Characterization of keratinase from Chryseobacterium camelliae Dolsongi-HT1 and efficacy on skin exfoliation.

Summary

A secreted keratinase from Chryseobacterium camelliae Dolsongi-HT1 effectively decomposed human skin keratin and exfoliated the stratum corneum in reconstituted skin models with less abrasion than chemical methods. The enzyme (iHT1) was identified, recombinantly expressed in Bacillus subtilis, and retained high activity across 30–60 °C with an optimal pH of 8.

Key Findings

• C. camelliae Dolsongi-HT1 secretes a keratinolytic enzyme that decomposes human skin keratin and efficiently exfoliates the stratum corneum in reconstituted skin models.
• Enzymatic exfoliation with HT1 was less abrasive and did not damage the epidermal layer compared with common chemical exfoliants.
• The identified enzyme (iHT1) was purified, mass-spectrometry characterized, recombinantly expressed in Bacillus subtilis, and showed broad thermal activity (30–60 °C) with optimal pH 8.

Clinical Implications

If safety and tolerability are confirmed clinically, keratinase-based exfoliants could provide gentler options for patients with sensitive skin or barrier impairment, reducing risks associated with chemical peels.

Limitations

• No in vivo human clinical trials; safety and irritation profiles remain untested in participants.
• Long-term effects on skin barrier function and microbiome were not assessed.

Future Directions

Conduct dose-ranging human trials assessing irritation, sensitization, barrier recovery, and comparative efficacy versus alpha/beta-hydroxy acids; optimize formulation and delivery.