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Volumn 9, Issue 4, 1999, Pages 443-449

Production of a fibrinolytic enzyme in bioreactor culture by Bacillus subtilis BK-17

Author keywords

Bacillus subtilis; Bioreactor optimization; Fibrinolytic enzyme

Indexed keywords

BACTERIAL ENZYME; PLASMIN;

EID: 0032869605     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (18)

References (29)
  • 2
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • Astrup, T. and S. Müllertz. 1952. The fibrin plate method for estimating fibrinolytic Activity. Arch. Biochem. Biophys. 40: 346-351.
    • (1952) Arch. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Müllertz, S.2
  • 3
    • 0344579357 scopus 로고    scopus 로고
    • Department of Population Analysis, The Bureau of Statitics, Korea
    • Anonymous. 1997. Statistics of '96 death toll in Korea, Department of Population Analysis, The Bureau of Statitics, Korea.
    • (1997) Statistics of '96 Death Toll in Korea
  • 5
    • 0345441428 scopus 로고    scopus 로고
    • Effects of enviromental and nutritional conditions on fibrinolytic enzyme production from Bacillus subtilis BK-17 in flask culture
    • Choi, W.-A., J.-W. Lee, K.-H. Lee, and S.-H. Park. 1998. Effects of enviromental and nutritional conditions on fibrinolytic enzyme production from Bacillus subtilis BK-17 in flask culture. Korean J. Biotechnol. Bioeng, 13: 491-496.
    • (1998) Korean J. Biotechnol. Bioeng , vol.13 , pp. 491-496
    • Choi, W.-A.1    Lee, J.-W.2    Lee, K.-H.3    Park, S.-H.4
  • 6
    • 0026928538 scopus 로고
    • Production and degradation of alkaline protease in batch cultures of Bacillus subtilis ATCC 14416
    • Chu, I.-M., C. Lee, and T.-S. Li. 1992. Production and degradation of alkaline protease in batch cultures of Bacillus subtilis ATCC 14416. Enzyme Microb. Technol. 14: 755-761.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 755-761
    • Chu, I.-M.1    Lee, C.2    Li, T.-S.3
  • 8
    • 0016146682 scopus 로고
    • Studies on the formation of bacitracin by Bacillus licheniformis: Effect of glucose
    • Haavik, H. I. 1974. Studies on the formation of bacitracin by Bacillus licheniformis: Effect of glucose. J. Gen. Microbiol. 81: 383-390.
    • (1974) J. Gen. Microbiol. , vol.81 , pp. 383-390
    • Haavik, H.I.1
  • 9
    • 0016266062 scopus 로고
    • Studies on the formation of bacitracin by Bacillus licheniformis: Role of catabolite repression and organic acids
    • Haavik, H. I. 1974. Studies on the formation of bacitracin by Bacillus licheniformis: Role of catabolite repression and organic acids. J. Gen. Microbiol. 84: 321-326.
    • (1974) J. Gen. Microbiol. , vol.84 , pp. 321-326
    • Haavik, H.I.1
  • 10
    • 0019950356 scopus 로고
    • The influence of glucose, ammonium and magnesium availability on the production of protease and bacitracin by Bacillus licheniformis
    • Hanlon, G. W., N. A. Hodges, and A. D. Russell. 1982. The influence of glucose, ammonium and magnesium availability on the production of protease and bacitracin by Bacillus licheniformis. J. Gen. Microbiol. 128: 845-851.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 845-851
    • Hanlon, G.W.1    Hodges, N.A.2    Russell, A.D.3
  • 11
    • 0027369052 scopus 로고
    • Production of alkaline serine protease subtlisin Carlsberg by Bacillus licheniformis on complex medium in a stirred tank reactor
    • Hubner, U., U. Bock, and K. Schugerl. 1993. Production of alkaline serine protease subtlisin Carlsberg by Bacillus licheniformis on complex medium in a stirred tank reactor. Appl. Microbiol. Biotechnol. 40: 182-188.
    • (1993) Appl. Microbiol. Biotechnol. , vol.40 , pp. 182-188
    • Hubner, U.1    Bock, U.2    Schugerl, K.3
  • 13
    • 0031442243 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish
    • Kim, H.-K., G.-T. Kim, D.-K. Kim, W.-A. Choi, S.-H. Park, Y.-K. Jeong, and I.-S. Kong. 1997. Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish. J. Ferm. Bioeng. 84: 307-312.
    • (1997) J. Ferm. Bioeng. , vol.84 , pp. 307-312
    • Kim, H.-K.1    Kim, G.-T.2    Kim, D.-K.3    Choi, W.-A.4    Park, S.-H.5    Jeong, Y.-K.6    Kong, I.-S.7
  • 14
    • 0029960565 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK-14 screened from Chungkook-Jang
    • Kim, W., K. Choi, Y. Kim, H. Park, J. Choi, Y. Lee, H. Oh, I. Kwon, and S. Lee. 1996. Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK-14 screened from Chungkook-Jang. Appl. Environ. Microbiol. 62: 2482-2488.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2482-2488
    • Kim, W.1    Choi, K.2    Kim, Y.3    Park, H.4    Choi, J.5    Lee, Y.6    Oh, H.7    Kwon, I.8    Lee, S.9
  • 15
    • 0014062055 scopus 로고
    • Regulation of extracellular protease production in Bacillus cereus
    • Levisohn, S. and A. I. Aronson. 1967. Regulation of extracellular protease production in Bacillus cereus. J. Bacteriol. 93: 1023-1030.
    • (1967) J. Bacteriol. , vol.93 , pp. 1023-1030
    • Levisohn, S.1    Aronson, A.I.2
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 18
    • 0026950259 scopus 로고
    • Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis
    • Nakamura, T., Y. Yamagata, and E. Ichishima. 1992. Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto). Biosci. Biotech. Biochem. 56: 1869-1871.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 1869-1871
    • Nakamura, T.1    Yamagata, Y.2    Ichishima, E.3
  • 19
    • 0017652017 scopus 로고
    • Extracellular enzyme synthesis in the genus Bacillus
    • Priest, F. G. 1977. Extracellular enzyme synthesis in the genus Bacillus. Bacteriol. Rev. 41: 711-753.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 711-753
    • Priest, F.G.1
  • 20
    • 0023091774 scopus 로고
    • Formation of extracellular neutral proteinase and the stringent response in Bacillus subtilis
    • Riedel, K., A. Schroeter, P. Liebs, J.-P. Graba, M. Hecker, and D. Schrapel. 1987. Formation of extracellular neutral proteinase and the stringent response in Bacillus subtilis. Folia Microbiol. 32: 96-100.
    • (1987) Folia Microbiol. , vol.32 , pp. 96-100
    • Riedel, K.1    Schroeter, A.2    Liebs, P.3    Graba, J.-P.4    Hecker, M.5    Schrapel, D.6
  • 21
    • 0021892750 scopus 로고
    • 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
    • 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: 67-75.
    • (1985) Blood , vol.66 , pp. 67-75
    • Sasaki, K.1    Moriyama, S.2    Sumi, H.3    Toki, N.4    Robbins, K.C.5
  • 22
    • 0014481339 scopus 로고
    • Sporulation and the production of antibiotics, exoenzymes, and exotoxins
    • Schaeffer, P. 1969. Sporulation and the production of antibiotics, exoenzymes, and exotoxins. Bacteriol. Rev. 33: 48-71.
    • (1969) Bacteriol. Rev. , vol.33 , pp. 48-71
    • Schaeffer, P.1
  • 23
    • 0023656415 scopus 로고
    • A novel fibrinolytic enzyme (Nattokinase) in the vegetable cheese natto: A typical and popular soybean food in the Japanese diet
    • Sumi, H., H. Hamada, H. Tsushima, H. Mihara, and H. Muraki. 1987. 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) Experientia , vol.43 , pp. 1110-1111
    • Sumi, H.1    Hamada, H.2    Tsushima, H.3    Mihara, H.4    Muraki, H.5
  • 24
    • 0020602912 scopus 로고
    • Activation of plasma fibrinolysis after intrarectal administration of high molecular weight urokinase and its derivative
    • Sumi, H., M. Maruyama, T. Yoneta, and H. Mihara. 1983. Activation of plasma fibrinolysis after intrarectal administration of high molecular weight urokinase and its derivative. Acta Haematol. 70: 289-295.
    • (1983) Acta Haematol. , vol.70 , pp. 289-295
    • Sumi, H.1    Maruyama, M.2    Yoneta, T.3    Mihara, H.4
  • 25
    • 0021779484 scopus 로고
    • Plasma fibrinolysis after intraduodenal administration of urokinase in rats
    • Sumi, H., M. Seiki, N. Morimoto, H. Tsushima, M. Maruyama, and H. Mihara. 1985. Plasma fibrinolysis after intraduodenal administration of urokinase in rats. Enzyme 33: 121-127.
    • (1985) Enzyme , vol.33 , pp. 121-127
    • Sumi, H.1    Seiki, M.2    Morimoto, N.3    Tsushima, H.4    Maruyama, M.5    Mihara, H.6
  • 27
    • 0021910435 scopus 로고
    • Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins
    • Toki, N., H. Sumi, K. Sasaki, I. Boreisha, and K. C. Robbins. 1985. 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) J. Clin. Invest. , vol.75 , pp. 1212-1222
    • Toki, N.1    Sumi, H.2    Sasaki, K.3    Boreisha, I.4    Robbins, K.C.5
  • 28
    • 0029070053 scopus 로고
    • Thrombolytic agents in development
    • Verstraete, M., H. R. Lijnen, and D. Collen. 1995. Thrombolytic agents in development. Drugs 50: 29-42.
    • (1995) Drugs , vol.50 , pp. 29-42
    • Verstraete, M.1    Lijnen, H.R.2    Collen, D.3
  • 29
    • 0022174928 scopus 로고
    • Proteolytic enzymes
    • M. Moo-Young (ed.), Pergamon Press, Oxford, U.K.
    • Ward, O. P. 1985. Proteolytic enzymes, pp. 789-815. In M. Moo-Young (ed.), Comprehensive Biotechnology, vol. 3. Pergamon Press, Oxford, U.K.
    • (1985) Comprehensive Biotechnology , vol.3 , pp. 789-815
    • Ward, O.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.