Abstract
Enzymes are fascinating the researchers because of their enormous power of catalysis and eco-friendly nature. In biotechnological processes, diversity of microbes is studied, and different metabolic reactions entitle a potential repository that direct valuable production of desirable products. Although tremendous scientific and technological advances have been made by researchers and industrial enzyme producers, and despite the large flow of data on bacterial proteases, little data is currently available on the purification and characterization of proteases and keratinases from B. safensis. Accordingly, the present study reports on the purification and biochemical characterization of a novel detergent-stable protease (SAPRH) from B. safensis strain RH12 isolated from offshore sediment in the Gulf of Gabes (Tunisia). A novel extracellular protease (SAPRH) was hyper-produced (9,000 U/mL) from Bacillus safensis RH12. The enzyme was purified to homogeneity using salt-precipitation, heat-treatment, and FPLC anion-exchange chromatography. The purified enzyme is a monomer of molecular mass of ~28 kDa. The NH2-terminal 23 amino-acid sequence of SAPRH showed high homology with those of Bacillus-proteases. SAPRH showed optimal activity at pH 9 and 60°C. It is strongly inhibited by PMSF and DFP, showing that it belongs to the serine-proteases family. Moreover, SAPRH was extremely stable at a broad range of temperature and pH retaining 85% of its activity at 50°C and 75% at pH 11. The enzyme exhibited excellent-stability and compatibility with surfactants and commercial detergents, showing 90% stability with SDS and 100% stability with Class commercial laundry detergent. One of the distinguishing properties is its catalytic efficiency, which is higher than that of Alcalase 2.5 L, type DX (commercial enzyme) and SAPB from B. pumilus strain CBS. Interestingly, the results of the wash performance analysis demonstrated considerably good de-staining at 40°C for 30 min with low supplementation (500 U/mL). Accordingly, such protease can be considered as a good detergent-additive in detergent industry.
Highlights
Enzymes are fascinating the researchers owing to their enormous power of catalysis and eco-friendly nature
The present study reports on the purification and biochemical characterization of a novel detergent stable protease (SAPRH) from Bacillus safensis strain RH12 isolated from offshore sediment in the Gulf of Gabes (Tunisia)
All the data obtained with regard to the physiological and biochemical properties of the isolate, strongly confirmed that the RH12 strain belonged to the Bacillus genus
Summary
Enzymes are fascinating the researchers owing to their enormous power of catalysis and eco-friendly nature. The techniques and computational tools have immensely developed keeping pace with the cutting-edge industries to meet the growing demands. Techniques such as protein engineering helps in the development of quality products by mutating the amino acids in order to make more stable and efficient product (Kumar et al, 2017). The present study reports on the purification and biochemical characterization of a novel detergent stable protease (SAPRH) from Bacillus safensis strain RH12 isolated from offshore sediment in the Gulf of Gabes (Tunisia). It provides basic information on the potential use of SAPRH as a prospective candidate for future applications in detergent formulations mainly with Class, a commercial liquid laundry detergent from the local company JMAL (EJM)
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