Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

Summary

Scientists discovered a special protein-cutting enzyme from oyster mushrooms that works exceptionally well at high temperatures and in harsh cleaning conditions. This enzyme, called SPPS, cuts through protein stains similar to how detergent enzymes work in laundry. The enzyme is more stable and efficient than commonly used commercial enzymes and can withstand organic solvents. This discovery makes it a promising candidate for improving detergent formulations and other industrial applications.

Background

Proteases are hydrolytic enzymes that cleave peptide bonds in proteins and peptides. Serine proteases represent more than one-third of industrial proteases and are highly sought for detergent formulations. Fungi produce extracellular proteases that are easily separated from mycelium, making them attractive for industrial applications.

Objective

To identify, isolate, and characterize a novel alkaline protease (SPPS) from Pleurotus sajor-caju strain CTM10057 and evaluate its potential for industrial applications, particularly in detergent formulations.

Results

SPPS was identified as a 65 kDa monomeric serine protease with optimal activity at pH 9.5 and 70°C. It demonstrated high homology with mushroom proteases, superior hydrolysis levels and catalytic efficiency compared to commercial proteases, and exceptional organic solvent tolerance and detergent stability.

Conclusion

SPPS possesses excellent properties including high thermostability, alkaline activity, detergent compatibility, and organic solvent tolerance, making it a promising candidate for industrial applications, particularly in detergent formulations as a bio-additive.
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