Partial Purification and Characterization of Fibrinolytic Enzymes from Yellow Mealworm

Huang, Mingxing; Ye, Yun; Chen, Ya Xiong; Han, Ya Li

doi:10.1007/s10989-012-9288-x

Cited by 9 publications

(3 citation statements)

References 25 publications

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“…K + and Na + had almost no effect on the enzyme activity, but Fe 2+ , Fe 3+ , and Li + were found to inhibit the enzyme activity significantly. The effect of metal ions on PSLTro01 shows a similarity with [5] but a great difference from [29]. Inhibition studies of enzyme activity can provide a first insight into the nature of the enzyme, its cofactor requirements, and the nature of the active centre.…”

Section: Discussionmentioning

confidence: 99%

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Tian

Лі

Li-wei

et al. 2015

International Journal of Biological Macromolecules

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Section: Discussionmentioning

confidence: 99%

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Tian

Лі

Li-wei

et al. 2015

International Journal of Biological Macromolecules

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“…Fibrinolytic enzymes are agents that dissolve fibrin clots and are considered to be potential candidates in the treatment of many CVDs as thrombolytic agents [ 2 ]. A variety of fibrinolytic enzymes are obtained from various sources, such as plants [ 3 ], animals [ 4 ], and microorganisms [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Purification and proteomic analysis of potent fibrinolytic enzymes extracted from Lumbricus rubellus

Stephani¹,

Rahayu²,

Retnoningrum

et al. 2023

Proteome Sci

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Background Lumbrokinase derived from earthworms, Lumbricus rubellus is known to have fibrinolytic enzymes that have potential as therapeutic drugs due to its ability to dissolve fibrin. The current study is aimed to purify the Lumbrokinase from L. rubellus and identify its protein component. Methods Water extract of local earthworm Lumbricus rubellus revealed several proteins. Therefore, to identify its protein component, purification through HiPrep DEAE fast flow and proteomic analysis were conducted prior to identifications. A combination of two-dimension gel electrophoresis (2DE) and electrospray ionization mass spectrometry analysis was used to identify the purified fractions. Results The purified fractions contain five protein bands, namely F25-1, F25-2, F85-1, F85-2, and F85-3, which displayed strong fibrinogenolytic activity. F25 fractions showed fibrinogenolytic activity of 974.85 U/mg, while F85 fractions showed higher activity of 1,484.11 U/mg. Fractions F85-1, F85-2, and F85-3 showed molecular weights of 42.6 kDa, 27.03 kDa, and 14 kDa, respectively and were identified as Lumbrokinase iso-enzymes. Conclusion This preliminary study indicates that the F25 and F85 fractions are similar to published fibrinolytic protease-1 and lumbrokinase, respectively, in terms of their amino acid sequence.

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“…A variety of fibrinolytic enzymes are obtained from various sources viz. plants (Chung et al 2010); animals (Huang et al 2012); and microorganisms (Ju et al 2012).…”

Section: Introductionmentioning

confidence: 99%

Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media

et al. 2017

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Intravascular thrombosis is one of the major causes of variety of cardiovascular disorders leading to high mortality worldwide. Fibrinolytic enzymes from microbial sources possess ability to dissolve these clots and help to circumvent these problems in more efficient and safer way. In the present study, fibrinolytic protease with higher fibrinolytic activity than plasmin was obtained from Serratia sp. KG-2-1 isolated from garbage dump soil. Response surface methodology was used to study the interactive effect of concentration of maltose, yeast extract + peptone (1:1), incubation time, and pH on enzyme production and biomass. Maximum enzyme production was achieved at 33 °C after 24 h at neutral pH in media containing 1.5% Maltose, 4.0% yeast extract + peptone and other trace elements resulting in 1.82 folds increased production. The enzyme was purified from crude extract using ammonium sulfate precipitation and DEAE-Sephadex chromatography resulting in 12.9 fold purification with 14.9% yield. The purified enzyme belongs to metalloprotease class and had optimal activity in conditions similar to physiological environment with temperature optima of 40 °C and pH optima of 8. The enzyme was found to be stable in various solvents and its activity was enhanced in presence of Na, K, Ba, Cu, Mn, Hg but inhibited by Ca and Fe. Hence, the obtained enzyme may be used as potential therapeutic agent in combating various thrombolytic disorders.

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Partial Purification and Characterization of Fibrinolytic Enzymes from Yellow Mealworm

Cited by 9 publications

References 25 publications

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Purification and proteomic analysis of potent fibrinolytic enzymes extracted from Lumbricus rubellus

Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media

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