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.
Highlights
Proteases are a group of enzymes that catalyze the hydrolysis of peptide bonds to produce short peptides and amino acids
Considering their significances in industries, this study aims to purify and characterize protease produced by a local microorganism isolated from undersea fumaroles
Sequence alignment to other 16S rRNA genes of the same sequence showed that strain PLS A has a close relationship with Geobacillus thermoleovorans strain SGAir0734 (Figure 1), as they were clustered in the same branch
Summary
Proteases are a group of enzymes that catalyze the hydrolysis of peptide bonds to produce short peptides and amino acids. Proteases can be grouped according to their optimum activity pH, i.e. acidic, neutral, or alkaline proteases [1]. Based on their catalytic mechanism, proteases are grouped to exopeptidase (E.C. 3.4.11–3.4.19) and endopeptidases (E.C. 3.4.21–3.4.24, 3.4.99). Exopeptidases that hydrolyzed proteins from their termini are further grouped into aminopeptidases and carboxypeptidases based on the end locations of hydrolysis, releasing one, two, or three residues. Endopeptidases hydrolyze proteins in the interior [2]
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