Abstract

Cardiac disorders such as acute myocardial infarction, embolism and stroke are primarily attributed to excessive fibrin accumulation in the blood vessels, usually consequential in thrombosis. Numerous methodologies including the use of anti-coagulants, anti-platelet drugs, surgical operations and fibrinolytic enzymes are employed for the dissolution of fibrin clots and hence ameliorate thrombosis. Microbial fibrinolytic enzymes have attracted much more attention in the management of cardiovascular disorders than typical anti-thrombotic strategies because of the undesirable after-effects and high expense of the latter. Fibrinolytic enzymes such as plasminogen activators and plasmin-like proteins hydrolyse thrombi with high efficacy with no significant after-effects and can be cost effectively produced on a large scale with a short generation time. However, the hunt for novel fibrinolytic enzymes necessitates complex purification stages, physiochemical and structural-functional attributes, which provide an insight into their mechanism of action. Besides, strain improvement and molecular technologies such as cloning, overexpression and the construction of genetically modified strains for the enhanced production of fibrinolytic enzymes significantly improve their thrombolytic potential. In addition, the unconventional applicability of some fibrinolytic enzymes paves their way for protein hydrolysis in addition to fibrin/thrombi, blood pressure regulation, anti-microbials, detergent additives for blood stain removal, preventing dental caries, anti-inflammatory and mucolytic expectorant agents. Therefore, this review article encompasses the production, biochemical/structure-function properties, thrombolytic potential and other surplus applications of microbial fibrinolytic enzymes.

Highlights

  • Cardiovascular diseases (CVDs) for patients with myocardial infarct, hypertension, hyperlipidaemia, diabetes mellitus, stenocardia or coronary heart disease are dominant causes in the ensuing upsurge of mortality worldwide [1,2,3]

  • Fibrinolytic enzymes (EC 3.4.) of exogenic origin, based on their in vivo working mechanisms are currently distinguished into two categories: plasminogen activators (PAs) and plasmin-like enzymes [16] (Figure 1)

  • We will shed light on recent technological advances that facilitate the production of microbial fibrinolytic enzymes along with their properties, thrombolytic potential and additional unconventional applications

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Summary

Introduction

Cardiovascular diseases (CVDs) for patients with myocardial infarct, hypertension, hyperlipidaemia, diabetes mellitus, stenocardia or coronary heart disease are dominant causes in the ensuing upsurge of mortality worldwide [1,2,3]. Fibrinolytic enzymes (EC 3.4.) of exogenic origin, based on their in vivo working mechanisms are currently distinguished into two categories: plasminogen activators (PAs) and plasmin-like enzymes [16] (Figure 1). The structural-functional elucidation of enzymes is essential to study their mechanism of action and commercialisation [24] Regardless of their enormous uses, fibrinolytic enzymes exhibit several inadequacies such as low fibrin specificity, short half-life span, allergic reactions, resistance to repercussion and higher therapeutic dosage with increased risk of bleeding complications [5,17]. We will shed light on recent technological advances that facilitate the production of microbial fibrinolytic enzymes along with their properties, thrombolytic potential and additional unconventional applications

Microbial Fibrinolytic Enzymes
Process Optimisation Techniques
Recovery and Purification of Fibrinolytic Enzymes
Physicochemical Characterisation of Microbial Fibrinolytic Enzymes
45–60 KDa pH 9
Structural-Functional Attributes
Thrombolytic Potential of Microbial Fibrinolytic Enzymes
In Vitro Fibrinolytic Assays
In Vivo Thrombolytic Assays
Other Miscellaneous Applications of Microbial Fibrinolytic Enzymes
Microbial Fibrinolytic Enzymes in Clinical Practices and Food Sector
Industrial Applications of Microbial Fibrinolytic Enzymes
Findings
10. Conclusions

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