Purification, biochemical characterization and fibrinolytic potential of proteases produced by bacteria of the genus Bacillus: a systematic literature review

Leite, Arthur Hipólito Pereira; Silva, Ítalo Henrique Alves da; Pastrana, Lorenzo; Nascimento, Thiago Pajeú; Telles, Adriana Maria da Silva; Porto, Ana Lúcia Figueiredo

doi:10.1007/s00203-022-03134-y

Cited by 7 publications

(3 citation statements)

References 80 publications

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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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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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“…It is noteworthy that enzymes with fibrinolytic activity are found in marine animals as well as in microorganisms. Marine microorganisms of the genus Bacillus and Aspergillus are considered an important source of fibrinolytic enzyme production [4,[14][15][16]. The fibrinolytic enzymes derived from the fungus demonstrate promising thrombolytic and anticoagulant activities [17].…”

Section: Introductionmentioning

confidence: 99%

Purification and Properties of a Plasmin-like Marine Protease from Clamworm (Perinereis aibuhitensis)

Jiang,

Zhang,

Zhang

et al. 2024

Marine Drugs

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Marine organisms are a rich source of enzymes that exhibit excellent biological activity and a wide range of applications. However, there has been limited research on the proteases found in marine mudflat organisms. Based on this background, the marine fibrinolytic enzyme FELP, which was isolated and purified from clamworm (Perinereis aibuhitensis), has exhibited excellent fibrinolytic activity. We demonstrated the FELP with a purification of 10.61-fold by precipitation with ammonium sulfate, ion-exchange chromatography, and gel-filtration chromatography. SDS-PAGE, fibrin plate method, and LC–MS/MS indicated that the molecular weight of FELP is 28.9 kDa and identified FELP as a fibrinolytic enzyme-like protease. FELP displayed the maximum fibrinolytic activity at pH 9 (407 ± 16 mm2) and 50 °C (724 ± 27 mm2) and had excellent stability at pH 7–11 (50%) or 30–60 °C (60%), respectively. The three-dimensional structure of some amino acid residues of FELP was predicted with the SWISS-MODEL. The fibrinolytic and fibrinogenolytic assays showed that the enzyme possessed direct fibrinolytic activity and indirect fibrinolysis via the activation of plasminogen; it could preferentially degrade Aα-chains of fibrinogen, followed by Bβ- and γ-chains. Overall, the fibrinolytic enzyme was successfully purified from Perinereis aibuhitensis, a marine Annelida (phylum), with favorable stability that has strong fibrinolysis activity in vitro. Therefore, FELP appears to be a potent fibrinolytic enzyme with an application that deserves further investigation.

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“…Research on brinolytic enzymes derived from bacteria, especially Bacillus, has been interesting for several decades (Bode et al 1996; Leite et al 2022). Several species of Bacillus, such as B. licheniformis (Buiting et al 1990) (Ali and Bavisetty 2020).…”

Section: Introductionmentioning

confidence: 99%

Characteristics of Thermo-stable Serine Peptidase Vpr from Endophytic Bacillus cereus strain InaCC-B1657

Hastuty,

Mangunwardoyo,

Suhartono

et al. 2024

Preprint

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Bacterial endophytes are a promising source of novel fibrinolytic enzymes with unique metabolic pathways and desirable characteristics that may not be present from conventionally explored sources. This study aimed to characterize fibrinolytic enzymes from selected endophytic bacteria isolated from papaya (Carica papaya L.) leaves and the genes encoding the enzymes. A strain BFP1 (InaCC-B1657) that showed the highest fibrinolytic activity was identified as Bacillus cereus based on the phylogenetic analysis of the 16S rRNA sequence. The enzyme exhibited optimum activity at 50°C and pH 7.0, and remained stable until 80°C and pH 6–10 for 24 h. The assay of metal ions and inhibitors on the fibrinolytic enzyme activity found that adding Cu2+ stimulated, while Fe2+ reduced the activity. PMSF and TPCK inhibited the enzyme activity, while adding EDTA and EGTA increased the activity. These suggest that the fibrinolytic enzymes belong to the serine protease group. Of the 21 proteases/peptidases determined from the 5,257,484 base pairs (bp) genome, minor extracellular protease Vpr and S8 family peptidase genes were found related to the fibrinolytic enzyme activity. The Vpr gene has a molecular weight of 98.5 kDa. The subtilase domain (peptidase S8 family) and the catalytic triad subtilase active sites (Asp204, His237, and Ser531) were detected. A prediction of physicochemical characteristics of the Vpr gene showed that the enzyme is hydrophilic and exhibited alkali-halo stability and thermo-stability over a broad range of temperatures.

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Purification, biochemical characterization and fibrinolytic potential of proteases produced by bacteria of the genus Bacillus: a systematic literature review

Cited by 7 publications

References 80 publications

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

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

Purification and Properties of a Plasmin-like Marine Protease from Clamworm (Perinereis aibuhitensis)

Characteristics of Thermo-stable Serine Peptidase Vpr from Endophytic Bacillus cereus strain InaCC-B1657

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