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Volumn 4, Issue 1, 2014, Pages 1-10

Functional characterization and structural modeling of synthetic polyester-degrading hydrolases from Thermomonospora curvata

Author keywords

Polyester hydrolase; Polyethylene terephthalate (PET); Synthetic polyester; Thermomonospora curvata

Indexed keywords

ESTERASE; HYDROLASE; NANOPARTICLE; POLYCAPROLACTONE; POLYESTER; POLYETHYLENE TEREPHTHALATE;

EID: 84947032242     PISSN: None     EISSN: 21910855     Source Type: Journal    
DOI: 10.1186/s13568-014-0044-9     Document Type: Article
Times cited : (135)

References (42)
  • 1
    • 33745518447 scopus 로고    scopus 로고
    • Increase of the hydrophilicity of polyethylene terephthalate fibres by hydrolases from Thermomonospora fusca and Fusarium solani f. sp. pisi
    • COI: 1:CAS:528:DC%2BD28XmtVOqs7Y%3D, PID: 16791721
    • Alisch-Mark M, Herrmann A, Zimmermann W (2006) Increase of the hydrophilicity of polyethylene terephthalate fibres by hydrolases from Thermomonospora fusca and Fusarium solani f. sp. pisi. Biotechnol Lett 28(10):681–685. doi:10.1007/s10529-006-9041-7
    • (2006) Biotechnol Lett , vol.28 , Issue.10 , pp. 681-685
    • Alisch-Mark, M.1    Herrmann, A.2    Zimmermann, W.3
  • 2
    • 15844406213 scopus 로고    scopus 로고
    • Biocatalytic modification of polyethylene terephthalate fibres by esterases from actinomycete isolates
    • COI: 1:CAS:528:DC%2BD2MXitVCmsLk%3D
    • Alisch M, Feuerhack A, Müller H, Mensak B, Andreaus J, Zimmermann W (2004) Biocatalytic modification of polyethylene terephthalate fibres by esterases from actinomycete isolates. Biocatal Biotransform 22(5-6):347–351. doi:10.1080/10242420400025877
    • (2004) Biocatal Biotransform , vol.22 , Issue.5-6 , pp. 347-351
    • Alisch, M.1    Feuerhack, A.2    Müller, H.3    Mensak, B.4    Andreaus, J.5    Zimmermann, W.6
  • 3
    • 0037161960 scopus 로고    scopus 로고
    • Glass transition and structural relaxation in semi-crystalline poly(ethylene terephthalate): a DSC study
    • COI: 1:CAS:528:DC%2BD38Xjsl2ju74%3D
    • Alves NM, Mano JF, Balaguer E, Meseguer Duenas JM, Gomez Ribelles JL (2002) Glass transition and structural relaxation in semi-crystalline poly(ethylene terephthalate): a DSC study. Polymer 43(15):4111–4122. doi:10.1016/S0032-3861(02)00236-7
    • (2002) Polymer , vol.43 , Issue.15 , pp. 4111-4122
    • Alves, N.M.1    Mano, J.F.2    Balaguer, E.3    Meseguer Duenas, J.M.4    Gomez Ribelles, J.L.5
  • 5
    • 77955550271 scopus 로고    scopus 로고
    • Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3
    • COI: 1:CAS:528:DC%2BC3cXoslantbk%3D, PID: 20467738
    • Billig S, Oeser T, Birkemeyer C, Zimmermann W (2010) Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3. Appl Microbiol Biotechnol 87(5):1753–1764. doi:10.1007/s00253-010-2635-y
    • (2010) Appl Microbiol Biotechnol , vol.87 , Issue.5 , pp. 1753-1764
    • Billig, S.1    Oeser, T.2    Birkemeyer, C.3    Zimmermann, W.4
  • 6
    • 69549084345 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold: an update
    • COI: 1:CAS:528:DC%2BD1MXhtlentLzF, PID: 19508187
    • Carr PD, Ollis DL (2009) Alpha/beta hydrolase fold: an update. Protein Pept Lett 16(10):1137–1148. doi:10.2174/092986609789071298
    • (2009) Protein Pept Lett , vol.16 , Issue.10 , pp. 1137-1148
    • Carr, P.D.1    Ollis, D.L.2
  • 7
    • 77949540160 scopus 로고    scopus 로고
    • Biochemical characterization of the cutinases from Thermobifida fusca
    • COI: 1:CAS:528:DC%2BC3cXis1arsLk%3D
    • Chen S, Su L, Billig S, Zimmermann W, Chen J, Wu J (2010) Biochemical characterization of the cutinases from Thermobifida fusca. J Mol Catal B-Enzym 63(3–4):121–127. doi:10.1016/j.molcatb.2010.01.001
    • (2010) J Mol Catal B-Enzym , vol.63 , Issue.3-4 , pp. 121-127
    • Chen, S.1    Su, L.2    Billig, S.3    Zimmermann, W.4    Chen, J.5    Wu, J.6
  • 8
    • 54449102399 scopus 로고    scopus 로고
    • Identification and characterization of bacterial cutinase
    • COI: 1:CAS:528:DC%2BD1cXhtFSltLrN, PID: 18658138
    • Chen S, Tong X, Woodard RW, Du G, Wu J, Chen J (2008) Identification and characterization of bacterial cutinase. J Biol Chem 283(38):25854–25862. doi:10.1074/jbc.M800848200
    • (2008) J Biol Chem , vol.283 , Issue.38 , pp. 25854-25862
    • Chen, S.1    Tong, X.2    Woodard, R.W.3    Du, G.4    Wu, J.5    Chen, J.6
  • 10
    • 0010889058 scopus 로고
    • A universal buffer solution for use in ultra-violet spectrophotometry
    • COI: 1:CAS:528:DyaG1MXpt1Okuw%3D%3D
    • Davies MT (1959) A universal buffer solution for use in ultra-violet spectrophotometry. Analyst 84:248–251. doi:10.1039/AN9598400248
    • (1959) Analyst , vol.84 , pp. 248-251
    • Davies, M.T.1
  • 11
    • 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
    • COI: 1:CAS:528:DC%2BD1MXhtVKksbfJ, PID: 19616594
    • Eberl A, Heumann S, Bruckner T, Araujo R, Cavaco-Paulo A, Kaufmann F, Kroutil W, Guebitz GM (2009) Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules. J Biotechnol 143(3):207–212. doi:10.1016/j.jbiotec.2009.07.008
    • (2009) J Biotechnol , vol.143 , Issue.3 , pp. 207-212
    • Eberl, A.1    Heumann, S.2    Bruckner, T.3    Araujo, R.4    Cavaco-Paulo, A.5    Kaufmann, F.6    Kroutil, W.7    Guebitz, G.M.8
  • 12
    • 0033646650 scopus 로고    scopus 로고
    • Fusarium solani pisi cutinase
    • COI: 1:CAS:528:DC%2BD3cXovFagsr4%3D, PID: 11099798
    • Egmond MR, de Vlieg J (2000) Fusarium solani pisi cutinase. Biochimie 82(11):1015–1021. doi:10.1016/S0300-9084(00)01183-4
    • (2000) Biochimie , vol.82 , Issue.11 , pp. 1015-1021
    • Egmond, M.R.1    de Vlieg, J.2
  • 13
    • 34250956819 scopus 로고
    • Beitraege zur Morphologie und Systematik der thermophilen Actinomyceten
    • COI: 1:STN:280:DyaG2s%2Fot1Gjuw%3D%3D, PID: 13435805
    • Henssen A (1957) Beitraege zur Morphologie und Systematik der thermophilen Actinomyceten. Arch Mikrobiol 26(4):373–414. doi:10.1007/bf00407588
    • (1957) Arch Mikrobiol , vol.26 , Issue.4 , pp. 373-414
    • Henssen, A.1
  • 14
    • 0014213091 scopus 로고
    • Zur Kenntnis thermophiler Actinomyceten
    • COI: 1:STN:280:DyaF1M%2FgsFCrug%3D%3D, PID: 5600778
    • Henssen A, Schnepf E (1967) Zur Kenntnis thermophiler Actinomyceten. Arch Mikrobiol 57(3):214–231. doi:10.1007/bf00405948
    • (1967) Arch Mikrobiol , vol.57 , Issue.3 , pp. 214-231
    • Henssen, A.1    Schnepf, E.2
  • 17
    • 33745512493 scopus 로고    scopus 로고
    • Mechanism and kinetics of the enzymatic hydrolysis of polyester nanoparticles by lipases
    • COI: 1:CAS:528:DC%2BD28XmsF2isbs%3D
    • Herzog K, Müller RJ, Deckwer WD (2006) Mechanism and kinetics of the enzymatic hydrolysis of polyester nanoparticles by lipases. Polym Degrad Stab 91(10):2486–2498. doi:10.1016/j.polymdegradstab.2006.03.005
    • (2006) Polym Degrad Stab , vol.91 , Issue.10 , pp. 2486-2498
    • Herzog, K.1    Müller, R.J.2    Deckwer, W.D.3
  • 18
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • COI: 1:CAS:528:DC%2BD1cXhsVSqurc%3D
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3):435–447. doi:10.1021/ct700301q
    • (2008) J Chem Theory Comput , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 19
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • COI: 1:CAS:528:DC%2BD28XhtFWqt7fM, PID: 16981200
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling C (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65(3):712–725. doi:10.1002/prot.21123
    • (2006) Proteins , vol.65 , Issue.3 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 20
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • COI: 1:CAS:528:DyaK1MXmvVOnsb4%3D, PID: 10547694
    • Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315–351. doi:10.1146/annurev.micro.53.1.315
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 21
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • COI: 1:CAS:528:DyaK2sXis1KntLo%3D, PID: 9126849
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267(3):727–748. doi:10.1006/jmbi.1996.0897
    • (1997) J Mol Biol , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 22
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • COI: 1:CAS:528:DC%2BD1MXivF2itbs%3D, PID: 19247286
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4(3):363–371. doi:10.1038/nprot.2009.2
    • (2009) Nat Protoc , vol.4 , Issue.3 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 23
    • 84863418333 scopus 로고    scopus 로고
    • Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution
    • COI: 1:CAS:528:DC%2BC38Xjt1elsrY%3D
    • Kitadokoro K, Thumarat U, Nakamura R, Nishimura K, Karatani H, Suzuki H, Kawai F (2012) Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution. Polym Degrad Stab 97(5):771–775. doi:10.1016/j.polymdegradstab.2012.02.003
    • (2012) Polym Degrad Stab , vol.97 , Issue.5 , pp. 771-775
    • Kitadokoro, K.1    Thumarat, U.2    Nakamura, R.3    Nishimura, K.4    Karatani, H.5    Suzuki, H.6    Kawai, F.7
  • 24
    • 0031804477 scopus 로고    scopus 로고
    • Biodegradation of aliphatic-aromatic copolyesters by Thermomonospora fusca and other thermophilic compost isolates
    • COI: 1:CAS:528:DyaK1cXislWlsrc%3D, PID: 9572944
    • Kleeberg I, Hetz C, Kroppenstedt RM, Muller RJ, Deckwer WD (1998) Biodegradation of aliphatic-aromatic copolyesters by Thermomonospora fusca and other thermophilic compost isolates. Appl Environ Microbiol 64(5):1731–1735
    • (1998) Appl Environ Microbiol , vol.64 , Issue.5 , pp. 1731-1735
    • Kleeberg, I.1    Hetz, C.2    Kroppenstedt, R.M.3    Muller, R.J.4    Deckwer, W.D.5
  • 25
    • 24944479050 scopus 로고    scopus 로고
    • Enzymatic degradation of poly(ethylene terephthalate): rapid hydrolyse using a hydrolase from T. fusca
    • Müller R-J, Schrader H, Profe J, Dresler K, Deckwer W-D (2005) Enzymatic degradation of poly(ethylene terephthalate): rapid hydrolyse using a hydrolase from T. fusca. Macromol Rapid Commun 26(17):1400–1405. doi:10.1002/marc.200500410
    • (2005) Macromol Rapid Commun , vol.26 , Issue.17 , pp. 1400-1405
    • Müller, R.-J.1    Schrader, H.2    Profe, J.3    Dresler, K.4    Deckwer, W.-D.5
  • 26
    • 0037622193 scopus 로고    scopus 로고
    • Studies on the enzymatic hydrolysis of polyesters I. Low molecular mass model esters and aliphatic polyesters
    • COI: 1:CAS:528:DC%2BD3sXjtFehsb0%3D
    • Marten E, Müller R-J, Deckwer W-D (2003) Studies on the enzymatic hydrolysis of polyesters I. Low molecular mass model esters and aliphatic polyesters. Polym Degrad Stab 80(3):485–501. doi:10.1016/S0141-3910(03)00032-6
    • (2003) Polym Degrad Stab , vol.80 , Issue.3 , pp. 485-501
    • Marten, E.1    Müller, R.-J.2    Deckwer, W.-D.3
  • 27
    • 14844317362 scopus 로고    scopus 로고
    • Studies on the enzymatic hydrolysis of polyesters. II Aliphatic-aromatic copolyesters
    • COI: 1:CAS:528:DC%2BD2MXisVCks7g%3D
    • Marten E, Müller R-J, Deckwer W-D (2005) Studies on the enzymatic hydrolysis of polyesters. II Aliphatic-aromatic copolyesters. Polym Degrad Stab 88(3):371–381. doi:10.1016/j.polymdegradstab.2004.12.001
    • (2005) Polym Degrad Stab , vol.88 , Issue.3 , pp. 371-381
    • Marten, E.1    Müller, R.-J.2    Deckwer, W.-D.3
  • 28
    • 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
    • COI: 1:CAS:528:DC%2BD2sXktVWjt70%3D, PID: 17136729
    • Nimchua T, Punnapayak H, Zimmermann W (2007) Comparison of the hydrolysis of polyethylene terephthalate fibers by a hydrolase from Fusarium oxysporum LCH I and Fusarium solani f. sp. pisi. Biotechnol J 2(3):361–364. doi:10.1002/biot.200600095
    • (2007) Biotechnol J , vol.2 , Issue.3 , pp. 361-364
    • Nimchua, T.1    Punnapayak, H.2    Zimmermann, W.3
  • 29
    • 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)
    • COI: 1:CAS:528:DC%2BC3cXjs1eju7c%3D, PID: 20156495
    • Oeser T, Wei R, Baumgarten T, Billig S, Follner C, Zimmermann W (2010) High level expression of a hydrophobic poly(ethylene terephthalate)-hydrolyzing carboxylesterase from Thermobifida fusca KW3 in Escherichia coli BL21(DE3). J Biotechnol 146(3):100–104. doi:10.1016/j.jbiotec.2010.02.006
    • (2010) J Biotechnol , vol.146 , Issue.3 , pp. 100-104
    • Oeser, T.1    Wei, R.2    Baumgarten, T.3    Billig, S.4    Follner, C.5    Zimmermann, W.6
  • 31
    • 0031117869 scopus 로고    scopus 로고
    • Chemical recycling of poly(ethylene terephthalate)
    • COI: 1:CAS:528:DyaK2sXhslGhs7Y%3D
    • Paszun D, Spychaj T (1997) Chemical recycling of poly(ethylene terephthalate). Ind Eng Chem Res 36(4):1373–1383. doi:10.1021/ie960563c
    • (1997) Ind Eng Chem Res , vol.36 , Issue.4 , pp. 1373-1383
    • Paszun, D.1    Spychaj, T.2
  • 34
    • 67651095678 scopus 로고    scopus 로고
    • Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate)
    • COI: 1:CAS:528:DC%2BD1MXotVGksb0%3D
    • Ronkvist ÃM, Xie W, Lu W, Gross RA (2009) Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate). Macromolecules 42(14):5128–5138. doi:10.1021/ma9005318
    • (2009) Macromolecules , vol.42 , Issue.14 , pp. 5128-5138
    • Ronkvist, Ã.M.1    Xie, W.2    Lu, W.3    Gross, R.A.4
  • 35
    • 23144440940 scopus 로고    scopus 로고
    • PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information
    • COI: 1:CAS:528:DC%2BD2MXlslyrur0%3D, PID: 15980472
    • Simossis VA, Heringa J (2005) PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information. Nucleic Acids Res 33(Web Server issue):W289–W294. doi:10.1093/nar/gki390
    • (2005) Nucleic Acids Res , vol.33 , Issue.Web Server issue , pp. 289-294
    • Simossis, V.A.1    Heringa, J.2
  • 36
    • 84863172260 scopus 로고    scopus 로고
    • Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach
    • COI: 1:CAS:528:DC%2BC38XjtVSntLY%3D, PID: 22194294
    • Sulaiman S, Yamato S, Kanaya E, Kim JJ, Koga Y, Takano K, Kanaya S (2012) Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach. Appl Environ Microbiol 78(5):1556–1562. doi:10.1128/AEM.06725-11
    • (2012) Appl Environ Microbiol , vol.78 , Issue.5 , pp. 1556-1562
    • Sulaiman, S.1    Yamato, S.2    Kanaya, E.3    Kim, J.J.4    Koga, Y.5    Takano, K.6    Kanaya, S.7
  • 37
    • 0026535749 scopus 로고
    • Purification and properties of lipase from Penicillium simplicissimum
    • COI: 1:CAS:528:DyaK38XhvV2qtbY%3D, PID: 1576166
    • Sztajer H, Lunsdorf H, Erdmann H, Menge U, Schmid R (1992) Purification and properties of lipase from Penicillium simplicissimum. Biochim Biophys Acta 1124(3):253–261
    • (1992) Biochim Biophys Acta , vol.1124 , Issue.3 , pp. 253-261
    • Sztajer, H.1    Lunsdorf, H.2    Erdmann, H.3    Menge, U.4    Schmid, R.5
  • 38
    • 84864717982 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
    • COI: 1:CAS:528:DC%2BC38XotlSks74%3D, PID: 22183084
    • Thumarat U, Nakamura R, Kawabata T, Suzuki H, Kawai F (2012) Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119. Appl Microbiol Biotechnol 95(2):419–430. doi:10.1007/s00253-011-3781-6
    • (2012) Appl Microbiol Biotechnol , vol.95 , Issue.2 , pp. 419-430
    • Thumarat, U.1    Nakamura, R.2    Kawabata, T.3    Suzuki, H.4    Kawai, F.5
  • 41
    • 0031799382 scopus 로고    scopus 로고
    • Reclassification of Thermomonospora and Microtetraspora
    • PID: 9731279
    • Zhang Z, Wang Y, Ruan J (1998) Reclassification of Thermomonospora and Microtetraspora. Int J Syst Bacteriol 48(2):411–422. doi:10.1099/00207713-48-2-411
    • (1998) Int J Syst Bacteriol , vol.48 , Issue.2 , pp. 411-422
    • Zhang, Z.1    Wang, Y.2    Ruan, J.3
  • 42
    • 82055202956 scopus 로고    scopus 로고
    • Enzymes for the biofunctionalization of poly(ethylene terephthalate)
    • Nyanhongo GS, Steiner W, Guebitz G, (eds), Adv Biochem Eng/Biotechnol, 125, Springer, Berlin/Heidelberg
    • Zimmermann W, Billig S (2011) Enzymes for the biofunctionalization of poly(ethylene terephthalate). In: Nyanhongo GS, Steiner W, Guebitz G (ed) Biofunctionalization of polymers and their applications. Adv Biochem Eng/Biotechnol, vol 125. Springer, Berlin/Heidelberg, pp 97–120. doi:10.1007/10_2010_87
    • (2011) Biofunctionalization of polymers and their applications , pp. 97-120
    • Zimmermann, W.1    Billig, S.2


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