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THERMUS THERMOPHILUS PUTATIVE ESTERASE.

Insufficient Data / SKIN CONDITIONING

Thermus Thermophilus Putative Esterase is an enzyme derived from the extremophilic bacterium Thermus thermophilus. It precisely catalyzes the hydrolysis of ester bonds, effectively breaking down lipids such as triglycerides, particularly those with water-soluble, short acyl chains (fewer than 10 carbons).

Enzyme Lipid-degrading agent Skin conditioning Antioxidant (potential, based on related ferments) Anti-inflammatory (potential, based on related ferments)

Science

As a specific enzyme, Thermus Thermophilus Putative Esterase primarily functions by hydrolyzing ester bonds, leading to the degradation of lipids, including various triglycerides. While direct skin-specific mechanisms for the isolated putative esterase have not been thoroughly elucidated in clinical studies, related Thermus thermophilus ferments are well-documented for broader dermal benefits. These benefits include antioxidant and anti-inflammatory properties, the promotion of cellular autophagy, upregulation of key skin structural proteins like collagen and elastin, enhancement of aquaporin-3 and dermal-epidermal junction markers, and inhibition of melanin production. It is important to note that these comprehensive regenerative and protective effects are observed in the context of complex ferments rather than being solely attributed to the isolated esterase.


Research

Low confidence
Effective range N/A
Optimal

N/A


Transparency

Not commonly dusted

Based on available research, there is no indication that Thermus Thermophilus Putative Esterase is frequently included in formulations merely to populate ingredient lists without providing substantial functional benefit.


The Formula

Solubility
Water
Optimal pH 4.5 – 9
0 7 14

Stability

This esterase exhibits robust stability and maintains activity across a wide pH range, typically from pH 4.5 to 9.0, with optimal activity observed at various points within this range (e.g., pH 7.5 for KLEST-3S). It also demonstrates high thermal stability and can remain active in the presence of organic solvents and detergents, suggesting versatility for diverse formulation environments.

Conflicts

  • While the wild-type E34Tt variant of this esterase required detergents (such as CHAPS above its Critical Micelle Concentration) to prevent aggregation, its recombinant variant, KLEST-3S, does not necessitate detergents for optimal activity or stability.
  • Generally, Thermus thermophilus esterases are known for their broad tolerance to surfactants, detergents, divalent cations, and high salinity, indicating good compatibility with many common cosmetic formulation components.

Safety

CIR Status
Not reviewed
Sensitization risk Unknown

No specific safety assessments from regulatory bodies such as CIR, SCCS, or FDA are available for Thermus Thermophilus Putative Esterase as a standalone ingredient. Consequently, its specific sensitization risk and safety profile for use during pregnancy remain unassessed.


Your Skin

Yes Normal
Yes Dry
Yes Oily
Yes Sensitive
Irritancy Unknown
Comedogenicity Unknown

Our Assessment

Insufficient Data

While Thermus Thermophilus Putative Esterase exhibits clear enzymatic activity in breaking down lipids and related Thermus thermophilus ferments demonstrate promising broad skincare benefits, comprehensive clinical efficacy and safety data for the isolated enzyme are currently insufficient for a definitive rating.


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