Título:	Activity of a Recombinant Chitinase of the Atta sexdens Ant on Different Forms of Chitin and Its Fungicidal Effect against Lasiodiplodia theobromae.
Autor:	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.
Afiliación:	FEDERAL UNIVERSITY OF SAO CARLOS UNIVERSITY OF AVEIRO, ST. SANTIAGO UNIVERSITY OF SAO PAULO FEDERAL UNIVERSITY OF SAO CARLOS FEDERAL UNIVERSITY OF SAO CARLOS UNIVERSITY OF SAO PAULO LUIZ ALBERTO COLNAGO, CNPDIA FEDERAL UNIVERSITY OF SAO CARLOS.
Año:	2024
Referencia:	Polymers, v. 16, 529, 2014.
Páginas:	1 - 17
Descripción:	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.
Palabras clave:	Insect chitinase Fungicide
DOI:	https:// doi.org/10.3390/polym16040529
Tipo de Material:	Artigo de periódico
Acceso:	openAccess
Aparece en las colecciones:	Artigo em periódico indexado (CNPDIA)