α- and β-chitin substrates. 1H 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. Both solid state 13C NMR and XRD analyses showed minor differences in chitin crystallinity pre- and post-reaction, indicative of partial hydrolysis under the studied conditions, resulting in the formation of GlcNAc and a reduction in molecular mass. However, the enzyme was unable to completely degrade the chitin samples, as they retained most of their solid-state structure. It was also observed that the enzyme acts progressively and with a greater activity on α-chitin than on β-chitin. AsChtII-C4B1 significantly changed the hyphae of the phytopathogenic fungus Lasiodiplodia theobromae, hindering its growth in both solid and liquid media and reducing its dry biomass by approximately 61%. The results demonstrate that AsChtIIC4B1 could be applied as an agent for the bioproduction of chitin derivatives and as a potential antifungal agent.

Bibliographic Details

Main Authors:	CORREA, K. C. S., FACCHINATO, W. M., HABITZREUTER, F. B., RIBEIRO, G. H., RODRIGUES, L. G., MICOCCI, K. C., CAMPANA-FILHO, S. P., COLNAGO, L. A., SOUZA, D. H. F.
Other Authors:	FEDERAL UNIVERSITY OF SAO CARLOS
Format:	Artigo de periódico biblioteca
Language:	eng
Published:	2024-05-14
Subjects:	Insect chitinase, Fungicide,
Online Access:	http://www.alice.cnptia.embrapa.br/alice/handle/doc/1164249 https:// doi.org/10.3390/polym16040529
Tags:	Add Tag No Tags, Be the first to tag this record!