Related Experiment Video
Updated: Jul 16, 2026

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
Published on: January 17, 2025
Enzymatic Fructosylation of EGCG Significantly Enhances Its Stability for Skin Barrier Repair and Anti-Aging
Xiaojun Zhang1, Bohan Yang1, Qingna Gong1
1Key Laboratory of Synthetic and Biological Colloids, Ministry of Education, School of Chemical & Material Engineering, Jiangnan University, Wuxi 214122, China.
Abstract:
(-)-Epigallocatechin gallate (EGCG) possesses potent bioactivities but its applications in functional cosmetics is severely limited by its poor water solubility and chemical instability. To overcome these challenges, this study engineered a recombinant levansucrase from Vibrio natriegens to catalyze the transfructosylation of EGCG. The conversion rate of EGCG to fructoside reached 65.59%. The purified product was unequivocally identified as EGCG-1F, with a fructosyl group linked to the 3'-hydroxyl group. Compared to pristine EGCG, EGCG-1F exhibited remarkably enhanced water solubility (96.6-fold that of EGCG) and aqueous stability under acidic and thermal conditions. Biological evaluation revealed that EGCG-1F significantly enhanced HaCaT cell migration, upregulated the expression of basement membrane-associated collagens in ultraviolet B-damaged HaCaT cells, and modulated ultraviolet A-induced senescence in human dermal fibroblasts by type I collagen, type III collagen and matrix metalloproteinase-1 balance. This study demonstrates that enzymatic fructosylation is an effective approach to generate a stable and safe EGCG derivative with potential applications in skin barrier repair and anti-aging functional cosmetics.