Novel serine keratinase from Caldicoprobacter algeriensis exhibiting outstanding hide dehairing abilities

• A novel keratinase (called KERCA) from C. algeriensis strain TH7C1T was studied.
• KERCA with a molecular mass of 33246.10-Da was purified and characterized.
• The optimum pH and temperature values for activity were pH 7 and 50 °C, respectively.
• KERCA displayed higher levels of hydrolysis and catalytic efficiency than KERQ7.
• KERCA is a potential candidate for animal hide dehairing in the leather processing.

The current paper reports on the purification of an extracellular thermostable keratinase (KERCA) produced from Caldicoprobacter algeriensis strain TH7C1T, a thermophilic, anaerobic bacterium isolated from a hydrothermal hot spring in Algeria. The maximum keratinase activity recorded after 24-h of incubation at 50 °C was 21000 U/ml. The enzyme was purified by ammonium sulfate precipitation-dialysis and heat treatment (2 h at 50 °C) followed by UNO Q-6 FPLC anion exchange chromatography, and submitted to biochemical characterization assays. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI–TOF/MS) analysis revealed that the purified enzyme was a monomer with a molecular mass of 33246.10 Da. The sequence of the 23 N-terminal residues of KERCA showed high homology with those of bacterial keratinases. Optimal activity was achieved at pH 7 and 50 °C. The enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP), which suggests that it belongs to the serine keratinase family. KERCA displayed higher levels of hydrolysis and catalytic efficiency than keratinase KERQ7 from Bacillus tequilensis strain Q7. These properties make KERCA a potential promising and eco-friendly alternative to the conventional chemicals used for the dehairing of goat, sheep, and bovine hides in the leather processing industry.