Abstract
In this study, we explored a novel dehairing process for sheepskins. We used thioredoxin (Trx) from Bacteroides fragilis as a disulfide reductase to minimize skin damage. The thioredoxin expression level reached 88 mg/mL in Escherichia coli, with an activity of 1.178 U/mg, having the potential for industrial application. Thioredoxin promoted keratin hydrolysis and its induction of the enzymatic hydrolysis of hair was 417.817 % higher than that promoted by protease alone. Thioredoxin exhibited better dehairing effects compared with dehairing using only proteases or proteases combined with beta mercaptoethanol (BME). Additionally, thioredoxin promoted wool hydrolysis but did not cause excessive damage to the sheep skin surface. These results indicated that thioredoxin is a disulfide bond reductase that effectively addresses the challenges of protease dehairing and skin damage.
| Original language | English |
|---|---|
| Article number | 149658 |
| Journal | International Journal of Biological Macromolecules |
| Volume | 337 |
| DOIs | |
| State | Published - Jan 2026 |
Keywords
- Disulfide reductase
- Hair keratin
- Keratin enzymatic hydrolysis
- Skin dehairing
- Thioredoxin