Identification of a fibrinolytic enzyme by Bacillus vallismortis and its potential as a bacteriolytic enzyme against Streptococcus mutans.
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.
Kim
Jae-Bum
JB
AceBiotech Co., Ltd., #114 Bio-Venture Center, KRIBB, Yuseong, Daejeon, Korea.
Jung
Woo-Hyuk
WH
Ryu
Ji-Myung
JM
Lee
Yeo-Joon
YJ
Jung
Joon-Ki
JK
Jang
Hyung-Wook
HW
Kim
Sung-Woo
SW
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D001433:Bacteriolysis / Q000187:drug effects*; D002470:Cell Survival / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D005240:Feasibility Studies; D005342:Fibrinolysis; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000008:administration & dosage* / Q000737:chemistry* / Q000378:metabolism; D013295:Streptococcus mutans / Q000166:cytology* / Q000187:drug effects*
D010447:Peptide Hydrolases