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Volumn 11, Issue 8, 2016, Pages 1082-1087

A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films

Author keywords

Biocatalysis; Biodegradation; Bioprocess engineering; Polyester hydrolases; Synthetic polymers

Indexed keywords

BIOCATALYSTS; BIODEGRADABLE POLYMERS; BIODEGRADATION; DEGRADATION; ENZYMATIC HYDROLYSIS; ENZYMES; HYDROLASES; HYDROLYSIS; POLYETHYLENE TEREPHTHALATES;

EID: 84979742773     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201600008     Document Type: Article
Times cited : (165)

References (27)
  • 1
    • 84883176461 scopus 로고    scopus 로고
    • Chemical recycling of poly(ethylene terephthalate) using sulfuric acid
    • Tabekh, H., Koudsi, Y., Ajji, Z., Chemical recycling of poly(ethylene terephthalate) using sulfuric acid. Rev. Roum. Chim. 2012, 57, 1031–1036.
    • (2012) Rev. Roum. Chim. , vol.57 , pp. 1031-1036
    • Tabekh, H.1    Koudsi, Y.2    Ajji, Z.3
  • 2
    • 84887918056 scopus 로고    scopus 로고
    • Post-consumer PET bottles recycling II. PET depolymerization using microwaves
    • Rusen, E., Mocanu, A., Rizea, F., Diacon, A. et al., Post-consumer PET bottles recycling II. PET depolymerization using microwaves. Mater. Plast. 2013, 50, 201–207.
    • (2013) Mater. Plast. , vol.50 , pp. 201-207
    • Rusen, E.1    Mocanu, A.2    Rizea, F.3    Diacon, A.4
  • 3
    • 78649319944 scopus 로고    scopus 로고
    • Plastic waste management in the context of a European recycling society: Comparing results and uncertainties in a life cycle perspective
    • Lazarevic, D., Aoustin, E., Buclet, N., Brandt, N., Plastic waste management in the context of a European recycling society: Comparing results and uncertainties in a life cycle perspective. Resour. Conserv. Recycl. 2010, 55, 246–259.
    • (2010) Resour. Conserv. Recycl. , vol.55 , pp. 246-259
    • Lazarevic, D.1    Aoustin, E.2    Buclet, N.3    Brandt, N.4
  • 4
    • 24944479050 scopus 로고    scopus 로고
    • Enzymatic degradation of poly(ethylene terephthalate): Rapid hydrolyse using a hydrolase from T. fusca
    • Mueller, R.-J., Schrader, H., Profe, J., Dresler, K., Deckwer, W.-D., Enzymatic degradation of poly(ethylene terephthalate): Rapid hydrolyse using a hydrolase from T. fusca. Macromol. Rapid Commun. 2005, 26, 1400–1405.
    • (2005) Macromol. Rapid Commun. , vol.26 , pp. 1400-1405
    • Mueller, R.-J.1    Schrader, H.2    Profe, J.3    Dresler, K.4    Deckwer, W.-D.5
  • 5
    • 84909619411 scopus 로고    scopus 로고
    • Effect of hydrolysis products on the enzymatic degradation of polyethylene terephthalate nanoparticles by a polyester hydrolase from Thermobifida fusca
    • Barth, M., Oeser, T., Wei, R., Then, J. et al., Effect of hydrolysis products on the enzymatic degradation of polyethylene terephthalate nanoparticles by a polyester hydrolase from Thermobifida fusca. Biochem. Eng. J. 2015, 93, 222–228.
    • (2015) Biochem. Eng. J. , vol.93 , pp. 222-228
    • Barth, M.1    Oeser, T.2    Wei, R.3    Then, J.4
  • 7
    • 0035970980 scopus 로고    scopus 로고
    • Biodegradation of polyesters containing aromatic constituents
    • Mueller, R. J., Kleeberg, I., Deckwer, W. D., Biodegradation of polyesters containing aromatic constituents. J. Biotechnol. 2001, 86, 87–95.
    • (2001) J. Biotechnol. , vol.86 , pp. 87-95
    • Mueller, R.J.1    Kleeberg, I.2    Deckwer, W.D.3
  • 8
    • 84905993861 scopus 로고    scopus 로고
    • Synthetic polyester-hydrolyzing enzymes from thermophilic actinomycetes
    • Wei, R., Oeser, T., Zimmermann, W., Synthetic polyester-hydrolyzing enzymes from thermophilic actinomycetes. Adv. Appl. Microbiol. 2014, 89, 267–305.
    • (2014) Adv. Appl. Microbiol. , vol.89 , pp. 267-305
    • Wei, R.1    Oeser, T.2    Zimmermann, W.3
  • 9
    • 67651095678 scopus 로고    scopus 로고
    • Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate)
    • Ronkvist, A., Xie, W., Lu, W., Gross, R., Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate). Macromolecules 2009, 42, 5128–5138.
    • (2009) Macromolecules , vol.42 , pp. 5128-5138
    • Ronkvist, A.1    Xie, W.2    Lu, W.3    Gross, R.4
  • 10
    • 84940205524 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of polyethylene terephthalate films in an ultrafiltration membrane reactor
    • Barth, M., Wei, R., Oeser, T., Then, J. et al., Enzymatic hydrolysis of polyethylene terephthalate films in an ultrafiltration membrane reactor. J. Membr. Sci. 2015, 494, 182–187.
    • (2015) J. Membr. Sci. , vol.494 , pp. 182-187
    • Barth, M.1    Wei, R.2    Oeser, T.3    Then, J.4
  • 11
    • 77949567647 scopus 로고    scopus 로고
    • Reactor design for minimizing product inhibition during enzymatic lignocellulose hydrolysis II. Quantification of inhibition and suitability of membrane reactors
    • Andric, P., Meyer, A. S., Jensen, P. A., Dam-Johansen, K., Reactor design for minimizing product inhibition during enzymatic lignocellulose hydrolysis II. Quantification of inhibition and suitability of membrane reactors. Biotechnol. Adv. 2010, 28, 407–425.
    • (2010) Biotechnol. Adv. , vol.28 , pp. 407-425
    • Andric, P.1    Meyer, A.S.2    Jensen, P.A.3    Dam-Johansen, K.4
  • 12
    • 0021460975 scopus 로고
    • Enzymatic hydrolysis of sodium-hydroxide-pretreated sallow in an ultrafiltration membrane reactor
    • Ohlson, I., Trägårdh, G., Hahn-Hägerdal, B., Enzymatic hydrolysis of sodium-hydroxide-pretreated sallow in an ultrafiltration membrane reactor. Biotechnol. Bioeng. 1984, 26, 647–653.
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 647-653
    • Ohlson, I.1    Trägårdh, G.2    Hahn-Hägerdal, B.3
  • 13
    • 84881093666 scopus 로고    scopus 로고
    • Chemical approaches for the construction of multi-enzyme reaction systems
    • Schoffelen, S., van Hest, J. C. M., Chemical approaches for the construction of multi-enzyme reaction systems. Curr. Opin. Struct. Biol. 2013, 23, 613–621.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 613-621
    • Schoffelen, S.1    van Hest, J.C.M.2
  • 14
    • 80052812654 scopus 로고    scopus 로고
    • Multi-enzymatic cascade reactions: Overview and perspectives
    • Ricca, E., Brucher, B., Schrittwieser, J. H., Multi-enzymatic cascade reactions: Overview and perspectives. Adv. Synth. Catal. 2011, 353, 2239–2262.
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2239-2262
    • Ricca, E.1    Brucher, B.2    Schrittwieser, J.H.3
  • 15
    • 77949873378 scopus 로고    scopus 로고
    • Review: Continuous hydrolysis and fermentation for cellulosic ethanol production
    • Brethauer, S., Wyman, C. E., Review: Continuous hydrolysis and fermentation for cellulosic ethanol production. Bioresour. Technol. 2010, 101, 4862–4874.
    • (2010) Bioresour. Technol. , vol.101 , pp. 4862-4874
    • Brethauer, S.1    Wyman, C.E.2
  • 16
    • 77957021521 scopus 로고    scopus 로고
    • Technological trends, global market, and challenges of bio-ethanol production
    • Mussatto, S. I., Dragone, G., Guimarães, P. M., Silva, J. P. A. et al., Technological trends, global market, and challenges of bio-ethanol production. Biotechnol. Adv. 2010, 28, 817–830.
    • (2010) Biotechnol. Adv. , vol.28 , pp. 817-830
    • Mussatto, S.I.1    Dragone, G.2    Guimarães, P.M.3    Silva, J.P.A.4
  • 17
    • 84856764807 scopus 로고    scopus 로고
    • Multi-enzyme systems: Bringing enzymes together in vitro
    • Schoffelen, S., van Hest, J. C., Multi-enzyme systems: Bringing enzymes together in vitro. Soft Matter 2012, 8, 1736–1746.
    • (2012) Soft Matter , vol.8 , pp. 1736-1746
    • Schoffelen, S.1    van Hest, J.C.2
  • 19
    • 33144488261 scopus 로고    scopus 로고
    • Immobilization of beta-glucosidase on Eupergit C for lignocellulose hydrolysis
    • Tu, M. B., Zhang, X., Kurabi, A., Gilkes, N. et al., Immobilization of beta-glucosidase on Eupergit C for lignocellulose hydrolysis. Biotechnol. Lett. 2006, 28, 151–156.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 151-156
    • Tu, M.B.1    Zhang, X.2    Kurabi, A.3    Gilkes, N.4
  • 20
    • 0016558488 scopus 로고
    • Kinetic studies on insoluble cellulose-cellulase system
    • Huang, A. A., Kinetic studies on insoluble cellulose-cellulase system. Biotechnol. Bioeng. 1975, 17, 1421–1433.
    • (1975) Biotechnol. Bioeng. , vol.17 , pp. 1421-1433
    • Huang, A.A.1
  • 21
    • 84870703309 scopus 로고    scopus 로고
    • A high-throughput assay for enzymatic polyester hydrolysis activity by fluorimetric detection
    • Wei, R., Oeser, T., Billig, S., Zimmermann, W., A high-throughput assay for enzymatic polyester hydrolysis activity by fluorimetric detection. Biotechnol. J. 2012, 7, 1517–1521.
    • (2012) Biotechnol. J. , vol.7 , pp. 1517-1521
    • Wei, R.1    Oeser, T.2    Billig, S.3    Zimmermann, W.4
  • 22
    • 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
  • 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
    • 84897051705 scopus 로고    scopus 로고
    • Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase
    • Sulaiman, S., You, D.-J., Kanaya, E., Koga, Y., Kanaya, S., Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase. Biochemistry 2014, 53, 1858–1869.
    • (2014) Biochemistry , vol.53 , pp. 1858-1869
    • Sulaiman, S.1    You, D.-J.2    Kanaya, E.3    Koga, Y.4    Kanaya, S.5
  • 27
    • 0342459772 scopus 로고    scopus 로고
    • Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
    • Gonçalves, A., Schacht, E., Matthijs, G., Barros, M. A. et al., Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports. Enzyme Microb. Technol. 1999, 24, 60–66.
    • (1999) Enzyme Microb. Technol. , vol.24 , pp. 60-66
    • Gonçalves, A.1    Schacht, E.2    Matthijs, G.3    Barros, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.