Fibrinolytic activity of an enzyme produced by Bacillus subtilis

Fayek, K. I.; El‐Sayed, Sanaa T.

doi:10.1007/bf02021067

Cited by 2 publications

(2 citation statements)

References 7 publications

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“…Bacillus sp. has been recognized as being safe for humans (Fayek & El-Sayed 1980). Therefore, the result of these studies may provide important insights into development of more safe and affordable thrombolytic agents.…”

Section: Enzymatic Properties Of Bk IImentioning

confidence: 98%

Molecular cloning and characterization of the gene encoding a fibrinolytic enzyme from Bacillus subtilis Strain A1

Jeong

Kim

Gal

et al. 2004

World J Microbiol Biotechnol

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A fibrinolytic metalloprotease gene from Bacillus subtilis has been cloned in Escheridria coli XL1-Blue and the bacterial expressed enzyme was purified. The nucleotide sequence of the cloned fibrinolytic enzyme gene revealed a single open reading frame of 1023 bp coding for 341 amino acids (M r 37708.21 Da). N-terminal amino acid sequencing of the fibrinolytic enzyme excreted from E. coli host cells revealed that the mature fibrinolytic enzyme consists of 288 amino acids (M r 31391.1 Da). The deduced amino acid sequence showed significant homology with Erwina carotovora neutral metalloprotease and Serratia marcescens minor metalloprotease by 65 and 58% amino acid sequence identity, respectively. The protein showed significant alignments with the conserved domain of catalytic activity and the a-helix domain in Bacillus anthracis thermolysis metalloprotease. The biochemical properties of the purified enzyme suggested that the enzyme is a fibrinolytic metalloprotease, which has optimal activity at pH 7.0 and 50°C.

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Section: Enzymatic Properties Of Bk IImentioning

confidence: 98%

Molecular cloning and characterization of the gene encoding a fibrinolytic enzyme from Bacillus subtilis Strain A1

Jeong

Kim

Gal

et al. 2004

World J Microbiol Biotechnol

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“…A fibrinolytic enzyme produced from Bacillus subtilis has also been reported (5), but it did not show the same level of plasminogen activator activity as does NK.…”

mentioning

confidence: 92%

Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang

Kim¹,

Choi²,

Kim³

et al. 1996

Appl Environ Microbiol

276

118

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Bacillus sp. strain CK 11-4, which produces a strongly fibrinolytic enzyme, was screened from Chungkook-Jang, a traditional Korean fermented-soybean sauce. The fibrinolytic enzyme (CK) was purified from supernatant of Bacillus sp. strain CK 11-4 culture broth and showed thermophilic, hydrophilic, and strong fibrinolytic activity. The optimum temperature and pH were 70؇C and 10.5, respectively, and the molecular weight was 28,200 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The first 14 amino acids of the N-terminal sequence of CK are Ala-Gln-Thr-Val-Pro-Tyr-Gly-Ile-Pro-Leu-Ile-Lys-Ala-Asp. This sequence is identical to that of subtilisin Carlsberg and different from that of nattokinase, but CK showed a level of fibrinolytic activity that was about eight times higher than that of subtilisin Carlsberg. The amidolytic activity of CK increased about twofold at the initial state of the reaction when CK enzyme was added to a mixture of plasminogen and substrate (H-D-Val-Leu-Lys-NA). A similar result was also obtained from fibrin plate analysis.

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Fibrinolytic activity of an enzyme produced by Bacillus subtilis

Cited by 2 publications

References 7 publications

Molecular cloning and characterization of the gene encoding a fibrinolytic enzyme from Bacillus subtilis Strain A1

Molecular cloning and characterization of the gene encoding a fibrinolytic enzyme from Bacillus subtilis Strain A1

Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang

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