Purification and characterization of haloalkaline thermoactive, solvent stable and SDS-induced protease from Bacillus sp.: A potential additive for laundry detergents

An extracellular haloalkaline, thermoactive, solvent stable, SDS-induced serine protease was purified and characterized from an alkali-thermo tolerant strain Bacillus sp. SM2014 isolated from reverse osmosis reject. The enzyme was purified to homogeneity with recovery of 54.4% and purity fold of 64. The purified enzyme was composed of single polypeptide of molecular mass about 71 kDa. The enzyme showed optimum activity at alkaline pH 10 and temperature 60 °C. The km and Vmax for the enzyme was 0.57 mg/ml and 445.23 U/ml respectively. The enzyme showed novel catalytic ability at high pH (10), temperature (60 °C) and salinity (3 M). Moreover, the stability of enzyme in organic solvents (50% v/v) of logP ⩾ 2 signified the prospective of this enzyme for peptide synthesis. The compatibility of the enzyme with surfactants and various detergent matrices together with wash performance test confirmed its potential applicability in laundry industry.

► An extracellular protease is characterized from polyextremotolerant strain.
► The reaction has been catalyzed at pH (10), temperature (60 °C), and salinity (15%).
► Enzyme has functional activity in various organic solvents (50% v/v).
► Enzyme has stability with surfactants and commercial detergents.
► Study showed its substantial role in laundry industry and prospects for peptide synthesis.