Identification, cloning, and characterization of a novel chitinase from leaf-cutting ant Atta sexdens: An enzyme with antifungal and insecticidal activity

Micocci, Kelli Cristina; Moreira, Ariele C.; Sanchez, Amanda D.; Pettinatti, Jessica L.; Rocha, Marina Campos; Dionizio, Bruna Soares; Correa, Katia C.S.; Malavazi, Iran; Wouters, Felipe C.; Bueno, Odair Corrêa; Souza, Dulce Helena Ferreira de

doi:10.1016/j.bbagen.2022.130249

Cited by 4 publications

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“…The recombinant chitinase AsChtII-C4B1 contains a catalytic domain and a carbohydrate-binding module (CBM), which has been reported to assist in anchoring the enzyme to the insoluble substrate through the interaction of conserved aromatic residues, breaking the crystalline structure of the substrate, resulting in the formation of free chain ends [ 23 , 42 ]. This enzyme shows activity against colloidal α-chitin and has been shown to have fungicidal and larvicidal activity [ 27 ]; it was inferred that it might also act on solid-state chitin. Thus, this study assessed the activity of the enzyme against solid α-chitin and colloidal and solid β-chitin.…”

Section: Resultsmentioning

confidence: 99%

“…A previous study reported that the recombinant chitinase AsChtII-C4B1 demonstrated fungicidal activity against the filamentous fungus Aspergillus fumigatus [ 27 ]. In the present study, the enzyme was purified via ammonium sulfate precipitation and affinity chromatography and evaluated against the phytopathogenic fungus L. theobromae , an ascomycete belonging to class Dothideomycetes , order Botryospheriales , family Botryosphaeriaceae [ 54 ].…”

Section: Resultsmentioning

confidence: 99%

“…The recombinant chitinase AsChtII-C4B1 was obtained as reported in the literature, being expressed into the extracellular medium in a Picchia pastoris system and purified on a nickel resin affinity column [ 27 ].…”

Section: Methodsmentioning

confidence: 99%

“…Recently, our research group expressed in Pichia pastoris a chitinase from the leaf-cutting ant Atta sexdens (AsChtII-C4B1), which consists of a catalytic domain and a chitin-binding domain (CBM) belonging to the GH18 family of GHs [ 27 ]. AsChtII-C4B1 exhibited larvicidal activity against the tested model Spodoptera frugiperda and fungicidal activity against human pathogenic fungi Candida albicans and Aspergillus fumigatus .…”

Section: Introductionmentioning

confidence: 99%

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

Correa,

Facchinatto,

Habitzreuter

et al. 2024

Polymers

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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 AsChtII-C4B1 could be applied as an agent for the bioproduction of chitin derivatives and as a potential antifungal agent.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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