메뉴 건너뛰기




Volumn 110, Issue 10, 2013, Pages 2581-2590

Surface engineering of a cutinase from Thermobifida Cellulosilytica for improved polyester hydrolysis

Author keywords

PET degradation; Polyesterase; Surface engineering

Indexed keywords

ESCHERICHIA COLI; HYDROLYSIS; SUBSTRATES; SURFACE CHEMISTRY; SURFACE PROPERTIES; SURFACES;

EID: 84896419055     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24930     Document Type: Article
Times cited : (133)

References (35)
  • 3
    • 33745518447 scopus 로고    scopus 로고
    • Increase of the hydrophilicity of polyethylene terephthalate fibers by hydrolases from Thermomonospora fusca and Fusarium solani f. sp pisi
    • Alisch-Mark M, Herrmann A, Zimmermann W. 2006. Increase of the hydrophilicity of polyethylene terephthalate fibers by hydrolases from Thermomonospora fusca and Fusarium solani f. sp pisi. Biotechnol Lett 28:681-685.
    • (2006) Biotechnol Lett , vol.28 , pp. 681-685
    • Alisch-Mark, M.1    Herrmann, A.2    Zimmermann, W.3
  • 5
    • 54749095850 scopus 로고    scopus 로고
    • Enzymatic and chemical hydrolysis of poly(ethylene terephthalate) fabrics
    • Brueckner T, Eberl A, Heumann S, Rabe M, Guebitz GM. 2008. Enzymatic and chemical hydrolysis of poly(ethylene terephthalate) fabrics. J Polym Sci [A1] 46:6435-6443.
    • (2008) J Polym Sci [A1] , vol.46 , pp. 6435-6443
    • Brueckner, T.1    Eberl, A.2    Heumann, S.3    Rabe, M.4    Guebitz, G.M.5
  • 6
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu AA, Shelenkov AA, Dunbrack RL, Jr. 2003. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci 12:2001-2014.
    • (2003) Protein Sci , vol.12 , pp. 2001-2014
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack Jr., R.L.3
  • 7
    • 79957875229 scopus 로고    scopus 로고
    • Tuning different expression parameters to achieve soluble recombinant proteins in E.coli: Advantage of high-throughput screening
    • Correa A, Oppezzo P. 2011. Tuning different expression parameters to achieve soluble recombinant proteins in E.coli: Advantage of high-throughput screening. Biotechnol J 6:715-730.
    • (2011) Biotechnol J , vol.6 , pp. 715-730
    • Correa, A.1    Oppezzo, P.2
  • 8
    • 77955515872 scopus 로고    scopus 로고
    • Surface structure and properties of poly-(ethylene terephthalate) hydrolyzed by alkali and cutinase
    • Donelli I, Freddi G, Nierstrasz VA, Taddei P. 2010. Surface structure and properties of poly-(ethylene terephthalate) hydrolyzed by alkali and cutinase. Polym Degrad Stab 95:1542-1550.
    • (2010) Polym Degrad Stab , vol.95 , pp. 1542-1550
    • Donelli, I.1    Freddi, G.2    Nierstrasz, V.A.3    Taddei, P.4
  • 10
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Dunbrack RL, Jr., Cohen FE. 1997. Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci 6:1661-1681.
    • (1997) Protein Sci , vol.6 , pp. 1661-1681
    • Dunbrack Jr., R.L.1    Cohen, F.E.2
  • 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
    • Eberl A, Heumann S, Brueckner T, Araújo R, Cavaco-Paulo A, Kaufmann F. 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 143:207-212.
    • (2009) J. Biotechnol , vol.143 , pp. 207-212
    • Eberl, A.1    Heumann, S.2    Brueckner, T.3    Araújo, R.4    Cavaco-Paulo, A.5    Kaufmann, F.6
  • 12
    • 37349064200 scopus 로고    scopus 로고
    • Enzymes go big: Surface hydrolysis and functionalisation of synthetic polymers
    • Guebitz GM, Cavaco-Paulo A. 2008. Enzymes go big: Surface hydrolysis and functionalisation of synthetic polymers. Trends Biotechnol 26:32-38.
    • (2008) Trends Biotechnol , vol.26 , pp. 32-38
    • Guebitz, G.M.1    Cavaco-Paulo, A.2
  • 13
    • 0034669395 scopus 로고    scopus 로고
    • Surface hydrophobic amino acid residues in cellulase molecules as a structural factor responsible for their high denim-washing performance
    • Gusakov AV, Sinitsyn AP, Berlin AG, Markov AV, Ankudimova NV. 2000. Surface hydrophobic amino acid residues in cellulase molecules as a structural factor responsible for their high denim-washing performance. Enzyme Microb Technol 27:664-671.
    • (2000) Enzyme Microb Technol , vol.27 , pp. 664-671
    • Gusakov, A.V.1    Sinitsyn, A.P.2    Berlin, A.G.3    Markov, A.V.4    Ankudimova, N.V.5
  • 16
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B, Nicholls A. 1995. Classical electrostatics in biology and chemistry. Science 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 17
    • 84863303532 scopus 로고    scopus 로고
    • Industrial production of recombinant therapeutics on Escherichia coli and its recent advancements
    • Huang CJ, Lin H, Yang X. 2012. Industrial production of recombinant therapeutics on Escherichia coli and its recent advancements. J Ind Microbiol Biotechnol 39:383-399.
    • (2012) J Ind Microbiol Biotechnol , vol.39 , pp. 383-399
    • Huang, C.J.1    Lin, H.2    Yang, X.3
  • 18
    • 84940285640 scopus 로고    scopus 로고
    • Conference Book, EMBO conference catalytic mechanism by biological systems, 7-10 October 2012,
    • Kellis J, Estell D, Cascão-Pereira L. 2012. Conference Book, EMBO conference catalytic mechanism by biological systems, 7-10 October 2012, page 45.
    • (2012) , pp. 45
    • Kellis, J.1    Estell, D.2    Cascão-Pereira, L.3
  • 19
    • 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
    • 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 Degradation Stab 97:771-775.
    • (2012) Polym Degradation Stab , vol.97 , pp. 771-775
    • Kitadokoro, K.1    Thumarat, U.2    Nakamura, R.3    Nishimura, K.4    Karatani, H.5    Suzuki, H.6    Kawai, F.7
  • 20
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G. 2004. Making optimal use of empirical energy functions: Force-field parameterization in crystal space. Proteins 57:678-683.
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 21
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA - a self-parameterizing force field
    • Krieger E, Koraimann G, Vriend G. 2002. Increasing the precision of comparative models with YASARA NOVA - a self-parameterizing force field. Proteins 47:393-402.
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 22
    • 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. 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 2:361-364.
    • (2007) Biotechnol J , vol.2 , pp. 361-364
    • Nimchua, T.1    Punnapayak, H.2    Zimmermann, W.3
  • 23
    • 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, Foellner 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 146:100-104.
    • (2010) J Biotechnol , vol.146 , pp. 100-104
    • Oeser, T.1    Wei, R.2    Baumgarten, T.3    Billig, S.4    Foellner, C.5    Zimmermann, W.6
  • 27
    • 84857624986 scopus 로고    scopus 로고
    • In vitro evaluation of the antimicrobial efficacy of a new silver-triclosan vs a silver collagen-coated polyester vascular graft against methicillin-resistant Staphylococcus aureus
    • Ricco J, Assadin A, Schneider F, Assadian O. 2012. In vitro evaluation of the antimicrobial efficacy of a new silver-triclosan vs a silver collagen-coated polyester vascular graft against methicillin-resistant Staphylococcus aureus. J Vasc Surg 55:823-829.
    • (2012) J Vasc Surg , vol.55 , pp. 823-829
    • Ricco, J.1    Assadin, A.2    Schneider, F.3    Assadian, O.4
  • 29
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner MF, Olson AJ, Spehner JC. 1996. Reduced surface: An efficient way to compute molecular surfaces. Biopolymers 38:305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 30
    • 84940256953 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version~1.41.
    • Schrödinger L. 2011. The PyMOL Molecular Graphics System, Version~1.41.
    • (2011)
    • Schrödinger, L.1
  • 34
    • 13144279300 scopus 로고    scopus 로고
    • Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 Å resolution
    • Wei Y, Swenson L, Castro C, Derewenda U, Minor W, Arai H, Aoki J, Inoue K, Servin-Gonzalez L, Derewenda ZS. 1998. Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 Å resolution. Structure 6:511-519.
    • (1998) Structure , vol.6 , pp. 511-519
    • Wei, Y.1    Swenson, L.2    Castro, C.3    Derewenda, U.4    Minor, W.5    Arai, H.6    Aoki, J.7    Inoue, K.8    Servin-Gonzalez, L.9    Derewenda, Z.S.10
  • 35
    • 56849095946 scopus 로고
    • Surface modification of polyester by alkaline treatments
    • Zeronian SH, Collins MJ. 1989. Surface modification of polyester by alkaline treatments. Textile Prog 20:1-34.
    • (1989) Textile Prog , vol.20 , pp. 1-34
    • Zeronian, S.H.1    Collins, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.