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Volumn 47, Issue 6, 2010, Pages 297-304

Medium optimization and immobilization of purified fibrinolytic URAK from Bacillus cereus NK1 on PHB nanoparticles

Author keywords

Bacillus cereus NK1; Batch fermentation; Immobilization; Purification; RSM; URAK

Indexed keywords

BATCH FERMENTATION; BLOOD CLOTS; CARDIO-VASCULAR DISEASE; CENTRAL COMPOSITE ROTARY DESIGN; DEGRADING ENZYMES; EXTRACELLULAR PROTEASE; FERMENTORS; IMMOBILIZATION; ION EXCHANGE CHROMATOGRAPHY; MEDIUM OPTIMIZATION; PRODUCTION MEDIUM; RESPONSE SURFACE METHODOLOGY; RSM; SHAKE-FLASK CULTURES; SOYBEAN MEAL; URAK;

EID: 77956456332     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2010.07.004     Document Type: Article
Times cited : (32)

References (35)
  • 1
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar L., Nesheim M.E., Tracy P.B. The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 1996, 88(6):2093-2100.
    • (1996) Blood , vol.88 , Issue.6 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 2
    • 0021260107 scopus 로고
    • Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urokinase) a study in vitro and in two animal species
    • Gurewich V., Pannell R., Louie S., Kelley P., Suddith R.L., Greenlee R. Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urokinase) a study in vitro and in two animal species. J Clin Invest 1984, 73:1731-1739.
    • (1984) J Clin Invest , vol.73 , pp. 1731-1739
    • Gurewich, V.1    Pannell, R.2    Louie, S.3    Kelley, P.4    Suddith, R.L.5    Greenlee, R.6
  • 3
    • 5144220471 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator: a historical perspective and personal account
    • Collen D., Lijnen H.R. Tissue-type plasminogen activator: a historical perspective and personal account. J Thromb Haemost 2004, 2:541-546.
    • (2004) J Thromb Haemost , vol.2 , pp. 541-546
    • Collen, D.1    Lijnen, H.R.2
  • 4
    • 0021989853 scopus 로고
    • Randomised trial of intravenous recombinant tissue-type plasminogen activator versus intravenous streptokinase in acute myocardial infarction: report from the European Cooperative Study Group for recombinant tissue-type plasminogen activator
    • Verstraete M., Bory M., Collen D., Erbel R., Lennane R.J., Mathey D., et al. Randomised trial of intravenous recombinant tissue-type plasminogen activator versus intravenous streptokinase in acute myocardial infarction: report from the European Cooperative Study Group for recombinant tissue-type plasminogen activator. Lancet 1985, 325(8433):842-847.
    • (1985) Lancet , vol.325 , Issue.8433 , pp. 842-847
    • Verstraete, M.1    Bory, M.2    Collen, D.3    Erbel, R.4    Lennane, R.J.5    Mathey, D.6
  • 5
    • 0031941584 scopus 로고    scopus 로고
    • Staphylokinase: a potent, uniquely fibrin-selective thrombolytic agent
    • Collen D. Staphylokinase: a potent, uniquely fibrin-selective thrombolytic agent. Nat Med 1998, 4:279-284.
    • (1998) Nat Med , vol.4 , pp. 279-284
    • Collen, D.1
  • 6
    • 0032532396 scopus 로고    scopus 로고
    • Risk for intracranial hemorrhage after tissue plasminogen activator treatment for acute myocardial infarction
    • Gurwitz J.H., Gore J.M., Goldberg R.J., Barron H.V., Breen T., Rundle A.C., et al. Risk for intracranial hemorrhage after tissue plasminogen activator treatment for acute myocardial infarction. Ann Intern Med 1998, 129:597-604.
    • (1998) Ann Intern Med , vol.129 , pp. 597-604
    • Gurwitz, J.H.1    Gore, J.M.2    Goldberg, R.J.3    Barron, H.V.4    Breen, T.5    Rundle, A.C.6
  • 7
    • 85007755756 scopus 로고    scopus 로고
    • ABC of antithrombotic therapy: an overview of antithrombotic therapy
    • Blann A.D., Landray M.J., Lip G.Y. ABC of antithrombotic therapy: an overview of antithrombotic therapy. Br Med J 2005, 325:762-765.
    • (2005) Br Med J , vol.325 , pp. 762-765
    • Blann, A.D.1    Landray, M.J.2    Lip, G.Y.3
  • 8
    • 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., Hamada H., Tsushima H., Mihara H., Muraki H. A novel fibrinolytic enzyme nattokinase in the vegetable cheese natto; a typical and popular soybean food in the Japanese diet. Experientia 1987, 15:1110-1111.
    • (1987) Experientia , vol.15 , pp. 1110-1111
    • Sumi, H.1    Hamada, H.2    Tsushima, H.3    Mihara, H.4    Muraki, H.5
  • 9
    • 2342617401 scopus 로고    scopus 로고
    • Natto Bacillus as an oral fibrinolytic agent: nattokinase activity and the ingestion effect of Bacillus subtilis natto
    • Sumi H., Yanagisawa Y., Yatagai C., Saito J. Natto Bacillus as an oral fibrinolytic agent: nattokinase activity and the ingestion effect of Bacillus subtilis natto. Food Sci Technol Res 2004, 10(1):17-20.
    • (2004) Food Sci Technol Res , vol.10 , Issue.1 , pp. 17-20
    • Sumi, H.1    Yanagisawa, Y.2    Yatagai, C.3    Saito, J.4
  • 10
    • 29144505132 scopus 로고    scopus 로고
    • Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo
    • Peng Y., Yang X., Zhang Y. Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo. Appl Microbiol Biotechnol 2005, 69:126-132.
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 126-132
    • Peng, Y.1    Yang, X.2    Zhang, Y.3
  • 11
    • 0029013691 scopus 로고
    • Characterization of nattokinase-degraded products from human fibrinogen or cross-linked fibrin
    • Fujita M., Ito Y., Hong K., Nishimuro S. Characterization of nattokinase-degraded products from human fibrinogen or cross-linked fibrin. Fibrinolysis 1995, 9(3):157-164.
    • (1995) Fibrinolysis , vol.9 , Issue.3 , pp. 157-164
    • Fujita, M.1    Ito, Y.2    Hong, K.3    Nishimuro, S.4
  • 12
    • 37149052902 scopus 로고    scopus 로고
    • Medium optimization for the production of recombinant nattokinase by Bacillus subtilis using response surface methodology
    • Chen P.T., Chiang C., Chao Y. Medium optimization for the production of recombinant nattokinase by Bacillus subtilis using response surface methodology. Biotechnol Prog 2007, 23:1327-1332.
    • (2007) Biotechnol Prog , vol.23 , pp. 1327-1332
    • Chen, P.T.1    Chiang, C.2    Chao, Y.3
  • 14
    • 53649086316 scopus 로고    scopus 로고
    • Medium optimization for the production of cyclic adenosine 3',5'-monophosphate by Microbacterium sp. no. 205 using response surface methodology
    • Chen X., Bai J., Cao J., Li Z., Xiong J., Zhang L., et al. Medium optimization for the production of cyclic adenosine 3',5'-monophosphate by Microbacterium sp. no. 205 using response surface methodology. Bioresour Technol 2009, 100(2):919-924.
    • (2009) Bioresour Technol , vol.100 , Issue.2 , pp. 919-924
    • Chen, X.1    Bai, J.2    Cao, J.3    Li, Z.4    Xiong, J.5    Zhang, L.6
  • 16
    • 0034556033 scopus 로고    scopus 로고
    • Production of poly3-hydroxybutyrate from inexpensive substrates
    • Kim B.S. Production of poly3-hydroxybutyrate from inexpensive substrates. Enzyme Microb Technol 2000, 27:774-777.
    • (2000) Enzyme Microb Technol , vol.27 , pp. 774-777
    • Kim, B.S.1
  • 17
    • 9244255681 scopus 로고    scopus 로고
    • Formulation aspects of biodegradable polymeric microspheres for antigen delivery
    • Tamber H., Johansen P., Merkle H.P., Gander B. Formulation aspects of biodegradable polymeric microspheres for antigen delivery. Adv Drug Deliver Rev 2005, 57:357-376.
    • (2005) Adv Drug Deliver Rev , vol.57 , pp. 357-376
    • Tamber, H.1    Johansen, P.2    Merkle, H.P.3    Gander, B.4
  • 18
    • 0037151546 scopus 로고    scopus 로고
    • Submicronparticles from biodegradable polymers
    • Jobmann M., Rafler G. Submicronparticles from biodegradable polymers. Int J Pharm 2002, 242:213-217.
    • (2002) Int J Pharm , vol.242 , pp. 213-217
    • Jobmann, M.1    Rafler, G.2
  • 19
    • 0036707316 scopus 로고    scopus 로고
    • Biodegradable nanoparticles for drug delivery and targeting
    • Hans M.L., Lowmanm A.M. Biodegradable nanoparticles for drug delivery and targeting. Curr Opin Solid State Mater Sci 2002, 63:19-327.
    • (2002) Curr Opin Solid State Mater Sci , vol.63 , pp. 19-327
    • Hans, M.L.1    Lowmanm, A.M.2
  • 20
    • 0026008520 scopus 로고
    • Enzyme stabilization: state of the art
    • Gianfreda L., Scarfi M.R. Enzyme stabilization: state of the art. Mol Cell Biochem 1991, 100:97-128.
    • (1991) Mol Cell Biochem , vol.100 , pp. 97-128
    • Gianfreda, L.1    Scarfi, M.R.2
  • 22
    • 52949120292 scopus 로고    scopus 로고
    • Improvement of the stability of nattokinase using γ-polyglutamic acid as a coating material for microencapsulation
    • Hsieh C.W., Lu W.C., Hsieh W.C., Huang Y.P., Lai C.H., Ko W.C. Improvement of the stability of nattokinase using γ-polyglutamic acid as a coating material for microencapsulation. LWT - Food Sci Technol 2009, 42:144-149.
    • (2009) LWT - Food Sci Technol , vol.42 , pp. 144-149
    • Hsieh, C.W.1    Lu, W.C.2    Hsieh, W.C.3    Huang, Y.P.4    Lai, C.H.5    Ko, W.C.6
  • 23
    • 69049101903 scopus 로고    scopus 로고
    • Purification, immobilization, and characterization of nattokinase on PHB nanoparticles
    • Deepak V., Pandian S.R., Kalishwaralal K., Gurunathan S. Purification, immobilization, and characterization of nattokinase on PHB nanoparticles. Bioresour Technol 2009, 100(24):6644-6646.
    • (2009) Bioresour Technol , vol.100 , Issue.24 , pp. 6644-6646
    • Deepak, V.1    Pandian, S.R.2    Kalishwaralal, K.3    Gurunathan, S.4
  • 24
    • 0033037037 scopus 로고    scopus 로고
    • A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds
    • Spiekermann P.B., Rehm H., Kalscheuer R., Baumeister D., Steinbüchel A. A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds. Arch Microbiol 1999, 171(2):73-80.
    • (1999) Arch Microbiol , vol.171 , Issue.2 , pp. 73-80
    • Spiekermann, P.B.1    Rehm, H.2    Kalscheuer, R.3    Baumeister, D.4    Steinbüchel, A.5
  • 25
    • 77956486291 scopus 로고    scopus 로고
    • Optimization of nutritional conditions for Nattokinase production by an isolated Bacillus subtilis from natto health food. A Master of Science Thesis, Tatung University;
    • Wu SY. Optimization of nutritional conditions for Nattokinase production by an isolated Bacillus subtilis from natto health food. A Master of Science Thesis, Tatung University; 2005.
    • (2005)
    • Wu, S.Y.1
  • 26
    • 70349435272 scopus 로고    scopus 로고
    • Optimization and fed-batch production of PHB utilizing dairy waste and sea water as nutrient sources by Bacillus megaterium SRKP-3
    • 2010
    • Pandian S.R., Deepak V., Kalishwaralal K., Rameshkumar N., Jeyaraj M., Gurunathan S. Optimization and fed-batch production of PHB utilizing dairy waste and sea water as nutrient sources by Bacillus megaterium SRKP-3. Bioresour Technol 2010, 101(2):705-711. 2010.
    • (2010) Bioresour Technol , vol.101 , Issue.2 , pp. 705-711
    • Pandian, S.R.1    Deepak, V.2    Kalishwaralal, K.3    Rameshkumar, N.4    Jeyaraj, M.5    Gurunathan, S.6
  • 28
    • 33846639223 scopus 로고    scopus 로고
    • Brain injury after intracerebral hemorrhage: the role of thrombin and iron
    • Hua Y., Keep R.F., Hoff J.T., Xi G. Brain injury after intracerebral hemorrhage: the role of thrombin and iron. Stroke 2007, 38:759-762.
    • (2007) Stroke , vol.38 , pp. 759-762
    • Hua, Y.1    Keep, R.F.2    Hoff, J.T.3    Xi, G.4
  • 29
    • 0037229448 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food
    • Peng Y., Huang Q., Zhang R., Zhang Y. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Phys B 2003, 134:45-52.
    • (2003) Comp Biochem Phys B , vol.134 , pp. 45-52
    • Peng, Y.1    Huang, Q.2    Zhang, R.3    Zhang, Y.4
  • 30
    • 33947433255 scopus 로고    scopus 로고
    • Application of thiolated gold nanoparticles for the enhancement of glucose oxidase activity
    • Pandey P., Singh S.P., Arya S.K., Gupta V., Datta M., Singh S., et al. Application of thiolated gold nanoparticles for the enhancement of glucose oxidase activity. Langmuir 2007, 23(6):3333-3337.
    • (2007) Langmuir , vol.23 , Issue.6 , pp. 3333-3337
    • Pandey, P.1    Singh, S.P.2    Arya, S.K.3    Gupta, V.4    Datta, M.5    Singh, S.6
  • 31
    • 33847216926 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability
    • Li D., He Q., Cui Y., Duan L., Li J. Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability. Biochem Biophys Res Commun 2007, 355(2):488-493.
    • (2007) Biochem Biophys Res Commun , vol.355 , Issue.2 , pp. 488-493
    • Li, D.1    He, Q.2    Cui, Y.3    Duan, L.4    Li, J.5
  • 33
    • 15744369257 scopus 로고    scopus 로고
    • Optimization of nutritional condition for Nattokinase production by Bacillus natto NLSSE using statistical experimental methods
    • Liu J., Xing J., Chang T., Ma Z., Liu H. Optimization of nutritional condition for Nattokinase production by Bacillus natto NLSSE using statistical experimental methods. Process Biochem 2005, 40:2757-2762.
    • (2005) Process Biochem , vol.40 , pp. 2757-2762
    • Liu, J.1    Xing, J.2    Chang, T.3    Ma, Z.4    Liu, H.5
  • 34
    • 0037202148 scopus 로고    scopus 로고
    • Lipophilic drug loaded nanospheres prepared by nanoprecipitation: effect of formulation variables on size, drug recovery and release kinetics
    • Chorny M., Fishbein I., Danenberg H.D., Golomb G. Lipophilic drug loaded nanospheres prepared by nanoprecipitation: effect of formulation variables on size, drug recovery and release kinetics. J Controlled Release 2002, 83:389-400.
    • (2002) J Controlled Release , vol.83 , pp. 389-400
    • Chorny, M.1    Fishbein, I.2    Danenberg, H.D.3    Golomb, G.4
  • 35
    • 21144438468 scopus 로고    scopus 로고
    • Production of catechol-siderophore and utilization of transferrin-bound iron in Bacillus cereus
    • Park R.Y., Choi M.H., Sun H.Y., Shin S.H. Production of catechol-siderophore and utilization of transferrin-bound iron in Bacillus cereus. Biol Pharm Bull 2005, 28(6):1132-1135.
    • (2005) Biol Pharm Bull , vol.28 , Issue.6 , pp. 1132-1135
    • Park, R.Y.1    Choi, M.H.2    Sun, H.Y.3    Shin, S.H.4


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