Abstract
Production of extracellular alkaline protease by new halotolerant alkaliphilic Bacillus sp. NPST-AK15 isolated from hyper saline soda lakes
Highlights
Proteases (EC 3.4.21) are a large group of hydrolytic enzymes that catalyze the hydrolysis of the proteins by cleavage of the peptide bonds between the amino acid residues in other proteins [1]
Alkaline protease secretion was coherent with the growth pattern, and increased with the increasing growth, which started at the beginning of the exponential phase (8–10 h), and was maximal in the mid stationary phase with the highest activity recorded at 36 h (1263.3 U/mL)
A new potent alkaline protease producing halotolerant alkaliphilic isolate NPST-AK15 was isolated from hyper saline soda lakes of Wadi El-Natrun Valley, located in northern Egypt
Summary
Proteases (EC 3.4.21) are a large group of hydrolytic enzymes that catalyze the hydrolysis of the proteins by cleavage of the peptide bonds between the amino acid residues in other proteins [1]. With high activity and stability in high alkaline range, are interesting for several bioengineering and biotechnological applications Their main application is in the detergent industry, accounting for approximately 30% of the total world enzyme production [6] because the pH of laundry detergents is in the range of. The industrial demand for highly active alkaline proteases with high specificity and stability of pH, temperature, and organic solvents continues to enhance the search for new enzymes [11]. The present study focused on isolation of new alkaline producing alkaliphilic bacteria from hyper saline soda lakes and optimization of the enzyme production. Results: A new potent alkaline protease producing halotolerant alkaliphilic isolate NPST-AK15 was isolated from hyper saline soda lakes, which affiliated to Bacillus sp. NPST-AK15 and its extracellular alkaline protease with salt tolerance signify their potential applicability in the laundry industry and other applications
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