Novel subtilase discovered through analytical chemistry

Scientists have discovered a novel subtilase through analytical chemistry that could have potential uses in a number of biotechnological applications.

Microbial proteases are enzymes with a high commercial value, the market share largely taken by subtilases or alkaline proteases of the Bacillus species, but as such there is always interest in the development of further novel proteases with unique properties.

In the study, published by BMC Biotechnology, the team of scientists isolated a novel member of the subtilase superfamily from Virgibacillus sp. SK37, a protease producing bacterium found following the fermentation of Thai fish sauce.

Using analytical chemistry methods, the team found that the novel subtilase has thermal stability, metal-dependant and was sensitive towards reducing agents, urea, and SDS but relatively stable up to five per cent of H2O2.

Naming their new discovery as alkaline serine protease-X (AprX), the scientists suggested that its stability towards H2O2 and its halo- and thermo-tolerant properties make it an attractive enzyme for a number of biotechnological applications.