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Industrial Applications of Bacterial Enzymes
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Nattokinase, a serine protease of the subtilisin family, despite its name, is actually not a kind of kinase; it is used for the inactivation of plasminogen activator inhibitor-I [PAI-I] by displaying a strong fibrinolytic action when exposed to human blood clots [57]. Dissimilar to different proteins, they are not inactivated or digested if ingested orally and passed through the gut [58]. Nattokinase also exhibits maximum stability and is economically feasible and effective, and it can be obtained from B. subtilis natto [59].
Purification, biochemical, and thermal properties of fibrinolytic enzyme secreted by Bacillus cereus SRM-001
Published in Preparative Biochemistry and Biotechnology, 2018
Manoj Kumar Narasimhan, Selvarajan Ethiraj, Tamilarasan Krishnamurthi, Mathur Rajesh
The currently available fibrinolytic agents are plasminogen activators, which convert the inactive plasminogen (zymogen) to active plasmin.[5] Plasmin is a serine protease in the blood that hydrolyzes fibrin clots and reverses thrombosis. Plasminogen activators can be classified as tissue-type plasminogen activators,[6] urokinase-type plasminogen activators[7], and bacterial plasminogen activators.[8] It has also been reported that the widely used plasminogen activators in fibrinolytic therapy possess relatively poor fibrin specificity with unacceptable side effects such as internal hemorrhage and are neurotoxic at high concentrations.[9,10] In human blood, there are several factors that may influence fibrin clot formation, but it can only be reversed by the action of the plasmin. Fibrinolytic enzymes with thrombolytic properties have been purified from diverse sources such as microorganisms,[111213141516] snake venom,[17] earthworm,[18,19] Polychaete worm,[20] and mushroom.[21] Initial reports have demonstrated fibrinolytic enzyme isolation from fermented food. For example, nattokinase is a commercially available and orally administered fibrinolytic enzyme reported to be isolated from natto, a Japanese food fermented of soybeans by Bacillus natto.[22] Subtilisin DFE and DJ-4 are fibrinolytic enzymes produced by fermentation of Chinese and Korean food, respectively, by Bacillus sp.[23,24] However, in recent years, fibrinolytic enzyme production has also been reported from other sources such as Streptomyces megasporous,[25]Pleurotus eryngii,[26]Bacillus sp. nov. SK006,[27]Bacillus licheniformis KJ-31,[28]Bacillus subtilis TP-6,[29] and Paenibacillus polymyxa EJS-3.[30] Current research interest in fibrinolytic agents centers on the discovery of plasmin-like microbial proteases with high fibrin specificity. The number and type of downstream processing steps dictates the cost of bioproducts such as therapeutic enzymes. Hence a facile and economical purification strategy is necessary to isolate the bioproducts of interest.