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

Barzkar, Noora; Jahromi, Saeid Tamadoni; Vianello, Fábio

doi:10.3390/md20010046

Cited by 29 publications

(17 citation statements)

References 75 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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“…Moreover, further improvements seem feasible if template genes with fewer homologies with each other are used for family gene shuffling. Family gene shuffling is an efficient method for obtaining diverse mutants, and thus seems an effective alternative for screening samples from various natural environments to isolate microorganisms with strong fibrinolytic activities [ 23 , 24 ]. To sum up, aprEFSM4 has good potential as a source for the mass production of fibrinolytic enzymes for the food and pharmaceutical industries.…”

Section: Resultsmentioning

confidence: 99%

DNA Shuffling of aprE Genes to Increase Fibrinolytic Activity and Thermostability

Zhuang

Jeon

Yoo

et al. 2022

J. Microbiol. Biotechnol.

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Four aprE genes encoding alkaline serine proteases from B. subtilis strains were used as template genes for family gene shuffling. Shuffled genes obtained by DNase I digestion followed by consecutive primerless and regular PCR reactions were ligated with pHY300PLK, an E. coli-Bacillus shuttle vector. The ligation mixture was introduced into B. subtilis WB600 and one transformant (FSM4) showed higher fibrinolytic activity. DNA sequencing confirmed that the shuffled gene (aprEFSM4) consisted of DNA mostly originated from either aprEJS2 or aprE176 in addition to some DNA from either aprE3-5 or aprESJ4. Mature AprEFSM4 (275 amino acids) was different from mature AprEJS2 in 4 amino acids and mature AprE176 in 2 amino acids. aprEFSM4 was overexpressed in E. coli BL21 (DE3) by using pET26b(+) and recombinant AprEFSM4 was purified. The optimal temperature and pH of AprEFSM4 were similar to those of parental enzymes. However, AprEFM4 showed better thermostability and fibrinogen hydrolytic activity than the parental enzymes. The results indicated that DNA shuffling could be used to improve fibrinolytic enzymes from Bacillus sp. for industrial applications.

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“…The difficulties in sampling impede complete exploration of the marine organisms; therefore, it is believed that the habitat can still provide new novel species [ 61 , 62 , 63 ]. Salinity and generally cold and alkaline environments are peculiar features of oceans that influence the life in that habitat which is known for harboring unique catalysts [ 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 , 75 ]. Therefore, potential applications of marine-derived catalysts can easily be conceived.…”

Section: Marine Dextranasementioning

confidence: 99%

Marine Bacterial Dextranases: Fundamentals and Applications

et al. 2022

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Dextran, a renewable hydrophilic polysaccharide, is nontoxic, highly stable but intrinsically biodegradable. The α-1, 6 glycosidic bonds in dextran are attacked by dextranase (E.C. 3.2.1.11) which is an inducible enzyme. Dextranase finds many applications such as, in sugar industry, in the production of human plasma substitutes, and for the treatment and prevention of dental plaque. Currently, dextranases are obtained from terrestrial fungi which have longer duration for production but not very tolerant to environmental conditions and have safety concerns. Marine bacteria have been proposed as an alternative source of these enzymes and can provide prospects to overcome these issues. Indeed, marine bacterial dextranases are reportedly more effective and suitable for dental caries prevention and treatment. Here, we focused on properties of dextran, properties of dextran—hydrolyzing enzymes, particularly from marine sources and the biochemical features of these enzymes. Lastly the potential use of these marine bacterial dextranase to remove dental plaque has been discussed. The review covers dextranase-producing bacteria isolated from shrimp, fish, algae, sea slit, and sea water, as well as from macro- and micro fungi and other microorganisms. It is common knowledge that dextranase is used in the sugar industry; produced as a result of hydrolysis by dextranase and have prebiotic properties which influence the consistency and texture of food products. In medicine, dextranases are used to make blood substitutes. In addition, dextranase is used to produce low molecular weight dextran and cytotoxic dextran. Furthermore, dextranase is used to enhance antibiotic activity in endocarditis. It has been established that dextranase from marine bacteria is the most preferable for removing plaque, as it has a high enzymatic activity. This study lays the groundwork for the future design and development of different oral care products, based on enzymes derived from marine bacteria.

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

Cited by 29 publications

References 75 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

DNA Shuffling of aprE Genes to Increase Fibrinolytic Activity and Thermostability

Marine Bacterial Dextranases: Fundamentals and Applications

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