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Volumn 49, Issue 4, 2011, Pages 388-394

Reactivation of a thermostable lipase by solid phase unfolding/refolding. Effect of cysteine residues on refolding efficiency

Author keywords

Additives; Cysteine oxidation; Enzyme reactivation; Immobilization; Lipase; Refolding

Indexed keywords

ACTIVITY RECOVERY; AGAROSE; AMINO GROUP; AQUEOUS MEDIA; BUFFER COMPOSITION; COVALENT ATTACHMENT; CYANOGEN BROMIDE; CYS RESIDUES; CYSTEINE OXIDATION; CYSTEINE RESIDUES; DIFFERENT EFFECTS; DITHIOTHREITOL; ENZYME REACTIVATION; EXPERIMENTAL CONDITIONS; GLYOXYL; GLYOXYL AGAROSE; HIGH CONCENTRATION; INITIAL ACTIVITY; MATRIX; MULTIPOINT; PROTEIN REFOLDING; REFOLDING; REFOLDING EFFICIENCY; SOLID DERIVATIVES; SOLID-PHASE;

EID: 80051794269     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.06.018     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 57849132335 scopus 로고    scopus 로고
    • Biocatalysis for the production of industrial products and functional foods from rice and other agricultural produce
    • Akoh C.C., Chang S.W., Lee G.C., Shaw J.F. Biocatalysis for the production of industrial products and functional foods from rice and other agricultural produce. J Agric Food Chem 2008, 56:10445-10451.
    • (2008) J Agric Food Chem , vol.56 , pp. 10445-10451
    • Akoh, C.C.1    Chang, S.W.2    Lee, G.C.3    Shaw, J.F.4
  • 2
    • 54449084497 scopus 로고    scopus 로고
    • Applications of biocatalysis in fragrance chemistry: the enantiomers of alpha-, beta-, and gamma-irones
    • Brenna E., Fuganti C., Serra S. Applications of biocatalysis in fragrance chemistry: the enantiomers of alpha-, beta-, and gamma-irones. Chem Soc Rev 2008, 37:2443-2451.
    • (2008) Chem Soc Rev , vol.37 , pp. 2443-2451
    • Brenna, E.1    Fuganti, C.2    Serra, S.3
  • 3
    • 43649098961 scopus 로고    scopus 로고
    • New opportunities for biocatalysis: making pharmaceutical processes greener
    • Woodley J.M. New opportunities for biocatalysis: making pharmaceutical processes greener. Trends Biotechnol 2008, 26:321-327.
    • (2008) Trends Biotechnol , vol.26 , pp. 321-327
    • Woodley, J.M.1
  • 4
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization-aqueous and non-aqueous environment
    • Iyer P.V., Ananthanarayan L. Enzyme stability and stabilization-aqueous and non-aqueous environment. Process Biochem 2008, 43:1019-1032.
    • (2008) Process Biochem , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 7
    • 79955048698 scopus 로고    scopus 로고
    • Immobilization of enzymes as 21st century begins
    • Humana Presss Inc., Totowa, NJ, J.M. Guisan (Ed.)
    • Guisan J.M. Immobilization of enzymes as 21st century begins. Immobilization of enzymes and cells 2006, 1-14. Humana Presss Inc., Totowa, NJ. J.M. Guisan (Ed.).
    • (2006) Immobilization of enzymes and cells , pp. 1-14
    • Guisan, J.M.1
  • 8
    • 0030796979 scopus 로고    scopus 로고
    • Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES
    • Teshima T., Kondo A., Fukuda H. Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES. Appl Microbiol Biotechnol 1997, 48:41-46.
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 41-46
    • Teshima, T.1    Kondo, A.2    Fukuda, H.3
  • 9
    • 70449631056 scopus 로고    scopus 로고
    • Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus
    • Bolivar J.M., Rocha-Martin J., Godoy C., Rodrigues R.C., Guisan J.M. Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus. Process Biochem 2010, 45:107-113.
    • (2010) Process Biochem , vol.45 , pp. 107-113
    • Bolivar, J.M.1    Rocha-Martin, J.2    Godoy, C.3    Rodrigues, R.C.4    Guisan, J.M.5
  • 10
    • 64049111786 scopus 로고    scopus 로고
    • Positive effects of the multipoint covalent immobilization in the reactivation of partially inactivated derivatives of lipase from Thermomyces lanuginosus
    • Rodrigues R.C., Bolivar J.M., Palau-Ors A., Volpato G., Ayub M.A.Z., Fernandez-Lafuente R., et al. Positive effects of the multipoint covalent immobilization in the reactivation of partially inactivated derivatives of lipase from Thermomyces lanuginosus. Enzyme Microb Technol 2009, 44:386-393.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 386-393
    • Rodrigues, R.C.1    Bolivar, J.M.2    Palau-Ors, A.3    Volpato, G.4    Ayub, M.A.Z.5    Fernandez-Lafuente, R.6
  • 11
    • 70350223483 scopus 로고    scopus 로고
    • Improved reactivation of immobilized-stabilized lipase from Thermomyces lanuginosus by its coating with highly hydrophilic polymers
    • Rodrigues R.C., Bolivar J.M., Volpato G., Filice M., Godoy C., Fernandez-Lafuente R., et al. Improved reactivation of immobilized-stabilized lipase from Thermomyces lanuginosus by its coating with highly hydrophilic polymers. J Biotechnol 2009, 144:113-119.
    • (2009) J Biotechnol , vol.144 , pp. 113-119
    • Rodrigues, R.C.1    Bolivar, J.M.2    Volpato, G.3    Filice, M.4    Godoy, C.5    Fernandez-Lafuente, R.6
  • 13
    • 38049012808 scopus 로고    scopus 로고
    • X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation
    • Ericsson D.J., Kasrayan A., Johansson P., Bergfors T., Sandstrom A.G., Backvall J.E., et al. X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation. J Mol Biol 2008, 376:109-119.
    • (2008) J Mol Biol , vol.376 , pp. 109-119
    • Ericsson, D.J.1    Kasrayan, A.2    Johansson, P.3    Bergfors, T.4    Sandstrom, A.G.5    Backvall, J.E.6
  • 14
    • 33744784809 scopus 로고    scopus 로고
    • Candida antarctica lipase B: an ideal biocatalyst for the preparation of nitrogenated organic compounds
    • Gotor-Fernández V., Busto E., Gotor V. Candida antarctica lipase B: an ideal biocatalyst for the preparation of nitrogenated organic compounds. Adv Synth Catal 2006, 348:797-812.
    • (2006) Adv Synth Catal , vol.348 , pp. 797-812
    • Gotor-Fernández, V.1    Busto, E.2    Gotor, V.3
  • 15
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • Reetz M.T. Lipases as practical biocatalysts. Curr Opin Chem Biol 2002, 6:145-150.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 145-150
    • Reetz, M.T.1
  • 16
    • 0034642243 scopus 로고    scopus 로고
    • Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase
    • Brzozowski A.M., Savage H., Verma C.S., Turkenburg J.P., Lawson D.M., Svendsen A., et al. Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase. Biochemistry 2000, 39:15071-15082.
    • (2000) Biochemistry , vol.39 , pp. 15071-15082
    • Brzozowski, A.M.1    Savage, H.2    Verma, C.S.3    Turkenburg, J.P.4    Lawson, D.M.5    Svendsen, A.6
  • 17
    • 0031023666 scopus 로고    scopus 로고
    • Interfacial activation' of lipases: facts and artifacts
    • Verger R. Interfacial activation' of lipases: facts and artifacts. Trends Biotechnol 1997, 15:32-38.
    • (1997) Trends Biotechnol , vol.15 , pp. 32-38
    • Verger, R.1
  • 18
    • 0035064602 scopus 로고    scopus 로고
    • Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus G. th.
    • Nazina T.N., Tourova T.P., Poltaraus A.B., Novikova E.V., Grigoryan A.A., Ivanova A.E., et al. Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus G. th. Int J Syst Evol Microbiol 2001, 51:433-446.
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 433-446
    • Nazina, T.N.1    Tourova, T.P.2    Poltaraus, A.B.3    Novikova, E.V.4    Grigoryan, A.A.5    Ivanova, A.E.6
  • 19
    • 0031057173 scopus 로고    scopus 로고
    • Bacillus thermocatenulatus lipase: a thermoalkalophilic lipase with interesting properties
    • Schmidt-Dannert C., Rua M.L., Wahl S., Schmid R.D. Bacillus thermocatenulatus lipase: a thermoalkalophilic lipase with interesting properties. Biochem Soc Trans 1997, 25:178-182.
    • (1997) Biochem Soc Trans , vol.25 , pp. 178-182
    • Schmidt-Dannert, C.1    Rua, M.L.2    Wahl, S.3    Schmid, R.D.4
  • 20
    • 0028025693 scopus 로고
    • Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus
    • Schmidt-Dannert C., Sztajer H., Stocklein W., Menge U., Schmid R.D. Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochim Biophys Acta 1994, 1214:43-53.
    • (1994) Biochim Biophys Acta , vol.1214 , pp. 43-53
    • Schmidt-Dannert, C.1    Sztajer, H.2    Stocklein, W.3    Menge, U.4    Schmid, R.D.5
  • 21
    • 0035911359 scopus 로고    scopus 로고
    • Mapping the substrate selectivity of new hydrolases using colorimetric screening: lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes
    • Liu A.M.F., Somers N.A., Kazlauskas R.J., Brush T.S., Zocher F., Enzelberger M.M., et al. Mapping the substrate selectivity of new hydrolases using colorimetric screening: lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes. Tetrahedron Asymmetry 2001, 12:545-556.
    • (2001) Tetrahedron Asymmetry , vol.12 , pp. 545-556
    • Liu, A.M.F.1    Somers, N.A.2    Kazlauskas, R.J.3    Brush, T.S.4    Zocher, F.5    Enzelberger, M.M.6
  • 22
    • 41549096482 scopus 로고    scopus 로고
    • Selective esterification of phthalic acids in two ionic liquids at high temperatures using a thermostable lipase of Bacillus thermocatenulatus: a comparative study
    • Martín J.R., Nus M., Gago J.V.S., Sánchez-Montero J.M. Selective esterification of phthalic acids in two ionic liquids at high temperatures using a thermostable lipase of Bacillus thermocatenulatus: a comparative study. J Mol Catal B: Enzym 2008, 52-53:162-167.
    • (2008) J Mol Catal B: Enzym , pp. 162-167
    • Martín, J.R.1    Nus, M.2    Gago, J.V.S.3    Sánchez-Montero, J.M.4
  • 24
    • 55949114692 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the BTL2 lipase from the extremophilic microorganism Bacillus thermocatenulatus
    • Carrasco-Lopez C., Godoy C., de las Rivas B., Fernandez-Lorente G., Palomo J.M., Guisan J.M., et al. Crystallization and preliminary X-ray diffraction studies of the BTL2 lipase from the extremophilic microorganism Bacillus thermocatenulatus. Acta Crystallogr. F 2008, 64:1043-1045.
    • (2008) Acta Crystallogr. F , vol.64 , pp. 1043-1045
    • Carrasco-Lopez, C.1    Godoy, C.2    de las Rivas, B.3    Fernandez-Lorente, G.4    Palomo, J.M.5    Guisan, J.M.6
  • 27
    • 52649136072 scopus 로고    scopus 로고
    • Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose
    • Fernandez-Lorente G., Godoy C.A., Mendes A.A., Lopez-Gallego F., Grazu V., de Las Rivas B., et al. Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose. Biomacromolecules 2008, 9:2553-2561.
    • (2008) Biomacromolecules , vol.9 , pp. 2553-2561
    • Fernandez-Lorente, G.1    Godoy, C.A.2    Mendes, A.A.3    Lopez-Gallego, F.4    Grazu, V.5    de Las Rivas, B.6
  • 28
    • 0030900522 scopus 로고    scopus 로고
    • Reactivation strategies by unfolding/refolding of chymotrypsin derivatives after inactivation by organic solvents
    • Soler G., Bastida A., Blanco R.M., Fernandez-Lafuente R., Guisan J.M. Reactivation strategies by unfolding/refolding of chymotrypsin derivatives after inactivation by organic solvents. Biochim Biophys Acta 1997, 1339:167-175.
    • (1997) Biochim Biophys Acta , vol.1339 , pp. 167-175
    • Soler, G.1    Bastida, A.2    Blanco, R.M.3    Fernandez-Lafuente, R.4    Guisan, J.M.5
  • 29
    • 16844362486 scopus 로고    scopus 로고
    • Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride
    • Ganea E., Harding J.J. Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride. Biol Chem 2005, 386:269-278.
    • (2005) Biol Chem , vol.386 , pp. 269-278
    • Ganea, E.1    Harding, J.J.2
  • 30
    • 0029186489 scopus 로고
    • Urea and guanidine hydrochloride denaturation curves
    • Shirley B.A. Urea and guanidine hydrochloride denaturation curves. Methods Mol Biol 1995, 40:177-190.
    • (1995) Methods Mol Biol , vol.40 , pp. 177-190
    • Shirley, B.A.1
  • 31
    • 0032584765 scopus 로고    scopus 로고
    • Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography
    • Rogl H., Kosemund K., Kuhlbrandt W., Collinson I. Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography. FEBS Lett 1998, 432:21-26.
    • (1998) FEBS Lett , vol.432 , pp. 21-26
    • Rogl, H.1    Kosemund, K.2    Kuhlbrandt, W.3    Collinson, I.4
  • 32
    • 72049106382 scopus 로고    scopus 로고
    • The effect of substitution of Phe181 and Phe182 with Ala on activity, substrate specificity and stabilization of substrate at the active site of Bacillus thermocatenulatus lipase
    • Karkhane A.A., Yakhchali B., Jazii F.R., Bambai B. The effect of substitution of Phe181 and Phe182 with Ala on activity, substrate specificity and stabilization of substrate at the active site of Bacillus thermocatenulatus lipase. J Mol Catal B: Enzym 2009, 61:162-167.
    • (2009) J Mol Catal B: Enzym , vol.61 , pp. 162-167
    • Karkhane, A.A.1    Yakhchali, B.2    Jazii, F.R.3    Bambai, B.4
  • 33
    • 0029899631 scopus 로고    scopus 로고
    • Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. molecular cloning, nucleotide sequence, purification and some properties
    • Schmidt-Dannert C., Rua M.L., Atomi H., Schmid R.D. Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. molecular cloning, nucleotide sequence, purification and some properties. Biochim Biophys Acta 1996, 1301:105-114.
    • (1996) Biochim Biophys Acta , vol.1301 , pp. 105-114
    • Schmidt-Dannert, C.1    Rua, M.L.2    Atomi, H.3    Schmid, R.D.4
  • 35
    • 58049184362 scopus 로고    scopus 로고
    • Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study
    • Krywka C., Sternemann C., Paulus M., Tolan M., Royer C., Winter R. Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study. ChemPhysChem 2008, 9:2809-2815.
    • (2008) ChemPhysChem , vol.9 , pp. 2809-2815
    • Krywka, C.1    Sternemann, C.2    Paulus, M.3    Tolan, M.4    Royer, C.5    Winter, R.6
  • 36
    • 34547537605 scopus 로고    scopus 로고
    • Chemical chaperone-mediated protein folding: stabilization of P22 tailspike folding intermediates by glycerol
    • Mishra R., Bhat R., Seckler R. Chemical chaperone-mediated protein folding: stabilization of P22 tailspike folding intermediates by glycerol. Biol Chem 2007, 388:797-804.
    • (2007) Biol Chem , vol.388 , pp. 797-804
    • Mishra, R.1    Bhat, R.2    Seckler, R.3
  • 37
    • 0021329847 scopus 로고
    • Free radical metabolites of L-cysteine oxidation
    • Harman L.S., Mottley C., Mason R.P. Free radical metabolites of L-cysteine oxidation. J Biol Chem 1984, 259:5606-5611.
    • (1984) J Biol Chem , vol.259 , pp. 5606-5611
    • Harman, L.S.1    Mottley, C.2    Mason, R.P.3
  • 38
    • 14644429003 scopus 로고    scopus 로고
    • Denaturant-assisted formation of a stabilizing disulfide bridge from engineered cysteines in nonideal conformations
    • Karlsson M., Martensson L.G., Karlsson C., Carlsson U. Denaturant-assisted formation of a stabilizing disulfide bridge from engineered cysteines in nonideal conformations. Biochemistry 2005, 44:3487-3493.
    • (2005) Biochemistry , vol.44 , pp. 3487-3493
    • Karlsson, M.1    Martensson, L.G.2    Karlsson, C.3    Carlsson, U.4
  • 39
    • 0034819513 scopus 로고    scopus 로고
    • Oxidative folding of murine prion mPrP(23-231)
    • Lu B.Y., Beck P.J., Chang J.Y. Oxidative folding of murine prion mPrP(23-231). Eur J Biochem 2001, 268:3767-3773.
    • (2001) Eur J Biochem , vol.268 , pp. 3767-3773
    • Lu, B.Y.1    Beck, P.J.2    Chang, J.Y.3


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