Pseudoalteromonas agarivorans-derived novel ulvan lyase of polysaccharide lyase family 40: Potential application of ulvan and partially hydrolyzed products in cosmetic industry.

Summary

The authors identify and recombinantly express a novel PL40 ulvan lyase from Pseudoalteromonas agarivorans, characterize its activity (optimal at 35°C, pH 8.0, 2.5 mM NaCl), and confirm ulvan depolymerization. Crucially, they provide the first evidence that ulvan and partially hydrolyzed ulvan inhibit hyaluronidase and elastase—enzymes targeted by anti-aging cosmetics.

Key Findings

• Discovered and recombinantly expressed a novel PL40 ulvan lyase (paul40) from Pseudoalteromonas agarivorans.
• Confirmed ulvan depolymerization using DNS assay, TLC, and GPC; optimal activity at 35°C, pH 8.0, and 2.5 mM NaCl.
• First report that ulvan and partially hydrolyzed ulvan inhibit hyaluronidase and elastase.
• Establishes groundwork for cosmetic applications of ulvan derivatives targeting skin-degrading enzymes.

Clinical Implications

While preclinical, ulvan-derived inhibitors could be developed into topical cosmetic ingredients targeting hyaluronidase/elastase to support skin firmness and reduce wrinkle formation, pending safety and efficacy testing.

Limitations

• Findings are limited to in vitro enzymology; no in vivo dermatologic models or clinical data.
• Specificity, stability in formulations, and safety/toxicity profiles remain to be established.

Future Directions

Evaluate bioactivity in skin models and human studies, elucidate structure–activity relationships of ulvan fragments, and develop scalable, GMP-ready processes for cosmetic-grade ingredients.