Functional Characterization and Antifungal Activity of Insect-Derived Chitinases Expressed in Pichia pastoris.

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dc.contributorFEDERAL UNIVERSITY OF SAO CARLOS
dc.contributorSAO PAULO STATE UNIVERSITY ‘JULIO DE MESQUITA FILHO’
dc.contributorLUIZ ALBERTO COLNAGO, CNPDIA
dc.contributorFEDERAL UNIVERSITY OF SÃO CARLOS
dc.contributorFEDERAL UNIVERSITY OF SÃO CARLOS.
dc.creatorCORREA, K. C. S.
dc.creatorRIBEIRO, G. H.
dc.creatorBUENO, O. C.
dc.creatorCOLNAGO, L. A.
dc.creatorMALAVAZI, I.
dc.creatorSOUZA, D. H. F. de
dc.date2026-06-22T13:54:34Z
dc.date2026-06-22T13:54:34Z
dc.date2026-06-22
dc.date2026
dc.date.accessioned2026-07-07T04:30:03Z
dc.descriptionChitinases 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.
dc.format20 p.
dc.identifierPolymers, v. 18, 402, 2026.
dc.identifierhttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1187727
dc.identifierhttps://doi.org/10.3390/polym18030402
dc.identifier.urihttp://hdl.handle.net/123456789/463295
dc.languageeng
dc.rightsopenAccess
dc.subjectInsect chitinases
dc.subjectAntifungal activity
dc.subjectRecombinant chitinases
dc.subjectBiotechnology applications
dc.titleFunctional Characterization and Antifungal Activity of Insect-Derived Chitinases Expressed in Pichia pastoris.
dc.typeArtigo de periódico

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