The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 9, 2007, Pages 2184-2189

  Sugimoto, Satoshi ^a   Fujii, Tadashi ^a   Morimiya, Tatsuo ^a   Johdo, Osamu ^a   Nakamura, Takumi ^b  

^a MERCIAN CORPORATION   (Japan)

^b Sodx Co   (Japan)

Author keywords

Fibrinolysis; Fusarium sp. BLB; Protease; Tempeh; Thrombolysis

Indexed keywords

AMINO ACIDS; CLONING; DNA; FERMENTATION; FUNGI; GENE ENCODING; PROTEINS;

FUSARIUM OXYSPORUM; GENOMIC GENE; PROTEASE; SYNTHETIC PEPTIDES;

ENZYME ACTIVITY;

PLASMINOGEN; PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; FIBRINOLYSIS; FUSARIUM; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SOYBEAN; THROMBOSIS;

AMINO ACID SEQUENCE; ENDOPEPTIDASES; FIBRINOLYSIS; FUSARIUM; MOLECULAR SEQUENCE DATA; PLASMINOGEN; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SOY FOODS; SUBSTRATE SPECIFICITY; THROMBOSIS;

FUNGI; FUSARIUM; FUSARIUM OXYSPORUM; FUSARIUM SP.; GLYCINE MAX; RHIZOPUS;

EID: 36148973934     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70153     Document Type: Article

References (25)

1. Sumi, H., Hamada, H., Tsushima, H., Mihara, H., and Muraki, H., A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia, 43, 1110-1111 (1987).
2. Steinkraus, K. H., Yap, B. H., Van Buren, J. P., Provvidenti, M. I., and Hand, D. B., Studies on tempeh - an Indonesian fermented soybean food. Food Res., 25, 777-788 (1960).
3. Okada, N., Development of tempeh microbiology. Nippon Jozo Kyokaishi (in Japanese), 81, 464-469 (1986).
4. Nout, M. J. R., and Rombouts, F. M., Recent developments in tempe research. J. Appl. Bacteriol., 69, 609-633 (1990).
5. Denter, J., Rehm, H. J., and Bisping, B., Changes in the contents of fat-soluble vitamins and provitamins during tempe fermentation. Int. J. Food Microbiol., 45, 129-134 (1998).
6. Keuth, S., and Bisping, B., Formation of vitamins by pure cultures of tempeh moulds and bacteria during the tempeh solid substrate fermentation. J. Appl. Bacteriol., 75, 427-434 (1993).
7. Keuth, S., and Bisping, B., Vitamin B12 production by Citrobacter freundii or Klebsiella pneumoniae during tempeh fermentation and proof of enterotoxin absence by PCR. Appl. Environ. Microbiol., 60, 1495-1499 (1994).
8. Cassidy, A., Hanley, B., and Lamuela-Raventos, R. M., Isoflavones, lignans and stilbenes - origins, metabolism and potential importance to human health. J. Sci. Food Agric., 80, 1044-1062 (2000).
9. Kalavi, F. N. M., Muroki, N. M., Omwega, A. M., and Mwadime, R. K. N., Effects of tempe yellow maize porridge and milk yellow maize porridge on growth rate, diarrhoea and duration of rehabilitation of malnourished children. East Afr. Med. J., 73, 427-431 (1996).
10. Karyadi, D., and Lukito, W., Beneficial effects of tempeh in disease prevention and treatment. Nutr. Rev., 54, 94-98 (1996).
11. Sumi, H., and Okamoto, T., Thrombolytic activity of an aqueous extract of tempe. Nippon Kasei Gakkaishi (in Japanese), 54, 337-342 (2003).
12. Sherry, S., Recombinant tissue plasminogen activator (rt-PA): is it the thrombolytic agent of choice for an evolving acute myocardial infarction? Am. J. Cardiol., 59, 984-989 (1987).
13. Sasaki, K., Moriyama, S., Tanaka, Y., Sumi, H., Toki, N., and Robbins, K. C., The transport of 125I-labeled human high molecular weight urokinase across the intestinal tract in a dog model with stimulation of synthesis and/or release of plasminogen activators. Blood, 66, 69-75 (1985).
14. Sumi, H., Maruyama, M., Yoneta, T., and Mihara, H., Activation of plasma fibrinolysis after intrarectal administration of high molecular weight urokinase and its derivative. Acta Haematol., 70, 289-295 (1983).
15. Toki, N., Sumi, H., Sasaki, K., Boreisha, I., and Robbins, K. C., Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins. J. Clin. Invest., 75, 1212-1222 (1985).
16. Ueda, M., Kubo, T., Miyatake, K., and Nakamura, T., Purification and characterization of fibrinolytic alkaline protease from Fusarium sp. BLB. Appl. Microbiol. Biotechnol., 74, 331-338 (2007).
17. Ochman, H., Gerber, A. S., and Hartl, D. L., Genetic applications of an inverse polymerase chain reaction. Genetics, 120, 621-623 (1988).
18. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
19. Astrup, T., and Mullertz, S., The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. Biophys., 40, 346-351 (1952).
20. Miyata, K., Hirai, S., Yashiki, T., and Tomoda, K., Intestinal absorption of Serratia protease. J. Appl. Biochem., 2, 111-116 (1980).
21. Moriya, N., Nakata, M., Nakamura, M., Takaoka, M., Iwasa, S., Kato, K., and Kakimura, A., Intestinal absorption of serrapeptase [TSP] in rats. Biotechnol. Appl. Biochem., 20, 101-108 (1994).
22. 131I-labelled elastase in vivo. Biochim. Biophys. Acta, 288, 181-189 (1972).
23. Papp, M., Fehár, S., Folly, G., and Horváth, E. J., Absorption of pancreatic lipase from the duodenum into lymphatics. Experientia, 33, 1191-1192 (1977).
24. Avakian, S., Further studies on the absorption of chymotrypsin. Clin. Pharmacol. Ther., 5, 712-715 (1964).
25. Warshaw, A. L., Walker, W. A., Cornell, R., and Isselbacher, K., Small intestinal permeability to macromolecules. Transmission of horseradish peroxidase into mesenteric lymph and portal blood. Lab. Invest., 25, 675-684 (1971).