Alkaline Thermo- and Oxidant-Stable Protease from Strain TNP93: Laundry Detergent Formulations

The study aims to produce a detergent-compatible and alkaline thermophilic protease from a strain and to investigate its usability as a detergent bio-additive. The protease-producing bacterium was identified as strain TNP93 according to the 16S rRNA sequence. The bacterium optimally synthesized the protease at 40 °C and pH 10 in 40 h. The raw protease displayed its optimum activity at pH 10 and 60 °C and its stability between pH 6-13 and 30-100 °C for 24 h. The molecular mass of the proteolytic band was estimated to be about 85 kDa. The protease was not inhibited by any of the metal ions used (Ba, Ca, Co, Cu, Mg, Mn, Zn). 97 and 90% of its original activity with 5 mM PMSF and EDTA remained. The activity was measured as 84, 124, and 95%, respectively, in the presence of 1% concentrations of Tween 20, Tween 80, and Triton X-100. In addition, all of its activity was preserved when the enzyme was exposed to 5% HO. The end products of casein were detected as tyrosine, aspartic acid, glycine, and cysteine by thin-layer chromatography. Considering the wash performance analysis, the mix of 1% commercial detergent and enzyme almost removed all of the protein-based stains (blood and egg yolk albumin). These remarkable findings indicate that the alkaline, thermo-, and oxidant-stable TNP93 protease is a valuable candidate for usage as a biological additive in various laundry detergents.