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. 2025 May 7;20(5):e0322106.
doi: 10.1371/journal.pone.0322106. eCollection 2025.

Developing a cosmetic formulation containing lipase produced by the fungus Aspergillus terreus

Gabriela Rocha Ramos  1 , Elissa Arantes Ostrosky  2 , Patrícia Santos Lopes  3 , Newton Andréo Filho  3 , Lohanna Luciyanla Kakuda  3 , Jéssica Nascimento da Silva Pinto  3 , Emanuela de Lima Viana  4 , Neyna Santos Morais  5 , Nathalia Saraiva Rios  6 , Ana Paula Barreto Gomes  2 , Francisco Humberto Xavier Júnior  7 , Francisco Canindé de Sousa Júnior  1   2 , Cristiane Fernandes de Assis  1   2
Affiliations

Developing a cosmetic formulation containing lipase produced by the fungus Aspergillus terreus

Gabriela Rocha Ramos et al. PLoS One. .

Abstract

This study aimed to evaluate the potential of lipase from Aspergillus terreus as an active ingredient in cosmetic formulations. Lipase was produced using the fungus Aspergillus terreus and was immobilized on gel silica as support. The enzymes were characterized using Scanning Electron Microscopy (SEM), Fourier Transform Infrared Spectroscopy (FTIR), X-ray Diffraction (XRD), Thermogravimetry and Differential Scanning Calorimetry (TG/DSC), and safety evaluation through cytotoxicity tests using NIH-3T3 fibroblast cells. A central composite rotatable design was employed to find the best conditions for enzymatic cosmetic production. The enzyme produced by A. terreus showed activity of 375.9 U/g of substrate, and the immobilized enzyme showed 12.78 U/g of silica, while the lipase from R. oryzae showed activity of 69.91 U/g. As confirmed by FTIR and XRD, SEM showed weak enzyme interaction with silica during immobilization. Cytotoxicity tests showed that only the lipase produced by A. terreus was safe for NIH-3T3 fibroblast cells. The central composite rotatable design showed the agitation time influenced the enzyme activity response. According to the results, the enzyme produced by the fungus A. terreus is a promising and safe product for research into developing new cosmetic products.

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1. Fourier Transform Infrared Spectroscopy (FTIR): (a): Silica gel; (b): Aspergillus terreus lipase produced immobilized; (c): Aspergillus terreus lipase produced free; (d): commercial lipase from Rhizopus oryzae.
Fig 2
Fig 2. Scanning Electron Microscopy for Silica Gel and Lipases: (A) silica gel magnification 100x; (B) silica gel magnification 250x; (C) silica gel 500x magnification (D) immobilized lipase from Aspergillus terreus produced 500x magnification; (E) commercial lipase from Rhizopus oryzae magnification 500x.
Fig 3
Fig 3. X-ray diffraction: (A) silica gel; (B) immobilized Aspergillus terreus lipase; (C) commercial lipase from Rhizopus oryzae.
Fig 4
Fig 4. (A) Thermogravimetry (TG) curves and (B) Differential Scanning Calorimetry (DSC) curves: (a) Silica gel, (b) immobilized lipase from Aspergillus terreus (c) commercial lipase from Rhizopus oryzae; (d) free Aspergillus terreus lipase.
Fig 5
Fig 5. Assessment of Cellular Viability of NIH-3T3 Fibroblasts.
(A) free Aspergillus terreus lipase dissolved in D10 medium, (B) free Aspergillus terreus lipase dissolved in ethanol, (C) commercial lipase from Rhizopus oryzae, (D) silica gel, (E) immobilized Aspergillus terreus lipase. * Statistically significant difference (p < 0.05) of the control using one-way ANOVA followed by Tukey post-test.
Fig 6
Fig 6. Relative activity at different temperatures (A) and pH (B).
*Statistically significant difference (p < 0.05) of the control using one-way ANOVA followed by Tukey post-test.
Fig 7
Fig 7. Relative activity in different metal ions, EDTA and surfactants.
*Statistically significant difference (p < 0.05) of the control using one-way ANOVA followed by Tukey post-test.
Fig 8
Fig 8. Pareto diagram for response droplet size (A), PDI (B), pH (C) and Zeta Potential (D).
Fig 9
Fig 9. Response surface for the dependent variable zeta potential (A) and enzymatic activity (B) as a function of time and enzyme concentration (%).
Fig 10
Fig 10. Formulation containing lipase.
See this image and copyright information in PMC

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Supplementary concepts