Optimization of fibrinolytic enzyme production by newly isolated Bacillus subtilis Egy using central composite design

Moharam, Maysa E.; El-Bendary, Magda A.; El-Beih, Fawkia M.; Easa, Saadia M.; Elsoud, Mostafa M. Abo; Azzam, Mohamed I.; Elgamal, Nora N.

doi:10.1016/j.bcab.2018.11.003

Cited by 13 publications

(12 citation statements)

References 31 publications

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“…The maximum enzyme yield (60.16 ± 0.05 FU/ml/min) was observed at incubation temperature 37 ºC as shown in figure 5. The results of the current study are comparable with the results of Moharam et al (2019) who reported maximum enzyme activity at 37 ºC by using Bacillus subtilis as both the bacterial strain belongs to mesophilic temperature range. Sharma et al (2015) reported maximum enzyme activity at 40 ºC by using Citrobacter braaki.…”

Section: Optimization Of Physical and Nutritional Parameterssupporting

confidence: 90%

“…The plasminogen is activated into plasmin to degrade the blood clot (Wen et al, 2018). There are several fibrinolytic enzymes including urokinase, nattokinase, and streptokinase that activate the plasminogen into plasmin so that the blood clot can be degraded (Moharam et al, 2019). Fibrinolytic enzymes have increased the survival rate of the patients by reducing the risk factor of thrombosis (Chen et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

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Biosynthesis of fibrinolytic agent urokinase by Enterococcus gallinarum isolated from sardine

Nawaz¹,

Gillani²,

Tahir³

et al. 2020

Rev.Mex.Ing.Quim.

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Section: Optimization Of Physical and Nutritional Parameterssupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Biosynthesis of fibrinolytic agent urokinase by Enterococcus gallinarum isolated from sardine

Nawaz¹,

Gillani²,

Tahir³

et al. 2020

Rev.Mex.Ing.Quim.

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“…Enzyme production is mainly related to the nutrient components, nature of the medium and bacteria. In Bacillus subtilis Egy, fibrinolytic protease productivity was high after 96 h ( Moharam et al, 2019 ). Enzyme production in relation with incubation temperature was analyzed.…”

Section: Resultsmentioning

confidence: 99%

In vitro fibrinolytic activity of an enzyme purified from Bacillus amyloliquefaciens strain KJ10 isolated from soybean paste

Rajaselvam

Benit²,

Alotaibi³

et al. 2021

Saudi Journal of Biological Sciences

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A fibrinolytic protease secreting producing Bacillus amyloliquefaciens strain KJ10 was initially screened from the fermented soybean. Maximum productivity was obtained in the culture medium after 40 h incubation, 34 °C incubation temperature at pH 8.0. Fibrinolytic protease production was enhanced in the culture medium with 1% sucrose (3712 ± 52 U/mL), 1% (w/v) yeast extract (3940 ± 28 U/mL) and 0.1% MgSO 4 (3687 ± 38 U/mL). Enzyme was purified up to 22.9-fold with 26%recovery after Q-Sepharose HP column chromatography. After three steps purification, enzyme activity was 1606U/mg and SDS-PAGE analysis revealed 29 kDa protein and enzyme band was detected by zymograpy. Enzyme was highly active at pH 8.0, at wide temperature ranges (40 °C − 55 °C) and was activated by Mn 2+ (102 ± 3.1%) and Mg 2+ (101.4 ± 2.9%) ions. The purified fibrinolytic enzyme was highly specific against N-Suc-Ala-Ala-Pro-Phe- p NA (189 mmol/min/mL) and clot lytic activity reached 28 ± 1.8% within 60 min in vitro . The purified fibrinolytic enzyme showed least erythrocytic lysis activity confirmed safety to prevent various health risks, including hemolytic anemia. Based on this study, administration of fibrinolytic enzyme from B. amyloliquefaciens strain KJ10 is safe for clinical applications.

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“…An identical investigation carried out by Lang et al concluded that shrimp shell powder acts as a potential inducer of alkaline protease production from Bacillus subtilis (26). Similar investigations on the production of fibrinolytic protease with various complex substrates, such as soybean filtrate (27), fodder yeast (5) and Cassava starch (28), have comparatively yielded lower amounts of enzyme than shrimp waste.…”

Section: Effect Of Complex Media On Flp Productionmentioning

confidence: 90%

“…Due to their undesirable side effects, such as gastrointestinal bleeding and less fibrin specificity (3,4), intense research has been directed at finding alternative microbial fibrinolytic enzymes with better task specificity. Recent investigations have identified Bacillus subtilis as a promising source for the production of specific fibrinolytic proteases (FLPs) that are reported to be safer for therapeutic use (5,6). However, purification of these therapeutically significant enzymes was accomplished with a sequence of downstream operations, such as ammonium sulfate precipitation, ultrafiltration, ion exchange chromatography (7) and affinity chromatography (8).…”

Section: Introductionmentioning

confidence: 99%

Switchable deep eutectic solvent driven micellar extractive fermentation of ultrapure fibrin digesting enzyme from Bacillus subtilis

Muniasamy

Rathnasamy

2021

Preprint

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Fibrinolytic protease (FLP) is a therapeutic enzyme used in the treatment of thrombolytic diseases. The present study proposed the concept of pH-driven swappable micellar two-phase extraction for the concurrent production and purification of FLP from Bacillus subtilis at cloud point extraction. Extractive fermentation was carried out with a pH swap mechanism, and FLP was extracted to the top phase by surfactant deep eutectic solvents (SADES). Shrimp waste was chosen as a sustainable low-cost substrate that yielded a maximum protease of 185 U/mg. Six SDESs were synthesized with nonionic surfactants as hydrogen bond donors and quaternary ammonium salts as hydrogen bond acceptors, and their association was confirmed by H1 NMR. Thermophysical investigation of the synthetic SADES was accomplished as a function of temperature. Response surface methodology for extractive fermentation was performed with the concentration of SADES (35% w/v), Na2SO4 (15% w/v) and pH (6.3) as variables and the enzyme activity (248 IU/mg) as a response. Furthermore, purification using gel filtration chromatography was used to quantify the amount of enzyme obtained in the extraction phase (849 IU/ml). After final purification with an anion exchange column, the maximum purity fold (22.32) with enzyme activity (1172 IU/ml) was achieved. The in vitro fibrinolytic activity was confirmed using a fibrin plate assay.

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Optimization of fibrinolytic enzyme production by newly isolated Bacillus subtilis Egy using central composite design

Cited by 13 publications

References 31 publications

Biosynthesis of fibrinolytic agent urokinase by Enterococcus gallinarum isolated from sardine

Biosynthesis of fibrinolytic agent urokinase by Enterococcus gallinarum isolated from sardine

In vitro fibrinolytic activity of an enzyme purified from Bacillus amyloliquefaciens strain KJ10 isolated from soybean paste

Switchable deep eutectic solvent driven micellar extractive fermentation of ultrapure fibrin digesting enzyme from Bacillus subtilis

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