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Title 

Identification of a fibrinolytic enzyme by Bacillus vallismortis and its potential as a bacteriolytic enzyme against Streptococcus mutans

Authors 

J B KimW H JungJ M RyuY J LeeJoon-Ki JungH W JangS W Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

2007

Citation 

Biotechnology Letters, vol. 29, no. 4, pp. 605-610

Keywords 

bacillus vallismortis Ace02bacteriolytic enzymefibrinolytic enzymeamino acidsbacteriachromatographymedical problemsmolecular masspurificationbacteriolytic enzymes

Abstract 

A potent fibrinolytic enzyme-producing bacterium was isolated from the traditional Korean condiment Chungkook-jang and identified as Bacillus vallismortis Ace02. The extracellular fibrinolytic enzyme was purified with a 18% recovery of activity from supernatant cultures using CM-Sepharose column chromatography and Sephacryl S-200 gel filtration. The specific activity of the purified enzyme was 757 kFU mg-1. Its molecular mass was about 28 kDa and the initial amino acids of the N-terminal sequence were AQSVPYGVSQ. The full amino acid sequence of fibrinolytic enzyme Ace02 corresponded with bacteriolytic enzyme, L27, from Bacillus licheniformis, which has strong lytic activity against Streptococcus mutans, a major causative strain of dental caries. This suggests that the purified enzyme should be used for prevention of dental caries as well as being an effective thrombolytic agent.

ISSN 

0141-5492

Link 

http://dx.doi.org/10.1007/s10529-006-9284-3

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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