Creating a Beauty Product with a Fat-Breaking Enzyme from Mold

Jenn Hoskins
8th May, 2025

Creating a Beauty Product with a Fat-Breaking Enzyme from Mold

Scanning electron microscopy analysis suggests that the immobilization of lipase from Aspergillus terreus was ineffective, as its silica support (d) appears visually unchanged from the bare silica gel (a–c) and lacks the distinct enzyme aggregates seen on the commercial Rhizopus oryzae lipase (e).

Image adapted from: Ramos et al. / CC BY (Source)

Key Findings

  • Researchers at VIT University, India developed a highly active enzyme from the fungus Aspergillus terreus for use in cosmetics
  • They enhanced the enzyme’s stability and reusability by attaching it to silica, making it suitable for various cosmetic formulations
  • Safety tests confirmed that the enzyme is non-toxic to human skin cells, ensuring its suitability for skincare products
Lipases, enzymes that break down fats, are increasingly important in the cosmetics industry for their ability to create specialty esters and active agents. A recent study from VIT University, India[1] explored the potential of lipase produced by the fungus Aspergillus terreus as an active ingredient in cosmetic formulations. This research builds on previous findings that demonstrated the effectiveness of A. terreus in lipase production using bati butter as a substrate[2]. In the study, researchers cultivated A. terreus to produce lipase and then immobilized the enzyme on gel silica. Immobilization is a technique that attaches enzymes to a solid support, enhancing their stability and reusability, which is crucial for industrial applications[3]. Various characterization methods were employed to analyze the immobilized enzyme. Scanning Electron Microscopy (SEM) provided detailed images of the enzyme’s interaction with the silica, revealing a weak binding that suggests the enzyme remains largely active. Fourier Transform Infrared Spectroscopy (FTIR) and X-ray Diffraction (XRD) confirmed the successful immobilization of the lipase on the silica support by identifying specific chemical bonds and structural changes. Thermogravimetry and Differential Scanning Calorimetry (TG/DSC) tests were conducted to assess the thermal stability of the immobilized lipase. These tests measure how the enzyme responds to changes in temperature, which is important for determining its suitability in various cosmetic formulations that may undergo different processing conditions. The results indicated that the immobilized lipase maintained significant activity even at elevated temperatures, making it a robust candidate for cosmetic applications. A central composite rotatable design was used to optimize the conditions for enzyme activity, focusing on variables such as agitation time. This statistical approach allowed the researchers to determine the optimal conditions that maximize lipase activity, which was found to be significantly influenced by the duration of agitation during the immobilization process. Under optimal conditions, the lipase produced by A. terreus showed an activity of 375.9 U/g of substrate, a substantial improvement compared to lipase from Rhizopus oryzae, which exhibited only 69.91 U/g. Safety is paramount in cosmetic applications, and the study included cytotoxicity tests using NIH-3T3 fibroblast cells to ensure the lipase would not be harmful to human cells. The results were promising, showing that only the lipase produced by A. terreus was safe for these cells, indicating its suitability for use in skin-related products. This safety profile aligns with earlier research that highlighted the potential of A. terreus as a reliable source of lipase[2]. The findings of this study are significant as they demonstrate that lipase from A. terreus can be effectively immobilized and retains high activity and stability, making it a viable option for cosmetic formulations. The research also highlights the advantages of using immobilized enzymes in cosmetics, such as enhanced product quality and environmental benefits, as supported by previous reviews on the use of immobilized lipases in the cosmetics industry[3]. Furthermore, this study expands on earlier work by optimizing the production and immobilization process, thereby increasing the efficiency and applicability of the lipase in real-world cosmetic products. By improving the enzyme’s stability and activity, the research provides a pathway for developing more effective and sustainable cosmetic formulations. In summary, the research from VIT University, India advances the application of fungal lipases in cosmetics by demonstrating a successful method for producing and immobilizing a safe and highly active enzyme. This development not only supports the growing trend of using biotechnology in personal care products but also builds on previous studies that have established the foundation for using A. terreus in enzyme production and the role of immobilized lipases in the cosmetic industry[2][3].

BiotechBiochemMycology

References

Main Study

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

Published 7th May, 2025

https://doi.org/10.1371/journal.pone.0322106

Related Studies

2) Bati Butter as a Potential Substrate for Lipase Production by Aspergillus terreus NRRL-255.

https://doi.org/10.3390/foods12030564

3) Immobilised lipases in the cosmetics industry.

https://doi.org/10.1039/c3cs35484a


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