메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages 1517-1521

A high-throughput assay for enzymatic polyester hydrolysis activity by fluorimetric detection

Author keywords

Biocatalysis; Enzymes; Fluorescence; High throughput; Screening

Indexed keywords

96-WELL; BIOCATALYSIS; BUFFER CONCENTRATIONS; DEGRADATION PRODUCTS; FLUORIMETRIC ASSAYS; FLUORIMETRIC DETECTION; FREE HYDROXYL RADICALS; HIGH-THROUGHPUT; HIGH-THROUGHPUT ASSAYS; HIGH-THROUGHPUT SCREENING; HPLC METHOD; HYDROLYSIS ACTIVITY; MICROPLATES; NUMBER OF SAMPLES; PET FILMS; PH VALUE; SYNTHETIC POLYMERS; TEREPHTHALATE; TEREPHTHALIC ACIDS; THERMOBIFIDA FUSCA;

EID: 84870703309     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201200119     Document Type: Article
Times cited : (60)

References (26)
  • 1
    • 33847261067 scopus 로고    scopus 로고
    • Polyester fibers: Fiber formation and end-use applications, in: Scheirs, J., Long, T. E. (Eds.), Modern Polyesters: Chemistry and Technology of Polyesters and Copolyesters, John Wiley & Sons Ltd, Chichester
    • Reese, G., Polyester fibers: Fiber formation and end-use applications, in: Scheirs, J., Long, T. E. (Eds.), Modern Polyesters: Chemistry and Technology of Polyesters and Copolyesters, John Wiley & Sons Ltd, Chichester 2003, pp. 401-434.
    • (2003) , pp. 401-434
    • Reese, G.1
  • 2
    • 0031117869 scopus 로고    scopus 로고
    • Chemical recycling of poly(ethylene terephthalate).
    • Paszun, D., Spychaj, T., Chemical recycling of poly(ethylene terephthalate). Ind. Eng. Chem. Res. 1997, 36, 1373-1383.
    • (1997) Ind. Eng. Chem. Res. , vol.36 , pp. 1373-1383
    • Paszun, D.1    Spychaj, T.2
  • 3
    • 33748543528 scopus 로고    scopus 로고
    • Biological degradation of synthetic polyesters-Enzymes as potential catalysts for polyester recycling.
    • Mueller, R.-J., Biological degradation of synthetic polyesters-Enzymes as potential catalysts for polyester recycling. Process. Biochem. 2006, 41, 2124-2128.
    • (2006) Process. Biochem. , vol.41 , pp. 2124-2128
    • Mueller, R.-J.1
  • 4
    • 67651095678 scopus 로고    scopus 로고
    • Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate).
    • Ronkvist, A. M., Xie, W., Lu, W., Gross, R. A., Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate). Macromolecules 2009, 42, 5128-5138.
    • (2009) Macromolecules , vol.42 , pp. 5128-5138
    • Ronkvist, A.M.1    Xie, W.2    Lu, W.3    Gross, R.A.4
  • 5
    • 82055202956 scopus 로고    scopus 로고
    • Enzymes for the biofunctionalization of poly(ethylene terephthalate).
    • Zimmermann, W., Billig, S., Enzymes for the biofunctionalization of poly(ethylene terephthalate). Adv. Biochem. Eng. Biotechnol. 2011, 125, 97-120.
    • (2011) Adv. Biochem. Eng. Biotechnol. , vol.125 , pp. 97-120
    • Zimmermann, W.1    Billig, S.2
  • 7
    • 69049109659 scopus 로고    scopus 로고
    • Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules.
    • Eberl, A., Heumann, S., Bruckner, T., Araujo, R. et al., Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules. J. Biotechnol. 2009, 143, 207-212.
    • (2009) J. Biotechnol. , vol.143 , pp. 207-212
    • Eberl, A.1    Heumann, S.2    Bruckner, T.3    Araujo, R.4
  • 8
    • 79959450350 scopus 로고    scopus 로고
    • Enzymatic surface hydrolysis of PET: Effect of structural diversity on kinetic properties of cutinases from
    • Herrero Acero, E., Ribitsch, D., Steinkellner, G., Gruber, K. et al., Enzymatic surface hydrolysis of PET: Effect of structural diversity on kinetic properties of cutinases from Thermobifida. Macromolecules 2011, 44, 4632-4640.
    • (2011) Thermobifida. Macromolecules , vol.44 , pp. 4632-4640
    • Herrero Acero, E.1    Ribitsch, D.2    Steinkellner, G.3    Gruber, K.4
  • 9
    • 15844367333 scopus 로고    scopus 로고
    • Monitoring biotransformations in polyesters.
    • O'Neill, A., Cavaco-Paulo, A., Monitoring biotransformations in polyesters. Biocatal. Biotransform. 2004, 22, 353-356.
    • (2004) Biocatal. Biotransform. , vol.22 , pp. 353-356
    • O'Neill, A.1    Cavaco-Paulo, A.2
  • 10
    • 0032728685 scopus 로고    scopus 로고
    • Assaying for hydroxyl radicals: Hydroxylated terephthalate is a superior fluorescence marker than hydroxylated benzoate.
    • Saran, M., Summer, K. H., Assaying for hydroxyl radicals: Hydroxylated terephthalate is a superior fluorescence marker than hydroxylated benzoate. Free Radical Res. 1999, 31, 429-436.
    • (1999) Free Radical Res. , vol.31 , pp. 429-436
    • Saran, M.1    Summer, K.H.2
  • 11
    • 0018854430 scopus 로고
    • The radiation chemistry of the terephthalate dosimeter.
    • Matthews, R. W., The radiation chemistry of the terephthalate dosimeter. Radiat. Res. 1980, 83, 27-41.
    • (1980) Radiat. Res. , vol.83 , pp. 27-41
    • Matthews, R.W.1
  • 12
    • 0028501285 scopus 로고
    • Dosimetry in sonochemistry: The use of aqueous terephthalate ion as a fluorescence monitor.
    • Mason, T. J., Lorimer, J. P., Bates, D. M., Zhao, Y., Dosimetry in sonochemistry: The use of aqueous terephthalate ion as a fluorescence monitor. Ultrason. Sonochem. 1994, 1, 91-95.
    • (1994) Ultrason. Sonochem. , vol.1 , pp. 91-95
    • Mason, T.J.1    Lorimer, J.P.2    Bates, D.M.3    Zhao, Y.4
  • 13
    • 0030081544 scopus 로고    scopus 로고
    • OH radical formation by ultrasound in aqueous solutions Part I: The chemistry underlying the terephthalate dosimeter.
    • Fang, X., Mark, G., von Sonntag, C., OH radical formation by ultrasound in aqueous solutions Part I: The chemistry underlying the terephthalate dosimeter. Ultrason. Sonochem. 1996, 3, 57-63.
    • (1996) Ultrason. Sonochem. , vol.3 , pp. 57-63
    • Fang, X.1    Mark, G.2    von Sonntag, C.3
  • 14
    • 0032092220 scopus 로고    scopus 로고
    • OH-radical formation by ultrasound in aqueous solution - Part II: Terephthalate and Fricke dosimetry and the influence of various conditions on the sonolytic yield.
    • Mark, G., Tauber, A., Laupert, R., Schuchmann, H.-P. et al., OH-radical formation by ultrasound in aqueous solution - Part II: Terephthalate and Fricke dosimetry and the influence of various conditions on the sonolytic yield. Ultrason. Sonochem. 1998, 5, 41-52.
    • (1998) Ultrason. Sonochem. , vol.5 , pp. 41-52
    • Mark, G.1    Tauber, A.2    Laupert, R.3    Schuchmann, H.-P.4
  • 15
    • 0028873446 scopus 로고
    • Terephthalic acid: A dosimeter for the detection of hydroxyl radicals in vitro.
    • Barreto, J. C., Smith, G. S., Strobel, N. H. P., McQuillin, P. A., Miller, T. A., Terephthalic acid: A dosimeter for the detection of hydroxyl radicals in vitro. Life Sci. 1994, 56, 89-96.
    • (1994) Life Sci. , vol.56 , pp. 89-96
    • Barreto, J.C.1    Smith, G.S.2    Strobel, N.H.P.3    McQuillin, P.A.4    Miller, T.A.5
  • 16
    • 80053929961 scopus 로고    scopus 로고
    • Engineered Thermobifida fusca cutinase with increased activity on polyester substrates.
    • Silva, C., Da, S., Silva, N., Matama, T. et al., Engineered Thermobifida fusca cutinase with increased activity on polyester substrates. Biotechnol. J. 2011, 6, 1230-1239.
    • (2011) Biotechnol. J. , vol.6 , pp. 1230-1239
    • Silva, C.1    Da, S.2    Silva, N.3    Matama, T.4
  • 17
    • 34248338771 scopus 로고    scopus 로고
    • Comparison of the hydrolysis of polyethylene terephthalate fibers by a hydrolase from Fusarium oxysporum LCH I and Fusarium solani f. sp. pisi.
    • Nimchua, T., Punnapayak, H., Zimmermann, W., Comparison of the hydrolysis of polyethylene terephthalate fibers by a hydrolase from Fusarium oxysporum LCH I and Fusarium solani f. sp. pisi. Biotechnol. J. 2007, 2, 361-364.
    • (2007) Biotechnol. J. , vol.2 , pp. 361-364
    • Nimchua, T.1    Punnapayak, H.2    Zimmermann, W.3
  • 18
    • 0037082130 scopus 로고    scopus 로고
    • Iron autoxidation and free radical generation: Effects of buffers, ligands, and chelators.
    • Welch, K. D., Davis, T. Z., Aust, S. D., Iron autoxidation and free radical generation: Effects of buffers, ligands, and chelators. Arch. Biochem. Biophys. 2002, 397, 360-369.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 360-369
    • Welch, K.D.1    Davis, T.Z.2    Aust, S.D.3
  • 19
    • 0034950805 scopus 로고    scopus 로고
    • Fe(II)-EDTA chelate-induced aromatic hydroxylation of terephthalate as a new method for the evaluation of hydroxyl radical-scavenging ability.
    • Yang, X., Guo, X., Fe(II)-EDTA chelate-induced aromatic hydroxylation of terephthalate as a new method for the evaluation of hydroxyl radical-scavenging ability. Analyst 2001, 126, 928-932.
    • (2001) Analyst , vol.126 , pp. 928-932
    • Yang, X.1    Guo, X.2
  • 20
    • 77953935093 scopus 로고    scopus 로고
    • High level expression of a hydrophobic poly(ethylene terephthalate)-hydrolyzing carboxylesterase from Thermobifida fusca KW3 in Escherichia coli BL21(DE3).
    • Oeser, T., Wei, R., Baumgarten, T., Billig, S. et al., High level expression of a hydrophobic poly(ethylene terephthalate)-hydrolyzing carboxylesterase from Thermobifida fusca KW3 in Escherichia coli BL21(DE3). J. Biotechnol. 2010, 146, 100-104.
    • (2010) J. Biotechnol. , vol.146 , pp. 100-104
    • Oeser, T.1    Wei, R.2    Baumgarten, T.3    Billig, S.4
  • 21
    • 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
  • 22
    • 84870663809 scopus 로고    scopus 로고
    • Isolierung identifizierung und biochemische charakterisierung dialkylphthalat spaltender esterasen. PhD Thesis, Heinrich-Heine-Universität, Düsseldorf
    • Pütz, A., Isolierung, identifizierung und biochemische charakterisierung dialkylphthalat spaltender esterasen. PhD Thesis, Heinrich-Heine-Universität, Düsseldorf 2006, pp. 39-40.
    • (2006) , pp. 39-40
    • Pütz, A.1
  • 23
    • 77955550271 scopus 로고    scopus 로고
    • Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3.
    • Billig, S., Oeser, T., Birkemeyer, C., Zimmermann, W., Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3. Appl. Microbiol. Biotechnol. 2010, 87, 1753-1764.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1753-1764
    • Billig, S.1    Oeser, T.2    Birkemeyer, C.3    Zimmermann, W.4
  • 24
    • 0029657410 scopus 로고    scopus 로고
    • Estimation of gas solubilities in salt solutions at temperatures from 273 K to 363 K.
    • Weisenberger, S., Schumpe, A., Estimation of gas solubilities in salt solutions at temperatures from 273 K to 363 K. AIChE J 1996, 42, 298-300.
    • (1996) AIChE J , vol.42 , pp. 298-300
    • Weisenberger, S.1    Schumpe, A.2
  • 25
    • 0025981555 scopus 로고
    • Oxidation of tris to one-carbon compounds in a radical-producing model system, in microsomes, in hepatocytes and in rats.
    • Schacker, M., Foth, H., Schluter, J., Kahl, R., Oxidation of tris to one-carbon compounds in a radical-producing model system, in microsomes, in hepatocytes and in rats. Free Radical Res. Commun. 1991, 11, 339-347.
    • (1991) Free Radical Res. Commun. , vol.11 , pp. 339-347
    • Schacker, M.1    Foth, H.2    Schluter, J.3    Kahl, R.4
  • 26
    • 4544260385 scopus 로고    scopus 로고
    • An HPLC assay of hydroxyl radicals by the hydroxylation reaction of terephthalic acid.
    • Linxiang, L., Abe, Y., Nagasawa, Y., Kudo, R. et al., An HPLC assay of hydroxyl radicals by the hydroxylation reaction of terephthalic acid. Biomed. Chromatogr. 2004, 18, 470-474.
    • (2004) Biomed. Chromatogr. , vol.18 , pp. 470-474
    • Linxiang, L.1    Abe, Y.2    Nagasawa, Y.3    Kudo, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.