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Volumn 31, Issue 10, 2010, Pages 1061-1072

Purification and characterization of a solvent-stable protease from Geomicrobium sp. EMB2

Author keywords

Detergent compatible; Haloalkaliphiles; Protease purification; Salt; Solvent stability

Indexed keywords

AMINO ACIDS; ENZYMES; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBICITY; ORGANIC SOLVENTS; PHOSPHATASES; SOAPS (DETERGENTS); SODIUM CHLORIDE; STABILITY; SURFACE ACTIVE AGENTS;

EID: 77953754385     PISSN: 09593330     EISSN: 1479487X     Source Type: Journal    
DOI: 10.1080/09593331003674556     Document Type: Article
Times cited : (37)

References (47)
  • 1
    • 34447313904 scopus 로고    scopus 로고
    • The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents
    • J. Mansfeld and R. Ulbrich-Hofmann, The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents, Biotechnol. Bioeng. 97 (2007), pp. 672-679.
    • (2007) Biotechnol. Bioeng. , vol.97 , pp. 672-679
    • Mansfeld, J.1    Ulbrich-Hofmann, R.2
  • 2
    • 3042807068 scopus 로고    scopus 로고
    • Enzymes in organic media
    • M.N. Gupta and I. Roy, Enzymes in organic media, Eur. J. Biochem. 271 (2004), pp. 2575-2583.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2575-2583
    • Gupta, M.N.1    Roy, I.2
  • 3
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • H. Ogino and H. Ishikawa, Enzymes which are stable in the presence of organic solvents, J. Biosci. Bioeng. 91 (2001), pp. 109-116.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 4
    • 11144243173 scopus 로고    scopus 로고
    • The biocatalytic potential of extremophiles and extremozymes
    • J. Gomes and W. Steiner, The biocatalytic potential of extremophiles and extremozymes, Food Technol. Biotechnol. 42 (2004), pp. 223-235.
    • (2004) Food Technol. Biotechnol. , vol.42 , pp. 223-235
    • Gomes, J.1    Steiner, W.2
  • 5
    • 0035319086 scopus 로고    scopus 로고
    • Potential of halotolerant and halophilic microorganisms for biotechnology
    • R. Margesin and F. Schinner, Potential of halotolerant and halophilic microorganisms for biotechnology, Extremophiles 5 (2001), pp. 73-83.
    • (2001) Extremophiles , vol.5 , pp. 73-83
    • Margesin, R.1    Schinner, F.2
  • 6
    • 0031810562 scopus 로고    scopus 로고
    • Biology of moderately halophilic aerobic bacteria
    • A. Ventosa, J.J. Nieto, and A. Oren, Biology of moderately halophilic aerobic bacteria, Microbiol. Mol. Biol. Rev. 62 (1998), pp. 504-544.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 504-544
    • Ventosa, A.1    Nieto, J.J.2    Oren, A.3
  • 7
    • 42949104034 scopus 로고    scopus 로고
    • Microbial life at high salt concentrations: Phylogenetic and metabolic diversity
    • DOI 10.1186/1746-1448-4-2
    • A. Oren, Microbial life at high salt concentrations: Phylogenetic and metabolic diversity, Saline Systems 4 (2008), doi 10.1186/1746-1448-4-2 (Pubitemid 351607636)
    • (2008) Saline Systems , vol.4 , Issue.1 , pp. 2
    • Oren, A.1
  • 9
    • 0031554717 scopus 로고    scopus 로고
    • Unusual salt and solvent dependence of a protease from an extreme halophile
    • J. Kim and J.S. Dordick, Unusual salt and solvent dependence of a protease from an extreme halophile, Biotechnol. Bioeng. 55 (1997), pp. 471-479.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 471-479
    • Kim, J.1    Dordick, J.S.2
  • 10
    • 33846409885 scopus 로고    scopus 로고
    • Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii
    • D.M. Ruiz and R.E.D. Castro, Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii, J. Ind. Microbiol. Biotechnol. 34 (2007), pp. 111-115.
    • (2007) J. Ind. Microbiol. Biotechnol. , vol.34 , pp. 111-115
    • Ruiz, D.M.1    Castro, R.E.D.2
  • 11
    • 33847273658 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents
    • H.R. Karbalaei-Heidari, A.A. Ziaee, and M.A. Amoozegar, Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents, Extremophiles 11 (2007), pp. 237-243.
    • (2007) Extremophiles , vol.11 , pp. 237-243
    • Karbalaei-Heidari, H.R.1    Ziaee, A.A.2    Amoozegar, M.A.3
  • 12
    • 76349122463 scopus 로고    scopus 로고
    • Purification and biological characterization of a halophilic thermostable protease from Haloferax lucentensis VKMM 007
    • M. Manikandan, L. Paší, and V. Kannan, Purification and biological characterization of a halophilic thermostable protease from Haloferax lucentensis VKMM 007, World J. Microbiol. Biotechnol. 25 (2009), pp. 2247-2256.
    • (2009) World J. Microbiol. Biotechnol. , vol.25 , pp. 2247-2256
    • Manikandan, M.1    Paší, L.2    Kannan, V.3
  • 13
    • 34748895406 scopus 로고    scopus 로고
    • Production of an extracellular alkaline metalloprotease from a newly isolated, moderately halophile, Salinivibrio sp. strain AF-2004
    • M.A. Amoozegar, A.Z. Fatemi, H.R. Karbalaei- Heidari, and M.R. Razavi, Production of an extracellular alkaline metalloprotease from a newly isolated, moderately halophile, Salinivibrio sp. strain AF-2004, Microbiol. Res. 62 (2007), pp. 369-377.
    • (2007) Microbiol. Res. , vol.62 , pp. 369-377
    • Amoozegar, M.A.1    Fatemi, A.Z.2    Karbalaei-Heidari, H.R.3    Razavi, M.R.4
  • 14
    • 58949094567 scopus 로고    scopus 로고
    • Isolation and identification of alkaline protease producing alkaliphilic bacteria from an Egyptian soda lake
    • A.S.S. Ibrahim, N.M.A. EI-Shayeb, and S.S. Mabrouk, Isolation and identification of alkaline protease producing alkaliphilic bacteria from an Egyptian soda lake, J. Appl. Sci. Res. 3 (2007), pp. 1363-1368.
    • (2007) J. Appl. Sci. Res. , vol.3 , pp. 1363-1368
    • Ibrahim, A.S.S.1    Ei-Shayeb, N.M.A.2    Mabrouk, S.S.3
  • 15
    • 33748588406 scopus 로고    scopus 로고
    • Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archaeon Halogeometricum sp. TSS101
    • M. Vidyasagar, S.B. Prakash, and K. Sreeramulu, Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archaeon Halogeometricum sp. TSS101, Lett. Appl. Microbiol. 43 (2006), pp. 385-391.
    • (2006) Lett. Appl. Microbiol. , vol.43 , pp. 385-391
    • Vidyasagar, M.1    Prakash, S.B.2    Sreeramulu, K.3
  • 16
    • 34248177816 scopus 로고    scopus 로고
    • Optimization of culture conditions for the production of halothermophilic protease from halophilic bacterium Chromohalobacter sp. TVSP101
    • M. Vidyasagar, S. Prakash, S.K. Jayalakshmi, and K. Sreeramulu, Optimization of culture conditions for the production of halothermophilic protease from halophilic bacterium Chromohalobacter sp. TVSP101, World J. Microbiol. Biotechnol. 23 (2007), pp. 655-662.
    • (2007) World J. Microbiol. Biotechnol. , vol.23 , pp. 655-662
    • Vidyasagar, M.1    Prakash, S.2    Jayalakshmi, S.K.3    Sreeramulu, K.4
  • 17
    • 57649225420 scopus 로고    scopus 로고
    • Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis
    • H.R. Karbalaei-Heidari, M.A. Amoozegar, M. Hajighasemi, A.A. Ziaee, and A. Ventosa, Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis, J. Ind. Microbiol. Biotechnol. 36 (2009), pp. 21-27.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 21-27
    • Karbalaei-Heidari, H.R.1    Amoozegar, M.A.2    Hajighasemi, M.3    Ziaee, A.A.4    Ventosa, A.5
  • 18
    • 70349454241 scopus 로고    scopus 로고
    • Molecular analysis of the gene encoding a cold-adapted halophilic subtilase from deep-sea psychrotolerant bacterium Pseudoalteromonas sp. SM9913: Cloning, expression, characterization and function analysis of the C-terminal PPC domains
    • B.Q. Yan, X.L. Chen, X.Y. Hou, H. He, B.C. Zhou, and Y.Z. Zhang, Molecular analysis of the gene encoding a cold-adapted halophilic subtilase from deep-sea psychrotolerant bacterium Pseudoalteromonas sp. SM9913: Cloning, expression, characterization and function analysis of the C-terminal PPC domains, Extremophiles 4 (2009), pp. 725-733.
    • (2009) Extremophiles , vol.4 , pp. 725-733
    • Yan, B.Q.1    Chen, X.L.2    Hou, X.Y.3    He, H.4    Zhou, B.C.5    Zhang, Y.Z.6
  • 19
    • 37549005219 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli
    • H.R. Karbalaei-Heidari, A.A. Ziaee, M.A. Amoozegar, Y. Cheburkin, and N. Budisa, Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli, Gene 408 (2008), pp. 196-203.
    • (2008) Gene , vol.408 , pp. 196-203
    • Karbalaei-Heidari, H.R.1    Ziaee, A.A.2    Amoozegar, M.A.3    Cheburkin, Y.4    Budisa, N.5
  • 20
    • 33751107167 scopus 로고    scopus 로고
    • An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: Gene cloning, expression and characterization
    • W. Shi, X.F. Tang, Y. Huang, F. Gan, B. Tang, and P. Shen, An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: Gene cloning, expression and characterization, Extremophiles 10 (2006), pp. 599-606.
    • (2006) Extremophiles , vol.10 , pp. 599-606
    • Shi, W.1    Tang, X.F.2    Huang, Y.3    Gan, F.4    Tang, B.5    Shen, P.6
  • 21
    • 77953780764 scopus 로고    scopus 로고
    • Bioseparation of proteins: Some cutting edge technologies
    • M.N. Gupta and I. Roy, Bioseparation of proteins: Some cutting edge technologies, Chem. World 1 (2002), pp. 30-31.
    • (2002) Chem. World , vol.1 , pp. 30-31
    • Gupta, M.N.1    Roy, I.2
  • 22
    • 0026212764 scopus 로고
    • Purification and properties of a novel surface active agent and alkaline- resistant protease from Bacillus sp
    • H. Shimogaki, K. Takeuchi, T. Nishino, M. Ohdera, T. Kudo, K. Ohba, M. Iwama, and M. Irie, Purification and properties of a novel surface active agent and alkaline- resistant protease from Bacillus sp., Agric. Biol. Chem. 55 (1991), pp. 2251-2258.
    • (1991) 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
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976), pp. 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970), pp. 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • C. Heussen and E.B. Dowdle, Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates, Anal. Biochem. 102 (1980), pp. 196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 26
    • 28944442196 scopus 로고    scopus 로고
    • Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma- Proteobacterium isolated from the marine environment of the Sundarbans
    • B. Sana, D. Ghosh, M. Saha, and J. Mukherjee, Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma- Proteobacterium isolated from the marine environment of the Sundarbans, Process Biochem. 41 (2006), pp. 208-215.
    • (2006) Process Biochem. , vol.41 , pp. 208-215
    • Sana, B.1    Ghosh, D.2    Saha, M.3    Mukherjee, J.4
  • 27
    • 0029072044 scopus 로고
    • Pseudolysin and other pathogen endopeptidases of thermolysin family
    • K. Morihara, Pseudolysin and other pathogen endopeptidases of thermolysin family, Methods Enzymol. 248 (1995), pp. 242-253.
    • (1995) Methods Enzymol. , vol.248 , pp. 242-253
    • Morihara, K.1
  • 28
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • B.F. Erlanger, N. Kokowsky, and W. Cohen, The preparation and properties of two new chromogenic substrates of trypsin, Arch. Biochem. Biophys. 95 (1961), pp. 271-278.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 30
    • 77953741475 scopus 로고    scopus 로고
    • Geomicrobium halophilum gen. nov., sp. nov., moderately halophilic and alkaliphilic bacteria isolated from soil samples
    • doi: ijs.0.013268-0
    • A. Echigo, H. Minegishi, T. Mizuki, M. Kamekura, and R. Usami, Geomicrobium halophilum gen. nov., sp. nov., moderately halophilic and alkaliphilic bacteria isolated from soil samples, Int. J. Syst. Evol. Microbiol. (2009), doi: ijs.0.013268-0.
    • (2009) Int. J. Syst. Evol. Microbiol.
    • Echigo, A.1    Minegishi, H.2    Mizuki, T.3    Kamekura, M.4    Usami, R.5
  • 31
    • 38049068849 scopus 로고    scopus 로고
    • Purification and stability characteristics of an alkaline serine protease from a newly isolated Haloalkaliphilic bacterium sp. AH-6
    • M.S. Dodia, C.M. Rawal, H.G. Bhimani, R.H. Joshi, S.K. Khare, and S.P. Singh, Purification and stability characteristics of an alkaline serine protease from a newly isolated Haloalkaliphilic bacterium sp. AH-6, J. Ind. Microbiol. Biotechnol. 35 (2008), pp. 121-131.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 121-131
    • Dodia, M.S.1    Rawal, C.M.2    Bhimani, H.G.3    Joshi, R.H.4    Khare, S.K.5    Singh, S.P.6
  • 32
    • 19344365162 scopus 로고    scopus 로고
    • One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp
    • A. Gupta, I. Roy, R.K. Patel, S.P. Singh, S.K. Khare, and M.N. Gupta, One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp., J. Chromatogr. A 1075 (2005), pp. 103-108.
    • (2005) J. Chromatogr. A , vol.1075 , pp. 103-108
    • Gupta, A.1    Roy, I.2    Patel, R.K.3    Singh, S.P.4    Khare, S.K.5    Gupta, M.N.6
  • 34
    • 0037735436 scopus 로고
    • J.G. Holt, N.R. Krieg, P.H.A. Sneath, J.T. Staley, and S.T. Williams (eds.) 9th ed., Williams & Wilkins, Baltimore, MD
    • J.G. Holt, N.R. Krieg, P.H.A. Sneath, J.T. Staley, and S.T. Williams (eds.), Bergey's Manual of Determinative Bacteriology, 9th ed., Williams & Wilkins, Baltimore, MD, 1994.
    • (1994) Bergey's Manual of Determinative Bacteriology
  • 35
    • 33748106363 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101
    • M. Vidyasagar, S. Prakash, C. Litchfield, and K. Sreeramulu, Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101, Archaea 2 (2006), pp. 51-57.
    • (2006) Archaea , vol.2 , pp. 51-57
    • Vidyasagar, M.1    Prakash, S.2    Litchfield, C.3    Sreeramulu, K.4
  • 36
    • 0034199501 scopus 로고    scopus 로고
    • Extracellular protease of Natrialba magadii: Purification and biochemical characterization
    • M.I. Gimenez, C.A. Studdert, J.J. Sanchez, and R.E. De Castro, Extracellular protease of Natrialba magadii: Purification and biochemical characterization, Extremophiles 4 (2000), pp. 181-188.
    • (2000) Extremophiles , vol.4 , pp. 181-188
    • Gimenez, M.I.1    Studdert, C.A.2    Sanchez, J.J.3    De Castro, R.E.4
  • 37
    • 33745514465 scopus 로고    scopus 로고
    • Halophilic serine protease from Halobacillus sp. SR 5-3 isolated from fish sauce: Purification and characterization
    • S. Namwong, T. Hiroga, K. Takada, M. Tsunemi, S. Tanasupawat, and K. Oda, Halophilic serine protease from Halobacillus sp. SR 5-3 isolated from fish sauce: Purification and characterization, Biosci. Biotechnol. Biochem. 70 (2006), pp. 1395-1401.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1395-1401
    • Namwong, S.1    Hiroga, T.2    Takada, K.3    Tsunemi, M.4    Tanasupawat, S.5    Oda, K.6
  • 38
    • 0021142304 scopus 로고
    • High-performance hydrophobic interaction chromatography of proteins
    • J.L. Fausnaijgh, E. Pfannkoch, S. Gupta, and F.E. Regnier, High-performance hydrophobic interaction chromatography of proteins, Anal. Biochem. 137 (1984), pp. 464-477.
    • (1984) Anal. Biochem. , vol.137 , pp. 464-477
    • Fausnaijgh, J.L.1    Pfannkoch, E.2    Gupta, S.3    Regnier, F.E.4
  • 39
    • 1542649404 scopus 로고    scopus 로고
    • Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76
    • C. Sanchez-Porro, E. Mellado, C. Bertoldo, G. Antranikian, and A. Ventosa, Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76, Extremophiles 7 (2003), pp. 221-228.
    • (2003) Extremophiles , vol.7 , pp. 221-228
    • Sanchez-Porro, C.1    Mellado, E.2    Bertoldo, C.3    Antranikian, G.4    Ventosa, A.5
  • 41
    • 33746375656 scopus 로고    scopus 로고
    • Purification and characterization of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp
    • R.K. Patel, M.S. Dodia, R.H. Joshi, and S.P. Singh, Purification and characterization of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp., Process Biochem. 41 (2006), pp. 2002-2009.
    • (2006) Process Biochem. , vol.41 , pp. 2002-2009
    • Patel, R.K.1    Dodia, M.S.2    Joshi, R.H.3    Singh, S.P.4
  • 42
    • 70349861723 scopus 로고    scopus 로고
    • Asian fish sauce as a source of nutrition
    • J. Shi, Chi-T. Ho, and F. Shahidi, eds., Marcel Dekker, Weimar, Texas, USA
    • C. Thongthai and A. Gildberg, Asian fish sauce as a source of nutrition, in Asian Functional Foods, J. Shi, Chi-T. Ho, and F. Shahidi, eds., Marcel Dekker, Weimar, Texas, USA 2005, pp. 215-265.
    • (2005) Asian Functional Foods , pp. 215-265
    • Thongthai, C.1    Gildberg, A.2
  • 43
    • 68849108440 scopus 로고    scopus 로고
    • Enzymes from solvent tolerant microbes: Useful biocatalysts for non-aqueous enzymology
    • A. Gupta and S.K. Khare, Enzymes from solvent tolerant microbes: Useful biocatalysts for non-aqueous enzymology, Crit. Rev. Biotechnol. 29 (2009), pp. 44-54.
    • (2009) Crit. Rev. Biotechnol. , vol.29 , pp. 44-54
    • Gupta, A.1    Khare, S.K.2
  • 44
    • 84874499889 scopus 로고    scopus 로고
    • Biologically active peptides and enzymatic approaches to their production
    • I. Gill, R. López Fandiño, X. Jorba, and E.N. Vulfson Biologically active peptides and enzymatic approaches to their production, Enzyme Microb. Technol. 18 (1996), pp. 162-183.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 162-183
    • Gill, I.1    López Fandiño, R.2    Jorba, X.3    Vulfson, E.N.4
  • 45
    • 0022009339 scopus 로고
    • Basic principles of protease catalyzed peptide bond formation
    • H.D. Jakubke, P. Kuhl, and A. Könnecke, Basic principles of protease catalyzed peptide bond formation, Angew. Chem. Int. Ed. Engl. 24 (1985), pp. 85-93.
    • (1985) Angew. Chem. Int. Ed. Engl. , vol.24 , pp. 85-93
    • Jakubke, H.D.1    Kuhl, P.2    Könnecke, A.3
  • 46
    • 0028414129 scopus 로고
    • Catalytic properties and potential of an extracellular protease from an extreme halophile
    • K. Ryu, J. Kim, and J.S. Dordick, Catalytic properties and potential of an extracellular protease from an extreme halophile, Enzym. Microb. Technol. 16 (1994), pp. 266-275.
    • (1994) Enzym. Microb. Technol. , vol.16 , pp. 266-275
    • Ryu, K.1    Kim, J.2    Dordick, J.S.3
  • 47
    • 15244356629 scopus 로고    scopus 로고
    • Purification and characterization of a solvent stable protease from Pseudomonas aeruginosa PseA
    • A. Gupta, I. Roy, S.K. Khare, and M.N. Gupta, Purification and characterization of a solvent stable protease from Pseudomonas aeruginosa PseA, J. Chromatogr. A 1069 (2005), pp. 155-161.
    • (2005) J. Chromatogr. A , vol.1069 , pp. 155-161
    • Gupta, A.1    Roy, I.2    Khare, S.K.3    Gupta, M.N.4


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