Purification, physicochemical properties, and statistical optimization of fibrinolytic enzymes especially from fermented foods: A comprehensive review

Ali, Ali Muhammed Moula; Bavisetty, Sri Charan Bindu

doi:10.1016/j.ijbiomac.2020.07.303

Cited by 32 publications

(17 citation statements)

References 176 publications

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“…Based on degradation pattern of fibrin and FIB, Velefibrinase should be classified as α/β-fibrinogenase. On the one hand, the K m of Velefibrinase to fibrin was 8.57 μmol/L (2.91 g/L), which was lower than that of Bvsp (3.19 g/L) which was from a marine bacterium B. vallismortis , and JP-Ⅰ (0.43 mmol/L), Ⅱ (0.69 mmol/L) which was from a Korean traditional fermented food, but higher than that of lumbrokinase (2.67 g/L) [ 39 , 40 ]. On the other hand, the K m of Velefibrinase to FIB was 18.16 μmol/L (6.17 g/L), which was higher than FIB content in human plasma (2.4–5.0 g/L) and that of nattokinase (2.19 g/L) [ 2 ].…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Zhou¹,

Chen²,

Yu³

et al. 2022

Microorganisms

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Fibrinolytic enzymes are the most effective agents for the treatment of thrombotic diseases. In the present study, we purified and characterized an extracellular fibrinolytic serine metalloprotease (named Velefibrinase) that is produced by marine Bacillus velezensis Z01 and assessed its thrombolysis in vivo. SDS-PAGE and MALDI-TOF-MS analyses showed that the molecular mass of Velefibrinase was 32.3 KDa and belonged to the peptidase S8 family. The optimal fibrinolytic activity conditions of Velefibrinase were 40 °C and pH 7.0. Moreover, Velefibrinase exhibited high substrate specificity to fibrin, and a higher ratio of fibrinolytic/caseinolytic (1.48) values, which indicated that Velefibrinase had excellent fibrinolytic properties. Based on the degradation pattern of fibrin and fibrinogen, Velefibrinase could be classified as α/β-fibrinogenase. In vitro, Velefibrinase demonstrated efficient thrombolytic ability, anti-platelet aggregation, and amelioration of blood coagulation (APTT, PT, TT, and FIB), which were superior to those of commercial anticoagulant urokinase. Velefibrinase showed no hemolysis for erythrocyte in vitro and no hemorrhagic activity in vivo. Finally, Velefibrinase effectively prevented mouse tail thrombosis in a dose-dependent (0.22–0.88 mg/kg) manner. These findings suggested that Velefibrinase has the potential to becoming a new thrombolytic agent.

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Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Zhou¹,

Chen²,

Yu³

et al. 2022

Microorganisms

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“…In the last two decades, several studies have been conducted in the search for new antithrombotic agents from natural sources, characterized by high therapeutic efficacy and low side effects, to be used as supplements or as alternatives to the antithrombotic drugs currently in use. In this regard, several fibrinolytic enzymes from various sources such as fermented products, snake venom, marine species, plants, earthworms, microorganisms and insects have been discovered [ 6 , 7 , 8 , 9 , 10 , 11 ]. In addition, fibrinolytic proteases were also discovered in the fruiting bodies and mycelia of many medicinal or edible mushrooms [ 12 ], including Agrocybe aegerita , Ganoderma lucidum , Armillaria mellea , Tricholoma saponaceum , Cordyceps militaris , Pleurotus ferulae , Pleurotus ostreatus and Pleurotus eryngii [ 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 ].…”

Section: Introductionmentioning

confidence: 99%

Edible Mushrooms as Source of Fibrin(ogen)olytic Enzymes: Comparison between Four Cultivated Species

et al. 2022

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Cardiovascular diseases represent the main cause of death. A common feature of cardiovascular disease is thrombosis resulting from intravascular accumulation of fibrin. In the last years, several fibrinolytic enzymes have been discovered in many medicinal or edible mushrooms as potential new antithrombotic agents. This study aimed to compare the fibrin(ogen)olytic activity of crude extracts from the fruiting bodies of four cultivated edible mushrooms: Lentinula edodes, Pleurotus ostreatus, Pleurotus eryngii, and Agrocybe aegerita. Fibrin(ogen)olytic activity was assessed by fibrin plate, spectrophotometric assay and electrophoretic analysis (SDS-PAGE and zymography). The highest activity was detected for P. ostreatus followed by P. eryngii, L. edodes and A. aegerita. Results indicated that enzymes exhibited maximum activity at pH 6–7 and 30–40 °C, respectively. Enzyme activity was inhibited by serine and metalloprotease inhibitors. We proposed a new index called the Specific Fibrin(ogen)olytic Index (SFI), which allows specification of the proportion of the total proteolytic capacity due to the fibrin(ogen)olytic activity. These data suggest that the extracts from fruiting bodies or powdered mushrooms can be used as functional ingredients for the development of new functional foods that may act as thrombolytic agents responding, at the same time, to the increasing demand for safe, healthy and sustainable food.

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“…7 Several fibrinolytic enzymes have been successively extracted from animals, plants, microbes, and fermented foods. 8 Microorganisms continue to be the primary source for enzyme production due to mass culture viability, substrate specificity, and low production costs. Microbial sources from fermented foods have become quite important especially in the commercial production of fibrinolytic enzymes due to their advantageous qualities, such as high substrate specificity, cheap production cost, and high yield rates.…”

Section: Introductionmentioning

confidence: 99%

“…9 Additionally, fibrinolytic enzymes from microorganisms have been assured for their negligible neg-ative impacts in patients, particularly those with inborn drawbacks. 8 As a result, several microbiological sources, such as actinomycetes, bacteria, algae, and even mushrooms, have yielded fibrinolytic enzymes. 10 Less fibrinolytic strains of filamentous fungi have been mentioned in literature.…”

Section: Introductionmentioning

confidence: 99%

Thrombolytic and anticoagulant efficiencies of purified fibrinolytic enzyme produced from Cochliobolus hawaiiensis under solid‐state fermentation

Abu‐Tahon,

Abdel‐Majeed,

Ghareib

et al. 2023

Biotech and App Biochem

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Cochliobolus hawaiiensis Alcorn Assiut University Mycological Centre 8606 was chosen from the screened 20 fungal species as the potent producer of fibrinolytic enzyme on skimmed‐milk agar plates. The greatest enzyme yield was attained when the submerged fermentation (SmF) conditions were optimized, and it was around (39.7 U/mg protein). Moreover, upon optimization of fibrinolytic enzyme production under solid‐state fermentation (SSF), the maximum productivity of fibrinolytic enzyme was greatly increased recorded a bout (405 U/mg protein) on sugarcane bagasse, incubation period of 5 days, moisture level of 100%, initial pH of salt basal medium 7.8, incubation temperature at 35°C, and supplementation of the salt basal medium with corn steep liquor (80％, v/v). The yield of fibrinolytic enzyme by C. hawaiiensis under SSF was higher than that of SmF with about 10.20‐fold. The purification procedures of fibrinolytic enzyme by ammonium sulfate (70%), gel filtration, and ion‐exchange columns chromatography caused a great increase in its specific activity to 2581.6 U/mg protein with an overall yield of 55.89%, 6.37 purification fold and molecular weight of 35 kDa. Maximal activity was recorded at pH 7 and 37°C. Significant pH stability was recorded at pH 6.6–7.2, and thermal stability was recorded at 33–41°C. The enzyme showed the highest affinity toward fibrin, with Vmax of 240 U/mL and an apparent Km value of 47.61 mmol. Mg2+ and Ca2+ moderately induced fibrinolytic activity, whereas Cu2+ and Zn2+ greatly suppressed the enzyme activity. The produced enzyme is categorized as serine protease and non‐metalloprotease. The purified fibrinolytic enzyme showed efficient thrombolytic and antiplatelet aggregation activities by completely prevention and dissolution of the blood clot which confirmed by microscopic examination and amelioration of blood coagulation assays. These findings suggested that the produced fibrinolytic enzyme is a promising agent in management of blood coagulation disorders.

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Purification, physicochemical properties, and statistical optimization of fibrinolytic enzymes especially from fermented foods: A comprehensive review

Cited by 32 publications

References 176 publications

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Edible Mushrooms as Source of Fibrin(ogen)olytic Enzymes: Comparison between Four Cultivated Species

Thrombolytic and anticoagulant efficiencies of purified fibrinolytic enzyme produced from Cochliobolus hawaiiensis under solid‐state fermentation

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