Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish

Kim, Hyun-Kuk; Kim, Gu-Taek; Kim, Daekyung; Choi, Won Chan; Park, Sunghoon; Jeong, Yong-Kee; Kong, In‐Soo

doi:10.1016/s0922-338x(97)89249-5

Cited by 105 publications

(7 citation statements)

References 22 publications

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“…Most known Wbrinolytic enzymes from microbes are serine proteases and are not inhibited by EDTA. KA38 [23], SW-1 [47], an enzyme from R. chinensis 12 [31] and AMMP [30] are metalloproteases. However, the characteristics and the N-terminal amino acid sequence of Fu-P were diVerent from those of these four enzymes.…”

Section: Evects Of Metal Ions and Protease Inhibitors On Enzyme Activitymentioning

confidence: 99%

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Li-cheng

Chen

et al. 2009

J Ind Microbiol Biotechnol

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A novel fibrinolytic enzyme from Fusarium sp. CPCC 480097, named Fu-P, was purified to electrophoretic homogeneity using ammonium sulfate precipitation and ion exchange and gel filtration chromatography. Fu-P, a single protein had a molecular weight of 28 kDa, which was determined by SDS-PAGE and gel filtration chromatography. The isoelectric point of Fu-P determined by isoelectric focusing electrophoresis (IEF) was 8.1, and the optimum temperature and pH value were 45 degrees C and 8.5, respectively. Fu-P cleaved the alpha-chain of fibrin (ogen) with high efficiency, and the beta-chain and gamma-gamma (gamma-)-chain with lower efficiency. Fu-P activity was inhibited by EDTA and PMSF, and the enzyme exhibited a high specificity for the chymotrypsin substrate S-2586. Fu-P was therefore identified as a chymotrypsin-like serine metalloprotease. The first 15 amino acids of the N-terminal sequence of Fu-P were Q-A-S-S-G-T-P-A-T-I-R-V-L-V-V and showed no homology with that of other known fibrinolytic enzymes. This protease may have potential applications in thrombolytic therapy and in thrombosis prevention.

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Section: Evects Of Metal Ions and Protease Inhibitors On Enzyme Activitymentioning

confidence: 99%

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Li-cheng

Chen

et al. 2009

J Ind Microbiol Biotechnol

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“…DJ-4) [45,46], Jeot-gals (Bacillus sp. KA38) [47], Gembus (Bacillus pumilus 2.g), [48], Kishk (Bacillus megaterium KSK-07) [27] and Moromi (Bacillus subtilis K2) [49], etc., have also been reported to yield enzymes with significant fibrinolytic potential. Probiotic lactic acid bacteria have also shown high proteolytic activity in fermented foods [50,51].…”

Section: Microbial Fibrinolytic Enzymes: Production Status and Diversitymentioning

confidence: 99%

Microbial Fibrinolytic Enzymes as Anti-Thrombotics: Production, Characterisation and Prodigious Biopharmaceutical Applications

2021

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Cardiac disorders such as acute myocardial infarction, embolism and stroke are primarily attributed to excessive fibrin accumulation in the blood vessels, usually consequential in thrombosis. Numerous methodologies including the use of anti-coagulants, anti-platelet drugs, surgical operations and fibrinolytic enzymes are employed for the dissolution of fibrin clots and hence ameliorate thrombosis. Microbial fibrinolytic enzymes have attracted much more attention in the management of cardiovascular disorders than typical anti-thrombotic strategies because of the undesirable after-effects and high expense of the latter. Fibrinolytic enzymes such as plasminogen activators and plasmin-like proteins hydrolyse thrombi with high efficacy with no significant after-effects and can be cost effectively produced on a large scale with a short generation time. However, the hunt for novel fibrinolytic enzymes necessitates complex purification stages, physiochemical and structural-functional attributes, which provide an insight into their mechanism of action. Besides, strain improvement and molecular technologies such as cloning, overexpression and the construction of genetically modified strains for the enhanced production of fibrinolytic enzymes significantly improve their thrombolytic potential. In addition, the unconventional applicability of some fibrinolytic enzymes paves their way for protein hydrolysis in addition to fibrin/thrombi, blood pressure regulation, anti-microbials, detergent additives for blood stain removal, preventing dental caries, anti-inflammatory and mucolytic expectorant agents. Therefore, this review article encompasses the production, biochemical/structure-function properties, thrombolytic potential and other surplus applications of microbial fibrinolytic enzymes.

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“…Novel fibrinolytic enzymes were purified and characterized from Bacillus sp. KA38 originated from fermented fish (Kim et al, 1997), and from the Japanese traditional food, Shiokara (lysate of Katsuwonus pelamis digestive tract) (Nakajima, Taya, & Sumi, 1993). Wong and Mine (2004) discovered a new fibrinolytic enzyme in fermented shrimp paste, a traditional Chinese fermented seasoning.…”

Section: Introductionmentioning

confidence: 99%

A novel fibrinolytic enzymes from the Korean traditional fermented food—Jotgal: Purification and characterization

Kim¹,

Ri²,

Choe

2020

J Food Biochem

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The fibrinolytic activity in Korean traditional fermented food, Jotgal (pickled fish) was identified. Though the fibrinolytic activity could vary in different kinds of Jotgal, this activity seems to be produced by microorganisms during the natural fermentation stage. From Gonjaengijot (pickled opossum shrimp), two novel fibrinolytic enzymes named by JP‐I and JP‐II, have been purified by ethanol precipitation, Bio‐GEL P‐100 gel filtration, and DEAE‐cellulose ion‐exchange chromatography. Compared to the crude enzyme extract, the specific activity of the JP‐I and JP‐II increased 258, 85‐fold with the recovery of 22.1, 8.5%, respectively. The molecular weights of both enzymes were estimated as 36 kDa on sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS–PAGE). The optimal condition for fibrinolytic activity of JP‐I was at 50°C and pH 8.1, while that of JP‐II was at 45°C and 9.9. Both enzymes were stable at a broad range of pH (5.0 to 10.5) and have metalloprotease nature. From these results, it concludes that these enzymes could be a novel potent thrombolytic agent. Practical applications The fibrinolytic enzyme is one of the clinical agents for cardiovascular diseases which is the leading cause of morbidity and mortality worldwide with 17 million deaths every year. A variety of fibrinolytic enzymes are found and characterized from various sources such as plants, animals, and microorganisms, and new sources for fibrinolytic enzymes continue to be explored. Jotgal, widely used in Korean people's diet, is a traditional Korean seafood prepared from many different types of fishes, fish eggs, fish intestines, and shellfishes. Through an amount of research, some of fibrinolytic enzymes were found and purified from Jotgal, however, no studies have been done on fibrinolytic enzyme from opossum shrimp. In this study, the purification, enzymatic characteristics, and fibrinolytic activity of the proteases, originated from Korean traditional fermented food, Jotgal were reported. These enzymes could be novel potent thrombolytic agent.

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Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish

Cited by 105 publications

References 22 publications

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Microbial Fibrinolytic Enzymes as Anti-Thrombotics: Production, Characterisation and Prodigious Biopharmaceutical Applications

A novel fibrinolytic enzymes from the Korean traditional fermented food—Jotgal: Purification and characterization

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