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- Identification of fibrinogen-induced nattokinase WRL101 from Bacillus subtilis WRL101 isolated from Doenjang
- C S Park; D H Kim; W Y Lee; D O Kang; Jae Jun Song; N S Choi
- Bibliographic Citation
- African Journal of Microbiology Research, vol. 7, no. 19, pp. 1983-1992
- Publication Year
- To increase the fibrinolytic enzyme (nattokinase WRL101) in Bacillus subtilis WRL101, bovine fibrin or
fibrinogen (1.0%, w/v) were added in the tryptic soy broth as a substrate. The fibrinolytic activity
cultured in the fibrinogen-contained medium was increased. On the other hand, fibrin decreased the
activity. Using the medium condition, nattokinase WRL101 (fibrinogen-induced nattokinase WRL101,
FIN-WRL101) was isolated by commercial chromatographic techniques and its biochemical
characteristics were investigated. The molecular weight of FIN-WRL101 was estimated to be 29 kDa.
FIN-WRL101 was optimally active at pH 11.0 and 47°C. It had high degrading activity for the Aα-chain
and Bb-chain of human fibrinogen, but did not affect the g-chain, indicating that it is an a-fibrinogenase.
FIN-WRL101 was completely inhibited by phenylmethylsulfonyl fluoride, indicating that it belongs to the
serine protease. FIN-WRL101 exhibited high specificity for Meo-Suc-Arg-Pro-Tyr-pNA (S-2586), a
synthetic chromogenic substrate for chymotrypsin. Its nucleotide and amino acid sequences were
- Bacillus subtilisDoenjangfibrinolytic enzymenattokinase.
- Academic Journals
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- Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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