Purification and partial characterization of a thermo-halostable protease produced by Geobacillus sp. strain PLS A isolated from undersea fumaroles

Abstract

The growing industrial demand for stable proteases has driven this study to purify and partially characterize a protease from a bacterial strain isolated from undersea fumaroles. Phylogenetic analysis of the 400bp conserved area of the 16S rRNA gene indicated that the isolate was related to Geobacillus thermoleovorans strain SGAir 0734. Purification by ammonium sulfate precipitation and anion exchange chromatography produced 118-fold purity. The optimum activity (646 U mL−1) of the pure enzyme was observed at 60 °C, pH 7 and with 5M sodium chloride addition. The enzyme retained 73% of its activity when in 50% n-hexane, while the activity was only 40% of the control when in 50% ethyl acetate. The enzyme was tested for its leather dehairing capability. It only caused a slight dehairing and produced soft leather. The enzyme may be applied in skin rejuvenation, wrinkle-smoothing, and high-quality suede production industries.