Título:	Functional Characterization and Antifungal Activity of Insect-Derived Chitinases Expressed in Pichia pastoris.
Autor:	CORREA, K. C. S. RIBEIRO, G. H. BUENO, O. C. COLNAGO, L. A. MALAVAZI, I. SOUZA, D. H. F. de
Afiliación:	FEDERAL UNIVERSITY OF SAO CARLOS SAO PAULO STATE UNIVERSITY ‘JULIO DE MESQUITA FILHO’ LUIZ ALBERTO COLNAGO, CNPDIA FEDERAL UNIVERSITY OF SÃO CARLOS FEDERAL UNIVERSITY OF SÃO CARLOS.
Año:	2026
Referencia:	Polymers, v. 18, 402, 2026.
Páginas:	20 p.
Descripción:	Chitinases catalyze the hydrolysis of β-1,4-glycosidic bonds in chitin, a structural biopoly mer synthesized by numerous organisms. Although these enzymes have been widely investigated, studies focusing on insect-derived chitinases remain limited. In this study, three recombinant chitinases from the leaf-cutter ant Atta sexdens were cloned, expressed in Pichia pastoris, and biochemically characterized. The enzymes-AsChtII-C2B3 (one catalytic and three chitin-binding domains), AsChtII-C3C4 (two catalytic domains), and AsChtII C5B1(one catalytic and one bindingdomain), exhibitedoptimalactivityatpH4–5and50 ◦C using colloidal chitin as substrate. Chitinase activity on colloidal α-chitin was confirmed by 1H NMR(proton nuclear magnetic resonance) spectroscopy, revealing GlcNAc concentra tions of 0.41, 0.48, and 0.56 mmol L−1 for AsChtII-C3C4, AsChtII-C2B3, and AsChtII-C5B1, respectively. Their antifungal activities were evaluated against the human pathogens Can dida albicans and Aspergillus fumigatus, as well as the phytopathogen Lasiodiplodia theobromae. Distinct inhibition profiles were observed: AsChtII-C5B1 (150 µg/mL) showed the highest activity against C. albicans (87.6% inhibition), while AsChtII-C3C4 (25 µg/mL) was most effective against A. fumigatus (60% inhibition). Notably, only AsChtII-C2B3 inhibited L. theobromae growth, inducing severe hyphal deformations observed by scanning electron microscopy (SEM). These findings demonstrate that recombinant A. sexdens chitinases ex hibit species-specific antifungal properties, underscoring their potential as biotechnological tools for medical and agricultural applications.
Palabras clave:	Insect chitinases Antifungal activity Recombinant chitinases Biotechnology applications
DOI:	https://doi.org/10.3390/polym18030402
Tipo de Material:	Artigo de periódico
Acceso:	openAccess
Aparece en las colecciones:	Artigo em periódico indexado (CNPDIA)