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Volumn 1784, Issue 9, 2008, Pages 1326-1334

Biochemical and structural characterisation of cutinase mutants in the presence of the anionic surfactant AOT

Author keywords

AOT; Cutinase; Kinetics; Protein folding; Stability

Indexed keywords

ANIONIC SURFACTANT; CUTINASE; DOCUSATE SODIUM; TRYPTOPHAN; TYROSINE; 1,4 BIS(2 ETHYLHEXYL) SODIUM SULFOSUCCINATE; 1,4-BIS(2-ETHYLHEXYL) SODIUM SULFOSUCCINATE; 1-ANILINO-8-NAPHTHALENESULFONATE; 4-NITROPHENYL BUTYRATE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; BUTYRIC ACID 4 NITROPHENYL ESTER; BUTYRIC ACID DERIVATIVE; CARBOXYLESTERASE; FUNGAL PROTEIN; RECOMBINANT PROTEIN; SUCCINIC ACID DERIVATIVE; SURFACTANT;

EID: 53149145988     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.017     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 85030581784 scopus 로고    scopus 로고
    • P.E. Kolattukudy, Cutinases from fungi and pollen, in: B. Borgstrom, H. Brockman (Eds.), Lipases, Amsterdam, Elsevier, 1984, pp. 471-504.
    • P.E. Kolattukudy, Cutinases from fungi and pollen, in: B. Borgstrom, H. Brockman (Eds.), Lipases, Amsterdam, Elsevier, 1984, pp. 471-504.
  • 2
    • 0001567583 scopus 로고
    • Cloning, expression and characterisation of cutinase, a fungal lipolytic enzyme
    • L. Alberghina, R.D. Schmid, R. Verger Eds, Lipases, Structure, Mechanism and Genetic Engineering, VCH, Weinheim
    • M. Lauwereys, P. de Geus, J. de Meutter, P. Stanssen, G. Matthyssens, Cloning, expression and characterisation of cutinase, a fungal lipolytic enzyme, in: L. Alberghina, R.D. Schmid, R. Verger (Eds.), Lipases, Structure, Mechanism and Genetic Engineering, GBF Monograph, 16, VCH, Weinheim, 1991, pp. 243-251.
    • (1991) GBF Monograph , vol.16 , pp. 243-251
    • Lauwereys, M.1    de Geus, P.2    de Meutter, J.3    Stanssen, P.4    Matthyssens, G.5
  • 3
    • 0032143952 scopus 로고    scopus 로고
    • Mechanism of removal of immobilized triacylglycerol by lipolytic enzymes in a sequential laundry wash process
    • J.A.C. Flipsen, A.C.M. Appel, H.T.W.M. van der Hijden, C.T. Verrips, Mechanism of removal of immobilized triacylglycerol by lipolytic enzymes in a sequential laundry wash process, Enzyme Microb. Technol. 23 (1998) 274-280.
    • (1998) Enzyme Microb. Technol , vol.23 , pp. 274-280
    • Flipsen, J.A.C.1    Appel, A.C.M.2    van der Hijden, H.T.W.M.3    Verrips, C.T.4
  • 5
    • 0032524506 scopus 로고    scopus 로고
    • Effects of amphipaths on the activity and stability of Fusarium solani pisi cutinase
    • D.J. Pocalyko, M. Tallman, Effects of amphipaths on the activity and stability of Fusarium solani pisi cutinase, Enzyme Microb. Technol. 22 (1998) 647-651.
    • (1998) Enzyme Microb. Technol , vol.22 , pp. 647-651
    • Pocalyko, D.J.1    Tallman, M.2
  • 6
    • 0001844392 scopus 로고    scopus 로고
    • Strategies and design of mutations in lipases
    • F.X. Malcata Ed, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • M.R. Egmond, J. de Vlieg, H.M. Verheij, G.H. de Haas, Strategies and design of mutations in lipases, in: F.X. Malcata (Ed.), Engineering of/with Lipases, Kluwer Academic Publishers, Dordrecht, The Netherlands, 1996, pp. 193-202.
    • (1996) Engineering of/with Lipases , pp. 193-202
    • Egmond, M.R.1    de Vlieg, J.2    Verheij, H.M.3    de Haas, G.H.4
  • 7
    • 44649102734 scopus 로고    scopus 로고
    • Improving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis
    • V. Brissos, T. Eggert, J.M.S. Cabral, K.E. Jaeger, Improving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis, Protein Eng. Des. Sel. 21 (2008) 387-393.
    • (2008) Protein Eng. Des. Sel , vol.21 , pp. 387-393
    • Brissos, V.1    Eggert, T.2    Cabral, J.M.S.3    Jaeger, K.E.4
  • 9
  • 10
    • 0002964990 scopus 로고    scopus 로고
    • Protein molecular weight determination by sodium dodecyl sulfate polyacrylamide gel electrophoresis
    • T.E. Creighton Ed, Oxford University Press, Oxford
    • G.S. Makowski, M.L. Ramsby, Protein molecular weight determination by sodium dodecyl sulfate polyacrylamide gel electrophoresis, in: T.E. Creighton (Ed.), Protein Structure - a Practical Approach, Oxford University Press, Oxford, 1997, pp. 1-27.
    • (1997) Protein Structure - a Practical Approach , pp. 1-27
    • Makowski, G.S.1    Ramsby, M.L.2
  • 11
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • J.P. Henley, A. Sadana, Categorization of enzyme deactivations using a series-type mechanism, Enzyme Microb. Technol. 7 (1985) 50-60.
    • (1985) Enzyme Microb. Technol , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 13
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase - increasing the stability of proteins against the rate of denaturation
    • J. Clarke, A.R. Fersht, Engineered disulfide bonds as probes of the folding pathway of barnase - increasing the stability of proteins against the rate of denaturation, Biochemistry 32 (1993) 4322-4329.
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 15
    • 0030038712 scopus 로고    scopus 로고
    • Denaturation of a recombinant cutinase from Fusarium solani in AOT-iso-octane reverse micelles: A steady-state fluorescence study
    • E.P. Melo, S.M.B. Costa, J.M.S. Cabral, Denaturation of a recombinant cutinase from Fusarium solani in AOT-iso-octane reverse micelles: a steady-state fluorescence study, Photochem. Photobiol. 63 (1996) 169-175.
    • (1996) Photochem. Photobiol , vol.63 , pp. 169-175
    • Melo, E.P.1    Costa, S.M.B.2    Cabral, J.M.S.3
  • 16
    • 0032817737 scopus 로고    scopus 로고
    • Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase
    • J.J. Prompers, C.W. Hilbers, H.A.M. Pepermans, Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase, Febs Lett. 456 (1999) 409-416.
    • (1999) Febs Lett , vol.456 , pp. 409-416
    • Prompers, J.J.1    Hilbers, C.W.2    Pepermans, H.A.M.3
  • 17
    • 0242365531 scopus 로고    scopus 로고
    • Fluorescence of the single tryptophan of cutinase: Temperature and pH effect on protein conformation and dynamics
    • J.M.G. Martinho, A.M. Santos, A. Fedorov, R.P. Baptista, M.A. Taipa, J.M.S. Cabral, Fluorescence of the single tryptophan of cutinase: temperature and pH effect on protein conformation and dynamics, Photochem. Photobiol. 78 (2003) 15-22.
    • (2003) Photochem. Photobiol , vol.78 , pp. 15-22
    • Martinho, J.M.G.1    Santos, A.M.2    Fedorov, A.3    Baptista, R.P.4    Taipa, M.A.5    Cabral, J.M.S.6
  • 18
    • 0030026581 scopus 로고    scopus 로고
    • Photophysics of the single tryptophan residue in Fusarium solani cutinase: Evidence for the occurrence of conformational substrates with unusual fluorescence behaviour
    • P.C.M. Weisenborn, H. Meder, M.R. Egmond, T.J.W.G. Visser, A. vanHoek, Photophysics of the single tryptophan residue in Fusarium solani cutinase: Evidence for the occurrence of conformational substrates with unusual fluorescence behaviour, Biophys. Chem. 58 (1996) 281-288.
    • (1996) Biophys. Chem , vol.58 , pp. 281-288
    • Weisenborn, P.C.M.1    Meder, H.2    Egmond, M.R.3    Visser, T.J.W.G.4    vanHoek, A.5
  • 20
    • 0025301439 scopus 로고
    • Protein secondary structure and circular-dichroism - a practical guide
    • W.C. Johnson, Protein secondary structure and circular-dichroism - a practical guide, Proteins, Structure Function and Genetics 7 (1990) 205-214.
    • (1990) Proteins, Structure Function and Genetics , vol.7 , pp. 205-214
    • Johnson, W.C.1
  • 21
    • 0031004544 scopus 로고    scopus 로고
    • S.M. Kelly, N.C. Price, The application of circular dichroism to studies of protein folding and unfolding, Biochim. Biophys. Acta, Prot. Struct. Mol. Enzymol. 1338 (1997) 161-185.
    • S.M. Kelly, N.C. Price, The application of circular dichroism to studies of protein folding and unfolding, Biochim. Biophys. Acta, Prot. Struct. Mol. Enzymol. 1338 (1997) 161-185.
  • 22
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • S.M. Kelly, N.C. Price, The use of circular dichroism in the investigation of protein structure and function, Curr. Protein Pept. Sci. 1 (2000) 349-384.
    • (2000) Curr. Protein Pept. Sci , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 23
    • 14744295719 scopus 로고    scopus 로고
    • T. Ternstrom, A. Svendsen, M. Akke, P. Adlercreutz, Unfolding and inactivation of cutinases by AOT and guanidine hydrochloride, Biochim. Biophys. Acta, Prot. Proteomic. 1748 (2005) 74-83.
    • T. Ternstrom, A. Svendsen, M. Akke, P. Adlercreutz, Unfolding and inactivation of cutinases by AOT and guanidine hydrochloride, Biochim. Biophys. Acta, Prot. Proteomic. 1748 (2005) 74-83.
  • 25
    • 0032525842 scopus 로고    scopus 로고
    • Characterization of a partially unfolded structure of cytochrome c induced by sodium dodecyl sulphate and the kinetics of its refolding
    • T.K. Das, S. Mazumdar, S. Mitra, Characterization of a partially unfolded structure of cytochrome c induced by sodium dodecyl sulphate and the kinetics of its refolding, Eur. J. Biochem. 254 (1998) 662-670.
    • (1998) Eur. J. Biochem , vol.254 , pp. 662-670
    • Das, T.K.1    Mazumdar, S.2    Mitra, S.3
  • 26
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • H. Roder, W. Colon, Kinetic role of early intermediates in protein folding, Curr. Opin. Struct. Biol. 7 (1997) 15-28.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 27
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1′-bis (4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • L. Shi, D.R. Palleros, A.L. Fink, Protein conformational changes induced by 1,1′-bis (4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK, Biochemistry 33 (1994) 7536-7546.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 28
    • 0030579811 scopus 로고    scopus 로고
    • Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state
    • V.N. Uversky, S. Winter, G. Lober, Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state, Biophys. Chem. 60 (1996) 79-88.
    • (1996) Biophys. Chem , vol.60 , pp. 79-88
    • Uversky, V.N.1    Winter, S.2    Lober, G.3
  • 29
    • 0032517304 scopus 로고    scopus 로고
    • V.N. Uversky, S. Winter, G. Lober, Self-association of 8-anilino-1-naphthalene-sulfonate molecules: spectroscopic characterization and application to the investigation of protein folding, Biochim. Biophys. Acta, Prot. Struct. Mol. Enzymol. 1388 (1998) 133-142.
    • V.N. Uversky, S. Winter, G. Lober, Self-association of 8-anilino-1-naphthalene-sulfonate molecules: spectroscopic characterization and application to the investigation of protein folding, Biochim. Biophys. Acta, Prot. Struct. Mol. Enzymol. 1388 (1998) 133-142.
  • 31
    • 0020488851 scopus 로고
    • Mechanism of action of cutinase - chemical modification of the catalytic triad characteristic for serine hydrolases
    • W. Koller, P.E. Kolattukudy, Mechanism of action of cutinase - chemical modification of the catalytic triad characteristic for serine hydrolases, Biochemistry 21 (1982) 3083-3090.
    • (1982) Biochemistry , vol.21 , pp. 3083-3090
    • Koller, W.1    Kolattukudy, P.E.2
  • 32
    • 0023647260 scopus 로고
    • The Activation of Aspergillus niger catalase by sodium N-dodecyl-sulfate
    • M.N. Jones, A. Finn, A. Mosavimovahedi, B.J. Waller, The Activation of Aspergillus niger catalase by sodium N-dodecyl-sulfate, Biochim. Biophys. Acta 913 (1987) 395-398.
    • (1987) Biochim. Biophys. Acta , vol.913 , pp. 395-398
    • Jones, M.N.1    Finn, A.2    Mosavimovahedi, A.3    Waller, B.J.4
  • 33
    • 0027165097 scopus 로고
    • Structural and functional studies on the interaction of sodium dodecyl-sulfate with beta-galactosidase
    • A. Muga, J.L.R. Arrondo, T. Bellon, J. Sancho, C. Bernabeu, Structural and functional studies on the interaction of sodium dodecyl-sulfate with beta-galactosidase, Arch. Biochem. Biophys. 300 (1993) 451-457.
    • (1993) Arch. Biochem. Biophys , vol.300 , pp. 451-457
    • Muga, A.1    Arrondo, J.L.R.2    Bellon, T.3    Sancho, J.4    Bernabeu, C.5
  • 34
    • 0030979596 scopus 로고    scopus 로고
    • DSC studies on bovine serum albumin denaturation - effects of ionic strength and SDS concentration
    • C. Giancola, C. DeSena, D. Fessas, G. Graziano, G. Barone, DSC studies on bovine serum albumin denaturation - effects of ionic strength and SDS concentration, Int. J. Biol. Macromol. 20 (1997) 193-204.
    • (1997) Int. J. Biol. Macromol , vol.20 , pp. 193-204
    • Giancola, C.1    DeSena, C.2    Fessas, D.3    Graziano, G.4    Barone, G.5
  • 35
    • 0031031282 scopus 로고    scopus 로고
    • Perturbation of conformational dynamics, enzymatic activity, and thermostability of beta-glycosidase from archaeon Sulfolobus solfataricus by pH and sodium dodecyl sulfate detergent
    • S. DAuria, M. Rossi, R. Nucci, G. Irace, E. Bismuto, Perturbation of conformational dynamics, enzymatic activity, and thermostability of beta-glycosidase from archaeon Sulfolobus solfataricus by pH and sodium dodecyl sulfate detergent, Proteins, Structure Function and Genetics 27 (1997) 71-79.
    • (1997) Proteins, Structure Function and Genetics , vol.27 , pp. 71-79
    • DAuria, S.1    Rossi, M.2    Nucci, R.3    Irace, G.4    Bismuto, E.5
  • 36
    • 0016157537 scopus 로고
    • Interaction of a cationic detergent with bovine serum-albumin and other proteins
    • Y. Nozaki, J.A. Reynolds, C. Tanford, Interaction of a cationic detergent with bovine serum-albumin and other proteins, J. Biol. Chem. 249 (1974) 4452-4459.
    • (1974) J. Biol. Chem , vol.249 , pp. 4452-4459
    • Nozaki, Y.1    Reynolds, J.A.2    Tanford, C.3
  • 37
    • 0030971723 scopus 로고    scopus 로고
    • Effects of temperature and SDS on the structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus
    • S. DAuria, R. Barone, M. Rossi, R. Nucci, G. Barone, D. Fessas, E. Bertoli, F. Tanfani, Effects of temperature and SDS on the structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus, Biochem. J. 323 (1997) 833-840.
    • (1997) Biochem. J , vol.323 , pp. 833-840
    • DAuria, S.1    Barone, R.2    Rossi, M.3    Nucci, R.4    Barone, G.5    Fessas, D.6    Bertoli, E.7    Tanfani, F.8
  • 39
    • 0023626273 scopus 로고
    • Protein folding - hypotheses and experiments
    • O.B. Ptitsyn, Protein folding - hypotheses and experiments, J. Protein Chem. 6 (1987) 273-293.
    • (1987) J. Protein Chem , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 40
    • 0021114569 scopus 로고
    • Molten-globule state - a compact form of globular-proteins with mobile side-chains
    • M. Ohgushi, A. Wada, Molten-globule state - a compact form of globular-proteins with mobile side-chains, Febs Lett. 164 (1983) 21-24.
    • (1983) Febs Lett , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 42
    • 0031574909 scopus 로고    scopus 로고
    • Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: Stereochemical analysis
    • S. Longhi, M. Czjzek, V. Lamzin, A. Nicolas, C. Cambillau, Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis, J. Mol. Biol. 268 (1997) 779-799.
    • (1997) J. Mol. Biol , vol.268 , pp. 779-799
    • Longhi, S.1    Czjzek, M.2    Lamzin, V.3    Nicolas, A.4    Cambillau, C.5


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