| RRC ID |
15421
|
| 著者 |
Sugimoto S, Fujii T, Morimiya T, Johdo O, Nakamura T.
|
| タイトル |
The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB.
|
| ジャーナル |
Biosci Biotechnol Biochem
|
| Abstract |
Tempeh is a traditional Indonesian soybean-fermented food produced by filamentous fungi, Rhizopus sp. and Fusarium sp. We isolated and sequenced the genomic gene and a cDNA clone encoding a novel protease (FP) from Fusarium sp. BLB. The genomic gene was 856 bp in length and contained two introns. An isolated cDNA clone encoded a protein of 250 amino acids. The predicted amino acid sequence of FP showed highest homology, of 76%, with that of trypsin from Fusarium oxysporum. The hydrolysis activity of FP toward synthetic peptide was higher than that of any other protease tested, including Nattokinases. Furthermore, the thrombolytic activity of FP was about 2.1-fold higher than that of Nattokinase when the concentration of plasminogen was 24 units/ml. These results suggest that FP is superior to Nattokinases in dissolving fibrin when absorbed into the blood.
|
| 巻・号 |
71(9)
|
| ページ |
2184-9
|
| 公開日 |
2007-9-1
|
| DOI |
10.1271/bbb.70153
|
| PII |
JST.JSTAGE/bbb/70153
|
| PMID |
17827689
|
| MeSH |
Amino Acid Sequence
Endopeptidases / chemistry
Endopeptidases / genetics
Endopeptidases / isolation & purification
Endopeptidases / metabolism*
Fibrinolysis*
Fusarium / enzymology*
Molecular Sequence Data
Plasminogen / metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Soy Foods*
Substrate Specificity
Thrombosis / enzymology
|
| IF |
1.516
|
| 引用数 |
25
|
|
WOS 分野
|
FOOD SCIENCE & TECHNOLOGY
CHEMISTRY, APPLIED
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| リソース情報 |
| 一般微生物 |
JCM 9511
JCM 9873. JCM 11502 |
