The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB.
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.
Sugimoto
Satoshi
S
Bioresource Laboratories, Mercian Co, 1808 Nakaizumi, Iwata, Shizuoka 438-0078, Japan. sugimoto-s@merican.co.jp
Fujii
Tadashi
T
Morimiya
Tatsuo
T
Johdo
Osamu
O
Nakamura
Takumi
T
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005342:Fibrinolysis; D005670:Fusarium / Q000201:enzymology*; D008969:Molecular Sequence Data; D010958:Plasminogen / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D045730:Soy Foods; D013379:Substrate Specificity; D013927:Thrombosis / Q000201:enzymology