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Volumn 20, Issue 5, 2010, Pages 881-888

Screening, characterization, and cloning of a solvent-tolerant protease from Serratia marcescens MH6

Author keywords

Metalloproteinase; Nonaqueous enzymology; Organic solvent tolerance; Screening; Serratia marcescens

Indexed keywords

1,10 PHENANTHROLINE; ALCOHOL; ALKANE; BACTERIAL ENZYME; CALCIUM ION; EDETIC ACID; MAGNESIUM ION; METALLOPROTEINASE; MH6 PROTEASE; NICKEL; ORGANIC SOLVENT; POLYSORBATE 80; TRITON X 100; UNCLASSIFIED DRUG;

EID: 77955002065     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0910.10038     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 0017040732 scopus 로고
    • The extracellular metalloprotease of Serratia marcescens: I. Purification and characterization
    • Aiyappa, P. S. and J. O. Harris. 1976. The extracellular metalloprotease of Serratia marcescens: I. Purification and characterization. Mol. Cell Biochem. 13: 95-100.
    • (1976) Mol. Cell Biochem , vol.13 , pp. 95-100
    • Aiyappa, P.S.1    Harris, J.O.2
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0025333259 scopus 로고
    • The metalloprotease gene of Serratia marcescens strain SM6
    • Braunagel, S. C. and M. J. Benedik. 1990. The metalloprotease gene of Serratia marcescens strain SM6. Molec. Gen. Genet. MGG 222: 446-451.
    • (1990) Molec. Gen. Genet. MGG , vol.222 , pp. 446-451
    • Braunagel, S.C.1    Benedik, M.J.2
  • 4
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • David, N. P., J. C. P. Darryl, M. C. David, and S. C. John. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • David, N.P.1    Darryl, J.C.P.2    David, M.C.3    John, S.C.4
  • 5
    • 57649178670 scopus 로고    scopus 로고
    • Isolation and screening of a novel extracellular organic solvent-stable protease producer
    • Fang, Y. W., S. Liu, S. J. Wang, and M. S. Lv. 2009. Isolation and screening of a novel extracellular organic solvent-stable protease producer. Biochem. Eng. J. 43: 212-215.
    • (2009) Biochem. Eng. J , vol.43 , pp. 212-215
    • Fang, Y.W.1    Liu, S.2    Wang, S.J.3    Lv, M.S.4
  • 6
    • 0037233491 scopus 로고    scopus 로고
    • Isolation and screening of an extracellular organic solvent-tolerant protease producer
    • Geok, L. P., C. N. A. Razak, R. N. Z. Abd Rahman, M. Basri, and A. B. Salleh. 2003. Isolation and screening of an extracellular organic solvent-tolerant protease producer. Biochem. Eng. J. 13: 73-77.
    • (2003) Biochem. Eng. J , vol.13 , pp. 73-77
    • Geok, L.P.1    Razak, C.N.A.2    Rahman, A.R.N.Z.3    Basri, M.4    Salleh, A.B.5
  • 7
    • 33745202363 scopus 로고    scopus 로고
    • A protease stable in organic solvents from solvent tolerant strain of Pseudomonas aeruginosa
    • Gupta, A. and S. K. Khare. 2006. A protease stable in organic solvents from solvent tolerant strain of Pseudomonas aeruginosa. Bioresource Technol. 97: 1788-1793.
    • (2006) Bioresource Technol , vol.97 , pp. 1788-1793
    • Gupta, A.1    Khare, S.K.2
  • 8
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization - Aqueous and non-aqueous environment
    • Iyer, P. V. and L. Ananthanarayan. 2008. Enzyme stability and stabilization - Aqueous and non-aqueous environment. Process Biochem. 43: 1019-1032.
    • (2008) Process Biochem , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 9
    • 0030031591 scopus 로고    scopus 로고
    • Isolating and characterizing deep-sea marine microorganisms
    • Kato, C., A. Inoue, and K. Horikoshi. 1996. Isolating and characterizing deep-sea marine microorganisms. Trends Biotechnol. 14: 6-12.
    • (1996) Trends Biotechnol , vol.14 , pp. 6-12
    • Kato, C.1    Inoue, A.2    Horikoshi, K.3
  • 10
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov, A. M. 2001. Improving enzymes by using them in organic solvents. Nature 409: 241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 11
    • 0346691421 scopus 로고
    • Protease stabilization by highly concentrated anionic surfactant mixtures
    • Lalonde, J., E. Witte, M. O'Connell, and L. Holliday. 1995. Protease stabilization by highly concentrated anionic surfactant mixtures. J. Am. Oil Chem. Soc. 72: 53-59.
    • (1995) J. Am. Oil Chem. Soc , vol.72 , pp. 53-59
    • Lalonde, J.1    Witte, E.2    O'Connell, M.3    Holliday, L.4
  • 12
    • 57449096150 scopus 로고    scopus 로고
    • A novel organic solvent-stable alkaline protease from organic solvent-tolerant Bacillus licheniformis YP1A
    • Li, S., B. F. He, Z. Z. Bai, and P. K. Ouyang. 2009. A novel organic solvent-stable alkaline protease from organic solvent-tolerant Bacillus licheniformis YP1A. J. Molec. Catal. B Enz. 56: 85-88.
    • (2009) J. Molec. Catal. B Enz , vol.56 , pp. 85-88
    • Li, S.1    He, B.F.2    Bai, Z.Z.3    Ouyang, P.K.4
  • 13
    • 19644372183 scopus 로고    scopus 로고
    • Isolation and characterization of benzene tolerant Rhodococcus opacus strains
    • Na, K. S., A. Kuroda, N. Takiguchi, T. Ikeda, H. Ohtake, and J. Kato. 2005. Isolation and characterization of benzene tolerant Rhodococcus opacus strains. J. Biosci. Bioeng. 99: 378-382.
    • (2005) J. Biosci. Bioeng , vol.99 , pp. 378-382
    • Na, K.S.1    Kuroda, A.2    Takiguchi, N.3    Ikeda, T.4    Ohtake, H.5    Kato, J.6
  • 15
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • Ogino, H. and H. Ishikawa. 2001. Enzymes which are stable in the presence of organic solvents. J. Biosci. Bioeng. 91: 109-116.
    • (2001) J. Biosci. Bioeng , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 16
    • 0033917914 scopus 로고    scopus 로고
    • Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03
    • Ogino, H., S. Nakagawa, K. Shinya, T. Muto, N. Fujimura, M. Yasuda, and H. Ishikawa. 2000. Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03. J. Biosci. Bioeng. 89: 451-457.
    • (2000) J. Biosci. Bioeng , vol.89 , pp. 451-457
    • Ogino, H.1    Nakagawa, S.2    Shinya, K.3    Muto, T.4    Fujimura, N.5    Yasuda, M.6    Ishikawa, H.7
  • 17
    • 34249731337 scopus 로고    scopus 로고
    • Effect of exchange of amino acid residues of the surface region of the PST-01 protease on its organic solvent-stability
    • Ogino, H., T. Uchiho, N. Doukyu, M. Yasuda, K. Ishimi, and H. Ishikawa. 2007. Effect of exchange of amino acid residues of the surface region of the PST-01 protease on its organic solvent-stability. Biochem. Biophys. Res. Commun. 358: 1028-1103.
    • (2007) Biochem. Biophys. Res. Commun , vol.358 , pp. 1028-1103
    • Ogino, H.1    Uchiho, T.2    Doukyu, N.3    Yasuda, M.4    Ishimi, K.5    Ishikawa, H.6
  • 18
    • 33748747129 scopus 로고    scopus 로고
    • An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization
    • Rahman, R. N. Z. R. A., L. P. Geok, M. Basri, and A. B. Salleh. 2006. An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization. Enz. Microb. Technol. 39: 1484-1491.
    • (2006) Enz. Microb. Technol , vol.39 , pp. 1484-1491
    • Rahman, R.N.Z.R.A.1    Geok, L.P.2    Basri, M.3    Salleh, A.B.4
  • 20
    • 59649121580 scopus 로고    scopus 로고
    • Ecological significance and some biotechnological application of an organic solvent stable alkaline serine protease from Bacillus subtilis strain DM-04
    • Rai, S. K. and A. K. Mukherjee. 2009. Ecological significance and some biotechnological application of an organic solvent stable alkaline serine protease from Bacillus subtilis strain DM-04. Bioresource Technol. 100: 2642-2645.
    • (2009) Bioresource Technol , vol.100 , pp. 2642-2645
    • Rai, S.K.1    Mukherjee, A.K.2
  • 22
    • 0035144817 scopus 로고    scopus 로고
    • Production, purification and partial characterization of two extracellular proteases from Serratia marcescens grown in whey
    • Romero, F. J., L. A. Garcia, J. A. Salas, M. Diaz, and L. M. Quiros. 2001. Production, purification and partial characterization of two extracellular proteases from Serratia marcescens grown in whey. Process Biochem. 36: 507-515.
    • (2001) Process Biochem , vol.36 , pp. 507-515
    • Romero, F.J.1    Garcia, L.A.2    Salas, J.A.3    Diaz, M.4    Quiros, L.M.5
  • 24
    • 0035991501 scopus 로고    scopus 로고
    • Tolerance of bacteria to organic solvents
    • Sardessai, Y. and S. Bhosle. 2002. Tolerance of bacteria to organic solvents. Res. Microbiol. 153: 263-268.
    • (2002) Res. Microbiol , vol.153 , pp. 263-268
    • Sardessai, Y.1    Bhosle, S.2
  • 25
    • 9644310304 scopus 로고    scopus 로고
    • Synthesis of kyotorphin precursor by an organic solvent-stable protease from Bacillus licheniformis RSP-09-37
    • Sareen, R., U. T. Bornscheuer, and P. Mishra. 2004. Synthesis of kyotorphin precursor by an organic solvent-stable protease from Bacillus licheniformis RSP-09-37. J. Molec. Catal. B Enz. 32: 1-5.
    • (2004) J. Molec. Catal. B Enz , vol.32 , pp. 1-5
    • Sareen, R.1    Bornscheuer, U.T.2    Mishra, P.3
  • 26
    • 0026212764 scopus 로고
    • Purification and properties of a novel surface active agent and alkaline resistant protease from Bacillus sp
    • Shimogaki, H., K. Takeuchi, T. Nishino, M. Ohdera, T. Kudo, K. Ohba, M. Iwama, and M. Irie. 1991. Purification and properties of a novel surface active agent and alkaline resistant protease from Bacillus sp. Y. Agric. Biol. Chem. 55: 2251-2258.
    • (1991) Y. Agric. Biol. Chem , vol.55 , pp. 2251-2258
    • Shimogaki, H.1    Takeuchi, K.2    Nishino, T.3    Ohdera, M.4    Kudo, T.5    Ohba, K.6    Iwama, M.7    Irie, M.8
  • 27
    • 34247366868 scopus 로고    scopus 로고
    • Nonionic surfactants: A key to enhance the enzyme activity at cationic reverse micellar interface
    • Shome, A., S. Roy, and P. K. Das. 2007. Nonionic surfactants: A key to enhance the enzyme activity at cationic reverse micellar interface. Langmuir 23: 4130-4136.
    • (2007) Langmuir , vol.23 , pp. 4130-4136
    • Shome, A.1    Roy, S.2    Das, P.K.3
  • 28
    • 0034135723 scopus 로고    scopus 로고
    • Protease-catalyzed tripeptide (RGD) synthesis
    • So, J. E., J. S. Shin, and B. G. Kim. 2000. Protease-catalyzed tripeptide (RGD) synthesis. Enz. Microb. Technol. 26: 108-114.
    • (2000) Enz. Microb. Technol , vol.26 , pp. 108-114
    • So, J.E.1    Shin, J.S.2    Kim, B.G.3
  • 29
    • 77949292306 scopus 로고    scopus 로고
    • Biochemical properties and potential applications of a solvent-stable protease from the high-yield protease producer Pseudomonas aeruginosa PT121
    • Tang, X. Y., B. Wu, H. J. Ying, and B. F. He. Biochemical properties and potential applications of a solvent-stable protease from the high-yield protease producer Pseudomonas aeruginosa PT121. Appl. Biochem. Biotechnol. 160: 1017-1031.
    • Appl. Biochem. Biotechnol , vol.160 , pp. 1017-1031
    • Tang, X.Y.1    Wu, B.2    Ying, H.J.3    He, B.F.4
  • 30
    • 44449086298 scopus 로고    scopus 로고
    • Screening and isolation of an organic solvent-tolerant bacterium for high-yield production of organic solvent-stable protease
    • Tang, X. Y., Y. Pan, S. Li, and B. F. He. 2008. Screening and isolation of an organic solvent-tolerant bacterium for high-yield production of organic solvent-stable protease. Bioresource Technol. 99: 7388-7392.
    • (2008) Bioresource Technol , vol.99 , pp. 7388-7392
    • Tang, X.Y.1    Pan, Y.2    Li, S.3    He, B.F.4
  • 31
    • 34547918897 scopus 로고    scopus 로고
    • Peptide synthesis of aspartame precursor using organic-solvent-stable PST-01 protease in monophasic aqueous-organic solvent systems
    • Tsuchiyama, S., N. Doukyu, M. Yasuda, K. Ishimi, and H. Ogino. 2007. Peptide synthesis of aspartame precursor using organic-solvent-stable PST-01 protease in monophasic aqueous-organic solvent systems. Biotechnol. Progr. 23: 820-823.
    • (2007) Biotechnol. Progr , vol.23 , pp. 820-823
    • Tsuchiyama, S.1    Doukyu, N.2    Yasuda, M.3    Ishimi, K.4    Ogino, H.5
  • 33
    • 43049117464 scopus 로고    scopus 로고
    • Purification and characterization of a chitosanase from Serratia marcescens TKU011
    • Wang, S. L., J. H. Peng, T. W. Liang, and K. C. Liu. 2008. Purification and characterization of a chitosanase from Serratia marcescens TKU011. Carbohydr. Res. 343: 1316-1323.
    • (2008) Carbohydr. Res , vol.343 , pp. 1316-1323
    • Wang, S.L.1    Peng, J.H.2    Liang, T.W.3    Liu, K.C.4
  • 34
    • 2942748507 scopus 로고    scopus 로고
    • Industrial potential of organic solvent tolerant bacteria
    • Yogita, N. and S. B. Sardessai. 2004. Industrial potential of organic solvent tolerant bacteria. Biotechnol. Progress 20: 655-660.
    • (2004) Biotechnol. Progress , vol.20 , pp. 655-660
    • Yogita, N.1    Sardessai, S.B.2
  • 35
    • 42749092984 scopus 로고    scopus 로고
    • Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010
    • Zhao, L. L., J. H. Xu, J. Zhao, J. Pan, and Z. L. Wang. 2008. Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010. Process Biochem. 43: 626-633.
    • (2008) Process Biochem , vol.43 , pp. 626-633
    • Zhao, L.L.1    Xu, J.H.2    Zhao, J.3    Pan, J.4    Wang, Z.L.5


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