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Volumn 192, Issue Part A, 2014, Pages 248-254

Improvement of the stability and activity of the BPO-A1 haloperoxidase from Streptomyces aureofaciens by directed evolution

Author keywords

Directed evolution; Haloperoxidase; Organic solvent stability; Thermostability

Indexed keywords

AMINO ACIDS; BACTERIA; DIMETHYL SULFOXIDE; DIMETHYLFORMAMIDE; STABILIZATION;

EID: 84918580230     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.10.030     Document Type: Article
Times cited : (25)

References (30)
  • 1
    • 0033106205 scopus 로고    scopus 로고
    • Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis
    • Akanuma S., Yamagishi A., Tanaka N., Oshima T. Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis. Eur. J. Biochem. 1999, 260:499-504.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 499-504
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 2
    • 0034623981 scopus 로고    scopus 로고
    • Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic archaea, Thermoplasma acidophilum and Pyrococcus furiosus
    • Arnott M.A., Michael R.A., Thompson C.R., Hough D.W., Danson M.J. Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic archaea, Thermoplasma acidophilum and Pyrococcus furiosus. J. Mol. Biol. 2000, 304:657-668.
    • (2000) J. Mol. Biol. , vol.304 , pp. 657-668
    • Arnott, M.A.1    Michael, R.A.2    Thompson, C.R.3    Hough, D.W.4    Danson, M.J.5
  • 3
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0242559061 scopus 로고    scopus 로고
    • Oxidizing enzymes as biocatalysts
    • Burton S.G. Oxidizing enzymes as biocatalysts. Trends Biotechnol. 2003, 21:543-549.
    • (2003) Trends Biotechnol. , vol.21 , pp. 543-549
    • Burton, S.G.1
  • 5
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau C., Claverie J.M. Structural and genomic correlates of hyperthermostability. J. Biol. Chem. 2000, 275:32383-32386.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 6
    • 75349100918 scopus 로고    scopus 로고
    • Organic solvent-tolerant enzymes
    • Doukyu N., Ogino H. Organic solvent-tolerant enzymes. Biochem. Eng. J. 2010, 48:270-282.
    • (2010) Biochem. Eng. J. , vol.48 , pp. 270-282
    • Doukyu, N.1    Ogino, H.2
  • 7
    • 0031686238 scopus 로고    scopus 로고
    • Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study
    • Facchiano A.M., Colonna G., Ragone R. Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Protein Eng. 1998, 11:753-760.
    • (1998) Protein Eng. , vol.11 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 8
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb. Technol. 2009, 45:405-418.
    • (2009) Enzyme Microb. Technol. , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 9
    • 3343015685 scopus 로고    scopus 로고
    • Structural stability and unfolding properties of thermostable bacterial α-amylases: a comparative study of homologous enzymes
    • Fitter J., Haber-Pohlmeier S. Structural stability and unfolding properties of thermostable bacterial α-amylases: a comparative study of homologous enzymes. Biochemistry 2004, 43:9589-9599.
    • (2004) Biochemistry , vol.43 , pp. 9589-9599
    • Fitter, J.1    Haber-Pohlmeier, S.2
  • 10
    • 20044367134 scopus 로고    scopus 로고
    • Enhancing effect of calcium and vanadium ions on thermal stability of bromoperoxidase from Corallina pilulifera
    • Garcia-Rodriguez E., Ohshiro T., Aibara T., Izumi Y., Littlechild J. Enhancing effect of calcium and vanadium ions on thermal stability of bromoperoxidase from Corallina pilulifera. J. Biol. Inorg. Chem. 2005, 10:275-282.
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 275-282
    • Garcia-Rodriguez, E.1    Ohshiro, T.2    Aibara, T.3    Izumi, Y.4    Littlechild, J.5
  • 11
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: a review
    • Haki G.D., Rakshit S.K. Developments in industrially important thermostable enzymes: a review. Bioresour. Technol. 2003, 89:17-34.
    • (2003) Bioresour. Technol. , vol.89 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 14
    • 73249115175 scopus 로고    scopus 로고
    • Enhancement of the organic solvent-stability of the LST-03 lipase by directed evolution
    • Kawata T., Ogino H. Enhancement of the organic solvent-stability of the LST-03 lipase by directed evolution. Biotechnol. Progr. 2009, 25:1605-1611.
    • (2009) Biotechnol. Progr. , vol.25 , pp. 1605-1611
    • Kawata, T.1    Ogino, H.2
  • 15
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino H., Aoki M., Aoshima M., Hayashi Y., Ohba M., Yamagishi A., Wakagi T., Oshima T. Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur. J. Biochem. 1994, 220:275-281.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature (London) 1970, 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0035424955 scopus 로고    scopus 로고
    • Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution
    • Lehmann M., Wyss M. Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution. Curr. Opin. Biotechnol. 2001, 12:371-375.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 371-375
    • Lehmann, M.1    Wyss, M.2
  • 18
    • 27544475025 scopus 로고    scopus 로고
    • Enhanced thermal stability achieved without increased conformational rigidity at physiological temperatures: spatial propagation of differential flexibility in rubredoxin hybrids
    • LeMaster D.M., Tang J., Paredes D.I., Hernández G. Enhanced thermal stability achieved without increased conformational rigidity at physiological temperatures: spatial propagation of differential flexibility in rubredoxin hybrids. Proteins 2005, 61:608-616.
    • (2005) Proteins , vol.61 , pp. 608-616
    • LeMaster, D.M.1    Tang, J.2    Paredes, D.I.3    Hernández, G.4
  • 19
    • 0033023976 scopus 로고    scopus 로고
    • Haloperoxidases and their role in biotransformation reactions
    • Littlechild J. Haloperoxidases and their role in biotransformation reactions. Curr. Opin. Chem. Biol. 1999, 3:28-34.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 28-34
    • Littlechild, J.1
  • 20
    • 0032709104 scopus 로고    scopus 로고
    • The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures
    • Maes D., Zeelen J.P., Thanki N., Beaucamp N., Alvarez M., Thi M.H.D., Backmann J., Martial J.A., Wyns L., Jaenicke R., Wierenga R.K. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins 1999, 37:441-453.
    • (1999) Proteins , vol.37 , pp. 441-453
    • Maes, D.1    Zeelen, J.P.2    Thanki, N.3    Beaucamp, N.4    Alvarez, M.5    Thi, M.H.D.6    Backmann, J.7    Martial, J.A.8    Wyns, L.9    Jaenicke, R.10    Wierenga, R.K.11
  • 22
    • 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., Uchiho T., Doukyu N., Yasuda M., Ishimi K., Ishikawa H. 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. 2007, 358:1028-1033.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 1028-1033
    • Ogino, H.1    Uchiho, T.2    Doukyu, N.3    Yasuda, M.4    Ishimi, K.5    Ishikawa, H.6
  • 23
    • 0035140742 scopus 로고    scopus 로고
    • Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in its organic solvent stability
    • Ogino H., Uchiho T., Yokoo J., Kobayashi R., Ichise R., Ishikawa H. Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in its organic solvent stability. Appl. Environ. Microbiol. 2001, 67:942-947.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 942-947
    • Ogino, H.1    Uchiho, T.2    Yokoo, J.3    Kobayashi, R.4    Ichise, R.5    Ishikawa, H.6
  • 24
    • 0028289015 scopus 로고
    • Cloning of a second non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification
    • Pelletier I., Pfeifer O., Altenbuchner J., van Pée K.-H. Cloning of a second non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification. Microbiology 1994, 140:509-516.
    • (1994) Microbiology , vol.140 , pp. 509-516
    • Pelletier, I.1    Pfeifer, O.2    Altenbuchner, J.3    van Pée, K.-H.4
  • 25
    • 0030781507 scopus 로고    scopus 로고
    • Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices
    • Petukhov M., Kil Y., Kuramitsu S., Lanzov V. Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices. Proteins 1997, 29:309-320.
    • (1997) Proteins , vol.29 , pp. 309-320
    • Petukhov, M.1    Kil, Y.2    Kuramitsu, S.3    Lanzov, V.4
  • 26
    • 0026694319 scopus 로고
    • Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762
    • Pfeifer O., Pelletier I., Altenbuchner J., van Pée K.-H. Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762. J. Gen. Microbiol. 1992, 138:1123-1131.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1123-1131
    • Pfeifer, O.1    Pelletier, I.2    Altenbuchner, J.3    van Pée, K.-H.4
  • 27
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C., Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 2001, 65:1-43.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 28
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • Villeret V., Clantin B., Tricot C., Legrain C., Roovers M., Stalon V., Glansdorff N., van Beeumen J. The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:2801-2806.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5    Stalon, V.6    Glansdorff, N.7    van Beeumen, J.8
  • 29
    • 0026008650 scopus 로고
    • Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762
    • Weng M., Pfeifer O., Krauss S., Lingens F., van Pee K.H. Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762. J. Gen. Microbiol. 1991, 137:2539-2546.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2539-2546
    • Weng, M.1    Pfeifer, O.2    Krauss, S.3    Lingens, F.4    van Pee, K.H.5
  • 30
    • 0141817121 scopus 로고    scopus 로고
    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • Zhang N., Suen W.C., Windsor W., Xiao L., Madison V., Zaks A. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng. 2003, 16:599-605.
    • (2003) Protein Eng. , vol.16 , pp. 599-605
    • Zhang, N.1    Suen, W.C.2    Windsor, W.3    Xiao, L.4    Madison, V.5    Zaks, A.6


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