Work

Production, optimization, and purification of serratiopeptidase from Bacillus siamensis found in marine sediments

Year: 2026

Type: article

Abstract: Serratiopeptidase is a proteolytic enzyme with significant clinical applications, specifically acting as a potent anti-inflammatory agent. The current study focuses on the optimization of different process parameters for the enhanced production of serratiopeptidase from marine Bacillus siamensis . The effect of pH, metal ions, surfactants, and inhibitors on enzyme activity was also analyzed. The enzyme was purified by ammonium sulfate precipitation, dialysis, and gel filtration chromatography. Growth kinetics of the bacterial strain showed a maximum of 3.449 U/mL of enzyme production at 18 h. The maximum growth rate and enzyme activity were obtained when the optimized medium was supplemented with lactose as the carbon source (1.779 U/mL) and yeast extract as the nitrogen source (1.807 U/mL), at a pH of 7.2 (1.589 U/mL) and an inoculum size of 250 μL (2.5 × 10 7 CFU/mL; 2.87 U/mL), respectively. The enzyme activity was highly stable at pH 6 (0.32 U/mL), in the presence of 20 mM CaCl₂ (0.45 U/mL), and 20 mM MgSO 4 (5.5 U/mL). After purification of the protein, a 3.6-fold increase in the specific activity of the enzyme was attained. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) analysis showed a band of molecular size of 50 kDa, confirming the presence of the anti-inflammatory protein. Fourier transform infrared spectroscopy (FTIR) analysis revealed the molecular and structural integrity of the protein. Serratiopeptidase produced from marine Bacillus siamensis was found to be highly stable and effective. The findings of this study support the potential of this anti-inflammatory protein as a potent candidate for therapeutic and industrial applications.

Source: Frontiers in Microbiology

DOI: 10.3389/fmicb.2026.1817064