Production of fibrinolytic protease fromStreptomyces lusitanusisolated from marine sediments

Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity

“…These enzymes possess potential efficacy for health augmentation and nutraceutical use, and their application could prevent cardiovascular diseases effectively [28]. Marine microorganisms producing fibrinolytic enzymes, including bacteria (Streptomyces lusitanus [43], Streptomyces radiopugnans VITSD8 [44], Streptomyces violaceus VI-TYGM [45], Pseudomonas aeruginosa KU1 [46,47], Alteromonas piscicida [48], Pseudoalteromonas sp. IND11 [49], bacterial strain GPJ3 [50], Marinobacter aquaeolei MS2-1 [51], Bacillus flexus [52], Bacillus subtilis [53], Bacillus subtilis HQS-3 [54], Bacillus vallismortis [55], Bacillus subtilis D21-8 [56], Bacillus pumilus BS15 [29], Bacillus subtilis WR350 [57], Bacillus subtilis JS2 [58], Bacillus velezensis BS2 [59], Bacillus subtilis ICTF-1 [41], Shewanella sp.…”

“…Currently, several approaches have been used for separating and purifying fibrinolytic enzymes from marine microorganisms (Table 2). These approaches involved the extraction of bacteria with aqueous buffer solution as first step, followed by a concentration/precipitation step using acetone or ammonium sulfate and dialysis [41,43,44,52,62,65,66]. As shown in Table 2, the use of ammonium sulfate for protein precipitation is preferred, as it is a low-cost reagent, highly soluble in water and it is able to stabilize proteins and enzymes [41,43,44,47,52,62,65].…”

“…These approaches involved the extraction of bacteria with aqueous buffer solution as first step, followed by a concentration/precipitation step using acetone or ammonium sulfate and dialysis [41,43,44,52,62,65,66]. As shown in Table 2, the use of ammonium sulfate for protein precipitation is preferred, as it is a low-cost reagent, highly soluble in water and it is able to stabilize proteins and enzymes [41,43,44,47,52,62,65]. Further purification is carried out by employing different chromatographic steps (Table 2).…”

“…The enzyme had a molecular mass of Table 3 provides a detailed overview of the significant physicochemical characteristics of marine microbial fibrinolytic enzymes, including molecular mass, optimal pH and temperature. The molecular mass of the purified marine microbial fibrinolytic enzymes varied significantly, ranging from as low as 21 kDa in an actinomycete (Streptomyces lusitanus) [43] to as high as 72 kDa in a cyanobacterium (Arthrospira platensis) [65]. Most marine microbial fibrinolytic enzymes have optimum pH fluctuating from neutral to alkaline values, ranging from 6 [65] to 7 [43,44,62] and from 8 [29,52,[58][59][60] to 9 [41,75].…”

“…The molecular mass of the purified marine microbial fibrinolytic enzymes varied significantly, ranging from as low as 21 kDa in an actinomycete (Streptomyces lusitanus) [43] to as high as 72 kDa in a cyanobacterium (Arthrospira platensis) [65]. Most marine microbial fibrinolytic enzymes have optimum pH fluctuating from neutral to alkaline values, ranging from 6 [65] to 7 [43,44,62] and from 8 [29,52,[58][59][60] to 9 [41,75]. The optimal temperature of marine microbial fibrinolytic enzymes ranges between 33 • C (Streptomyces radiopugnans VITSD8) [44] to 60 • C (Bacillus flexus) [52].…”