메뉴 건너뛰기




Volumn 45, Issue 5, 2010, Pages 757-764

Purification and characterization of a solvent stable aminopeptidase from Pseudomonas aeruginosa: Cloning and analysis of aminopeptidase gene conferring solvent stability

Author keywords

Aminopeptidase; Ion exchange chromatography; Metallopeptidase; Pseudomonas aeruginosa; Solvent tolerant

Indexed keywords

AMINO PEPTIDASE; ION-EXCHANGE CHROMATOGRAPHY; METALLOPEPTIDASES; PSEUDOMONAS AERUGINOSA; SOLVENT TOLERANT;

EID: 77950300151     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.01.017     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 33947585099 scopus 로고    scopus 로고
    • The structure and main functions of aminopeptidase N
    • Luan Y., and Xu W. The structure and main functions of aminopeptidase N. Curr Med Chem 14 (2007) 639-647
    • (2007) Curr Med Chem , vol.14 , pp. 639-647
    • Luan, Y.1    Xu, W.2
  • 2
    • 31644441857 scopus 로고    scopus 로고
    • Enzymatic debittering of food protein hydrolyzate
    • FitzGerald R.J., and Cuinn G.O. Enzymatic debittering of food protein hydrolyzate. Biotechnology 24 (2006) 234-237
    • (2006) Biotechnology , vol.24 , pp. 234-237
    • FitzGerald, R.J.1    Cuinn, G.O.2
  • 3
    • 0028808177 scopus 로고
    • Organic solvent-tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme
    • Ogino H., Yasui K., Shiotani T., Ishihara T., and Ishikawa H. Organic solvent-tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme. Appl Environ Microbiol 61 (1995) 4258-4262
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4258-4262
    • Ogino, H.1    Yasui, K.2    Shiotani, T.3    Ishihara, T.4    Ishikawa, H.5
  • 4
    • 0034237457 scopus 로고    scopus 로고
    • Characterization of a solvent resistant and thermostable aminopeptidase from the hyperthermophilic bacterium, Aquifex aeolicus
    • Khan A.R., Nirasawa S., Keneke S., Shimonishi T., and Hayashi K. Characterization of a solvent resistant and thermostable aminopeptidase from the hyperthermophilic bacterium, Aquifex aeolicus. Enzyme Microb Technol 27 (2000) 83-88
    • (2000) Enzyme Microb Technol , vol.27 , pp. 83-88
    • Khan, A.R.1    Nirasawa, S.2    Keneke, S.3    Shimonishi, T.4    Hayashi, K.5
  • 7
    • 2942748507 scopus 로고    scopus 로고
    • Industrial potential of organic solvent tolerant bacteria
    • Sardessai Y.N., and Bhosle S. Industrial potential of organic solvent tolerant bacteria. Biotechnol Prog 20 (2004) 655-660
    • (2004) Biotechnol Prog , vol.20 , pp. 655-660
    • Sardessai, Y.N.1    Bhosle, S.2
  • 8
    • 0031805729 scopus 로고    scopus 로고
    • Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp. strain ST-200
    • Doukyu N., and Aono R. Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp. strain ST-200. Appl Environ Microbiol 64 (1998) 1929-1932
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1929-1932
    • Doukyu, N.1    Aono, R.2
  • 9
    • 68849108440 scopus 로고    scopus 로고
    • Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology
    • Gupta A., and Khare S.K. Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology. Crit Rev Biotechnol 29 (2009) 44-54
    • (2009) Crit Rev Biotechnol , vol.29 , pp. 44-54
    • Gupta, A.1    Khare, S.K.2
  • 10
    • 15244356629 scopus 로고    scopus 로고
    • Purification and characterization of a solvent stable protease from Pseudomonas aeruginosa PseA
    • Gupta A., Roy I., Khare S.K., and Gupta M.N. Purification and characterization of a solvent stable protease from Pseudomonas aeruginosa PseA. J Chromatogr A 1069 (2005) 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
  • 11
    • 41849131490 scopus 로고    scopus 로고
    • Lipase from solvent tolerant Pseudomonas aeruginosa strain: production optimization by response surface methodology and application
    • Gaur R., Gupta A., and Khare S.K. Lipase from solvent tolerant Pseudomonas aeruginosa strain: production optimization by response surface methodology and application. Bioresour Technol 99 (2008) 4796-4802
    • (2008) Bioresour Technol , vol.99 , pp. 4796-4802
    • Gaur, R.1    Gupta, A.2    Khare, S.K.3
  • 12
    • 0000508579 scopus 로고    scopus 로고
    • Purification and characterization of Aeromonas caviae aminopeptidase possessing debittering activity
    • Izawa N., Ishikawa S., Tanokura T., Ohta K., and Hayashi K. Purification and characterization of Aeromonas caviae aminopeptidase possessing debittering activity. J Agric Food Chem 45 (1997) 4897-4902
    • (1997) J Agric Food Chem , vol.45 , pp. 4897-4902
    • Izawa, N.1    Ishikawa, S.2    Tanokura, T.3    Ohta, K.4    Hayashi, K.5
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0026486796 scopus 로고
    • Microsequence analysis of electroblotted proteins: I. Comparison of electroblotting recoveries using different types of PVDF membranes
    • Mozdzanowski J., and Speicher D.W. Microsequence analysis of electroblotted proteins: I. Comparison of electroblotting recoveries using different types of PVDF membranes. Anal Biochem 207 (1992) 11-18
    • (1992) Anal Biochem , vol.207 , pp. 11-18
    • Mozdzanowski, J.1    Speicher, D.W.2
  • 16
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen
    • Strover C.K., Pham X.Q.T., Ervin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., et al. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406 (2000) 959-964
    • (2000) Nature , vol.406 , pp. 959-964
    • Strover, C.K.1    Pham, X.Q.T.2    Ervin, A.L.3    Mizoguchi, S.D.4    Warrener, P.5    Hickey, M.J.6
  • 19
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim H.C., and Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7 (1979) 1513-1523
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 (1993) 283-291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 21
    • 0035941190 scopus 로고    scopus 로고
    • A secreted aminopeptidase of Pseudomonas aeruginosa. Identification, primary structure and relationship to other aminopeptidases
    • Cahan R., Axelrad I., Safrin M., Ohman D.E., and Kessler E. A secreted aminopeptidase of Pseudomonas aeruginosa. Identification, primary structure and relationship to other aminopeptidases. J Biol Chem 276 (2001) 43645-43652
    • (2001) J Biol Chem , vol.276 , pp. 43645-43652
    • Cahan, R.1    Axelrad, I.2    Safrin, M.3    Ohman, D.E.4    Kessler, E.5
  • 22
    • 0029858433 scopus 로고    scopus 로고
    • Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24
    • Ogasawara W., Kobayashi G., Okada H., and Morikawa Y. Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24. J Bacteriol 178 (1996) 6288-6295
    • (1996) J Bacteriol , vol.178 , pp. 6288-6295
    • Ogasawara, W.1    Kobayashi, G.2    Okada, H.3    Morikawa, Y.4
  • 23
    • 0043264772 scopus 로고    scopus 로고
    • Production, purification and characterization of intracellular alanylaminopeptidase of Pseudomonas sp.
    • Jankiewicz U., and Bielawski W. Production, purification and characterization of intracellular alanylaminopeptidase of Pseudomonas sp. Folia Microbiol 46 (2001) 515-518
    • (2001) Folia Microbiol , vol.46 , pp. 515-518
    • Jankiewicz, U.1    Bielawski, W.2
  • 24
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: properties and functions
    • Gonzales T., and Robert-Baudouy J. Bacterial aminopeptidases: properties and functions. FEMS Microbiol Rev 18 (1996) 319-344
    • (1996) FEMS Microbiol Rev , vol.18 , pp. 319-344
    • Gonzales, T.1    Robert-Baudouy, J.2
  • 26
    • 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., Doukyu N., Yasuda M., Ishimi K., and Ogino H. Peptide synthesis of aspartame precursor using organic-solvent-stable PST-01 protease in monophasic aqueous-organic solvent systems. Biotechnol Prog 23 (2007) 820-823
    • (2007) Biotechnol Prog , vol.23 , pp. 820-823
    • Tsuchiyama, S.1    Doukyu, N.2    Yasuda, M.3    Ishimi, K.4    Ogino, H.5
  • 27
    • 0034941427 scopus 로고    scopus 로고
    • Enhancement of enzyme activity through three-phase partitioning: crystal structure of a modified serine proteinase at 1.5 Å resolution
    • Singh R.K., Gourinath S., Sharma S., Roy I., Gupta M.N., Betzel Ch., et al. Enhancement of enzyme activity through three-phase partitioning: crystal structure of a modified serine proteinase at 1.5 Å resolution. Protein Eng 14 (2001) 307-313
    • (2001) Protein Eng , vol.14 , pp. 307-313
    • Singh, R.K.1    Gourinath, S.2    Sharma, S.3    Roy, I.4    Gupta, M.N.5    Betzel, Ch.6
  • 28
    • 33745163242 scopus 로고    scopus 로고
    • Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides
    • Arima J., Uesugi Y., Uraji M., Iwabuchi M., and Hatanaka T. Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides. Appl Environ Microbiol 72 (2006) 4225-4231
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4225-4231
    • Arima, J.1    Uesugi, Y.2    Uraji, M.3    Iwabuchi, M.4    Hatanaka, T.5
  • 29
    • 0025171939 scopus 로고
    • Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulpholobus sulphataricus
    • Hanner M., Redl B., and Stoffler G. Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulpholobus sulphataricus. Biochim Biophys Acta 1033 (1990) 148-153
    • (1990) Biochim Biophys Acta , vol.1033 , pp. 148-153
    • Hanner, M.1    Redl, B.2    Stoffler, G.3
  • 30
    • 0038162378 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the recombinant leucine aminopeptidase II of Bacillus stearothermophilus
    • Kuo L.Y., Hwang G.Y., Lai Y.J., Yang S.L., and Lin L.L. Overexpression, purification, and characterization of the recombinant leucine aminopeptidase II of Bacillus stearothermophilus. Curr Microbiol 47 (2003) 40-45
    • (2003) Curr Microbiol , vol.47 , pp. 40-45
    • Kuo, L.Y.1    Hwang, G.Y.2    Lai, Y.J.3    Yang, S.L.4    Lin, L.L.5
  • 31
    • 0027208935 scopus 로고
    • Aminopeptidases: towards a mechanism of action
    • Taylor A. Aminopeptidases: towards a mechanism of action. Trends Biochem Sci 18 (1993) 167-172
    • (1993) Trends Biochem Sci , vol.18 , pp. 167-172
    • Taylor, A.1
  • 33
    • 77950299542 scopus 로고    scopus 로고
    • Dodson RJ, Harkins D, Paulsen IT. Direct submission to NCBI, accession no. YP_001351283.
    • Dodson RJ, Harkins D, Paulsen IT. Direct submission to NCBI, accession no. YP_001351283.
  • 35
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157 (1982) 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 37
    • 51949097797 scopus 로고    scopus 로고
    • Solvent-stable Pseudomonas aeruginosa PseA protease gene: identification, molecular characterization, phylogenetic and bioinformatic analysis to study reasons for solvent stability
    • Gupta A., Ray S., Kapoor S., and Khare S.K. Solvent-stable Pseudomonas aeruginosa PseA protease gene: identification, molecular characterization, phylogenetic and bioinformatic analysis to study reasons for solvent stability. J Mol Biol Biotechnol 15 (2008) 234-243
    • (2008) J Mol Biol Biotechnol , vol.15 , pp. 234-243
    • Gupta, A.1    Ray, S.2    Kapoor, S.3    Khare, S.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.