Purification and characterization of protease enzyme from actinomycetes and its cytotoxic effect on cancer cell line (A549)

Proteases are the most important group of the enzymes produced commercially and industrial purpose[1,2]. They have extensive applications in a range of industrial products and processes including detergents, food, pharmaceuticals and leather[3,4]. They are classified into various groups such as alkaline protease, serine protease, cystein protease, aspartic protease and metallo protease[5]. Protease constitutes one of the most important groups of industrial enzymes, accounting for at least 25% of the total enzyme sales, with two-thirds of the proteases produced commercially being of microbial origin. In recent years a number of studies have been conducted to characterize protease from different microorganisms. The production of proteases by microorganisms is greatly influenced by media components, especially carbon and nitrogen sources, and by physical factors such as temperature, pH, incubation time, agitation and inoculum density. Although protease production is an inherent property of all organisms, only those microbes that produce a substantial amount of extracellular protease have been exploited commercially. They also include species that are able to degrade many macromolecules such as lipids, starch, chitin, pectin, and proteins[6]. While proteases from bacteria are extensively characterized, similar attention has not been paid to actinomycetes. Actinomycetes are Gram-positive, mycelium-forming soil bacteria that include many species considered to be among the most important producers of antibiotics[7]. However, the present knowledge concerning proteases of actinomycetes is much less than that of fungi and other bacteria. Proteases produced by actinomycetes are the most ARTICLE INFO ABSTRACT