Author(s)

Jake F. Wang ¹, Doris Dai ¹, Bella Song ¹, Waifun Mok ¹

Affiliation(s)

¹ Biowell R&D Center, Eternal Grace Pte. Ltd, Singapore

Corresponding Author

Doris Dai

ABSTRACT

Superoxide dismutase (SOD) is an essential antioxidant enzyme that catalyzes the conversion of superoxide radicals into oxygen and hydrogen peroxide, playing a crucial role in reducing oxidative stress. This study focuses on Cryptococcus albidosimilis, a polar yeast with high SOD activity, isolated from Antarctic soil. This yeast exhibits impressive resistance to cold, ultraviolet radiation, and oxidative stress, positioning it as a promising source of stable SOD. Our research characterizes C. albidosimilis SOD, revealing activity levels of about 3000 U/mg, significantly higher than those of conventional yeasts. Notable features include enhanced structural stability, retaining 80% activity under simulated gastric conditions and sustaining 90% activity at 45°C for up to 30 hours. Additionally, the unique molecular structure of this enzyme enhances its resilience against environmental stressors. In conjunction with the SOD analysis, we conducted an exclusive experiment at Biowell's laboratory to evaluate the potential of our proprietary Pure-Glo whitening composition, which incorporates Cryptococcus albidosimilis SOD along with glutathione, glacial water extract, and white tomato extract. This formulation demonstrated a significant ability to inhibit MITF (Microphthalmia-Associated Transcription Factor) gene signaling, a critical regulatory factor in melanin production, achieving a 67% inhibition rate. This breakthrough further confirms the effectiveness of Pure-Glo as a targeted skin whitening agent that operates at the genetic level.

KEYWORDS

Superoxide Dismutase, Polar Yeast, Antioxidant, Skincare

CITE THIS PAPER

Jake F. Wang, Doris Dai, Bella Song, Waifun Mok, Study on the High-Activity Superoxide Dismutase of the Polar Yeast Cryptococcus albidosimilis: From Extreme Survival to Functional Skincare. Journal of Enzyme Engineering (2025) Vol. 2: 1-6. DOI: http://dx.doi.org/10.23977/enzyme.2025.020101.

REFERENCES

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