Identification of fibrinogen-induced nattokinase WRL101 from Bacillus subtilis WRL101 isolated from Doenjang

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Title
Identification of fibrinogen-induced nattokinase WRL101 from Bacillus subtilis WRL101 isolated from Doenjang
Author(s)
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
2013
Abstract
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 B?-chain of human fibrinogen, but did not affect the ?-chain, indicating that it is an ?-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 determined.
Keyword
Bacillus subtilisDoenjangfibrinolytic enzymenattokinase.
ISSN
1996-0808
Publisher
Academic Journals
DOI
http://dx.doi.org/10.5897/AJMR12.041
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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