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. 2025 Jun;17(3):e70122.
doi: 10.1111/1758-2229.70122.

Enzymatic Strategies for Biocontrolling Phytopathogenic Fungi Using Trichoderma Koningiopsis LBM116

Natalia Soledad Amerio  1   2 , Marcela Paola Barengo  1   2 , Gustavo Angel Bich  1   2 , Pedro Dario Zapata  1   2 , Laura Lidia Villalba  1 , María Lorena Castrillo  1   2
Affiliations

Enzymatic Strategies for Biocontrolling Phytopathogenic Fungi Using Trichoderma Koningiopsis LBM116

Natalia Soledad Amerio et al. Environ Microbiol Rep. 2025 Jun.

Abstract

The growing demand for sustainable alternatives to chemical fungicides has driven the development of microbial-based biocontrol strategies. In this study, the native strain Trichoderma koningiopsis LBM116 (Misiones, Argentina) was optimised for the production of mycolytic enzymes (chitinases, β-1,3-glucanases, and proteases) using factorial and response surface experimental designs. Enzyme secretion was increased by more than 250% compared to initial conditions by selecting specific carbon and nitrogen sources and adjusting inoculum and pH parameters. The optimised enzyme formulation improved lettuce seed germination to 86.66% in the presence of the phytopathogen Fusarium sp., under controlled conditions. In seedling trials, it also reduced disease severity and improved growth parameters. These results confirm the dual effect of the enzyme formulation, acting as a biocontrol agent and plant growth promoter. This work highlights the potential of enzyme formulations derived from T. koningiopsis LBM116 as an effective, low-cost, and sustainable alternative for managing phytopathogens in agriculture.

Keywords: biological control; chitinases; enzymatic formulation; glucanases; proteases; sustainable agriculture.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

FIGURE 1
FIGURE 1
Enzymatic activity of T. koningiopsis LBM116 under different culture conditions. (A) Chitinase, (B) β‐1,3‐glucanase, and (C) Protease activities were measured in culture supernatants obtained after 8 days of growth. Carbon sources: QC: colloidal chitin; Gel: gelatin; Fit I: cell walls of Fusarium sp. treated; Fit II: cell walls of Fusarium sp. untreated. Nitrogen sources: Ex: yeast extract; Ma: mandels; SA: ammonium sulfate; Ur: urea. Bars represent mean values of three replicates ± standard error (SE).
FIGURE 2
FIGURE 2
Effect of different concentrations of the carbon source Fit I combined with two nitrogen sources on enzyme secretion by Trichoderma koningiopsis LBM116 after 10 days of incubation. (A) Chitinase activity. (B) β‐1,3‐glucanase activity. (C) Protease activity. Bars represent mean values of three replicates ± standard error (SE). The different letters in the columns represent significant differences (p < 0.05).
FIGURE 3
FIGURE 3
Effect of different concentrations of the carbon source Fit I on the secretion of enzymes by T. koningiopsis LBM116. (A) Chitinase activity, (B) β‐1,3‐glucanase activity, and (C) Protease activity. Bars represent mean values of three replicates ± standard error (SE). Different lowercase letters above the bars indicate statistically significant differences among treatments according to Tukey's test (p < 0.05).
FIGURE 4
FIGURE 4
Three‐dimensional response surface plots for enzymatic secretion by T. koningiopsis LBM116. The plots show the interactive effects of Ex concentration, initial inoculum, and pH culture medium. (A) Chitinase activity I: Ex and pH when inoculum is fixed at its middle level; II: Ex and inoculum when pH is fixed at its middle level. (B) β‐1,3‐glucanase activity I: Ex and pH when inoculum is fixed at its middle level; II: Ex and inoculum when pH is fixed at its middle level. (C) Protease activity I: Ex and pH when inoculum is fixed at its middle level; II: Ex and inoculum when pH is fixed at its middle level.
FIGURE 5
FIGURE 5
Lettuce seedlings after 30 days under different treatments. From left to right: (T1) Enzymatic formulation, (T2) Conidial suspension, (T3) Absolute control, (T4) Diseased control.
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References

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