Purification, characterization, and chemical modification of Bacillus velezensis SN-14 fibrinolytic enzyme

Lu, Mingyuan; Gao, Zexin; Xing, Shuqi; Long, Jia; Li, Cuiqin; He, Laping; Wang, Xiao

doi:10.1016/j.ijbiomac.2021.02.167

Cited by 14 publications

(5 citation statements)

References 35 publications

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“…Effects of pH on the stability and activity of versiase were illustrated in Figure 3A and the stability was determined at pH 2.0~10.0 by extending the conditions to 4 h. It w observed that versiase was more active in slightly acidic conditions with optimal p around 5.0 (Figure 3A), which is different from the serine proteases that prefer neutral alkali pH conditions [15][16][17]. It was found that versiase was relatively stable in a bro pH range over 4.0~8.0, with 85% of fibrinolytic activity maintained on average (Figure 3 The effects of temperature on versiase were shown in Figure 3C,D, and thermal s bility was determined by incubation at 10~80 °C for 4 h. The maximum enzymatic activ was observed at 40 °C (Figure 3C), which is identical to that of the reported fibrinoly enzymes [11,18,19]. The enzyme showed decent stability and retained nearly 80% of original activity below 50 °C.…”

Section: Biochemical Properties Of Versiasesupporting

confidence: 75%

“…The effects of temperature on versiase were shown in Figure 3C,D, and thermal stability was determined by incubation at 10~80 • C for 4 h. The maximum enzymatic activity was observed at 40 • C (Figure 3C), which is identical to that of the reported fibrinolytic enzymes [11,18,19]. The enzyme showed decent stability and retained nearly 80% of its original activity below 50 • C.…”

Section: Biochemical Properties Of Versiasesupporting

confidence: 63%

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A Novel Bi-Functional Fibrinolytic Enzyme with Anticoagulant and Thrombolytic Activities from a Marine-Derived Fungus Aspergillus versicolor ZLH-1

Zhao

Lin

et al. 2022

Marine Drugs

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Fibrinolytic enzymes are important components in the treatment of thrombosis-associated disorders. A new bi-functional fibrinolytic enzyme, versiase, was identified from a marine-derived fungus Aspergillus versicolor ZLH-1. The enzyme was isolated from the fungal culture through precipitation with ammonium sulfate at 90% saturation. Additionally, it was further purified by DEAE-based ion-exchange chromatography, with a recovery of 20.4%. The fibrinolytic enzyme presented as one band on both SDS-PAGE and fibrin-zymogram, with a molecular mass of 37.3 kDa. It was elucidated as a member of metalloprotease in M35 family by proteomic approaches. The homology-modeling analysis revealed that versiase shares significant structural homology wuth the zinc metalloendopeptidase. The enzyme displayed maximum activity at 40 °C and pH 5.0. The activity of versiase was strongly inhibited by the metalloprotease inhibitors EDTA and BGTA. Furthermore, versiase hydrolyzed fibrin directly and indirectly via the activation of plasminogen, and it was able to hydrolyze the three chains (α, β, γ) of fibrin(ogen). Additionally, versiase demonstrated promising thrombolytic and anticoagulant activities, without many side-effects noticed. In conclusion, versiase appears to be a potent fibrinolytic enzyme deserving further investigation.

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Section: Biochemical Properties Of Versiasesupporting

confidence: 75%

Section: Biochemical Properties Of Versiasesupporting

confidence: 63%

A Novel Bi-Functional Fibrinolytic Enzyme with Anticoagulant and Thrombolytic Activities from a Marine-Derived Fungus Aspergillus versicolor ZLH-1

Zhao

Lin

et al. 2022

Marine Drugs

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“…Data on Bacillus velezensis have been applied widely to the field of biological control and promotion of plant growth [ 13 ] and have shown its potential as a probiotic [ 14 ]. However, several studies only reported the discovery of and cloned fibrinolytic enzyme in Bacillus velezensis [ 15 , 16 , 17 , 18 ], therefore, it is a topic of further research. In the present study, a fibrinolytic protease (named Velefibrinase) was purified from marine B. velezensis Z01, which was screened from sea mud and its biochemical property was characterized.…”

Section: Introductionmentioning

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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“…Our previous report collected the sample supernatant to analyze the NK activity (FU/g) of fermented soybeans through the fibrin degradation method [ 29 ]. Ten grams of fermented soybeans were dissolved in 90 mL deionized water and homogenized in a beating machine for 10 s, then extracted at 4 °C for 24 h, and centrifuged at 10,000× g for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Effect of Adding Bifidobacterium animalis BZ25 on the Flavor, Functional Components and Biogenic Amines of Natto by Bacillus subtilis GUTU09

Zhang

Lan

Tian

et al. 2022

Foods

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Natto is a high-value fermented soybean produced by B. subtilis. However, B. subtilis produces a pungent amine odor. This study compared the volatile organic compounds (VOCs), free amino acids (FAAs) and biogenic amines (BAs), nattokinase (NK) of natto made by two-strain fermentation with Bifidobacterium animalis BZ25 and Bacillus subtilis GUTU09 (NMBB) and that of natto made by single-strain fermentation with Bacillus subtilis GUTU09 (NMB). Compared with NMB, volatile amine substances disappeared, ketones and aldehydes of NMBB were reduced, and alcohols increased. Besides that, the taste activity value of other bitter amino acids was lowered, and BA content was decreased from 255.88 mg/kg to 238.35 mg/kg but increased NK activity from 143.89 FU/g to 151.05 FU/g. Correlation analysis showed that the addition of BZ25 reduced the correlation between GUTU09 and BAs from 0.878 to 0.808, and pH was changed from a positive correlation to a negative one. All these results showed that the quality of natto was improved by two-strain co-fermentation, which laid a foundation for its potential industrial application.

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Purification, characterization, and chemical modification of Bacillus velezensis SN-14 fibrinolytic enzyme

Cited by 14 publications

References 35 publications

A Novel Bi-Functional Fibrinolytic Enzyme with Anticoagulant and Thrombolytic Activities from a Marine-Derived Fungus Aspergillus versicolor ZLH-1

A Novel Bi-Functional Fibrinolytic Enzyme with Anticoagulant and Thrombolytic Activities from a Marine-Derived Fungus Aspergillus versicolor ZLH-1

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

Effect of Adding Bifidobacterium animalis BZ25 on the Flavor, Functional Components and Biogenic Amines of Natto by Bacillus subtilis GUTU09

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