메뉴 건너뛰기




Volumn 14, Issue 6, 2013, Pages 1769-1776

Fusion of binding domains to Thermobifida cellulosilytica cutinase to tune sorption characteristics and enhancing PET hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ALCALIGENES FAECALIS; CATALYTIC EFFICIENCIES; CRYSTAL MICROBALANCE; ENHANCED ADSORPTIONS; HORSERADISH PEROXIDASE; POLY-HYDROXYALKANOATE; POLYETHYLENE TEREPHTHALATES (PET); SORPTION CHARACTERISTICS;

EID: 84878820905     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm400140u     Document Type: Article
Times cited : (149)

References (66)
  • 2
    • 67651095678 scopus 로고    scopus 로고
    • Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate)
    • Ronkvist, Å. 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, Å.M.1    Xie, W.2    Lu, W.3    Gross, R.A.4
  • 4
    • 77955515872 scopus 로고    scopus 로고
    • Surface structure and properties of poly-(ethylene terephthalate) hydrolyzed by alkali and cutinase
    • Donelli, I.; Freddi, G.; Nierstrasz, V. A.; Taddei, P. Surface structure and properties of poly-(ethylene terephthalate) hydrolyzed by alkali and cutinase Polym. Degrad. Stab. 2010, 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
  • 5
    • 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. 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    Foellner, C.5    Zimmermann, W.6
  • 6
    • 34247340001 scopus 로고    scopus 로고
    • Effect of the agitation on the adsorption and hydrolytic efficiency of cutinases on polyethylene terephthalate fibres
    • O'Neill, A.; Araújo, R.; Casal, M.; Guebitz, G. M.; Cavaco-Paulo, A. Effect of the agitation on the adsorption and hydrolytic efficiency of cutinases on polyethylene terephthalate fibres Enzyme Microb. Technol. 2007, 7, 1801-1805
    • (2007) Enzyme Microb. Technol. , vol.7 , pp. 1801-1805
    • O'Neill, A.1    Araújo, R.2    Casal, M.3    Guebitz, G.M.4    Cavaco-Paulo, A.5
  • 10
    • 84878871675 scopus 로고    scopus 로고
    • U.S. Patent 20050261465.
    • Nagarajan, V. U.S. Patent 20050261465, 2005.
    • (2005)
    • Nagarajan, V.1
  • 14
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A. B.; Bolam, D. N.; Gilbert, H. J.; Davies, G. J. Carbohydrate-binding modules: fine-tuning polysaccharide recognition Biochem. J. 2004, 382, 769-781
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 15
    • 0142134866 scopus 로고    scopus 로고
    • Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27
    • Boraston, A. B.; Revett, T. J.; Boraston, C. M.; Nurizzo, D.; Davies, G. J. Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27 Structure 2003, 11, 665-675
    • (2003) Structure , vol.11 , pp. 665-675
    • Boraston, A.B.1    Revett, T.J.2    Boraston, C.M.3    Nurizzo, D.4    Davies, G.J.5
  • 19
    • 0031599344 scopus 로고    scopus 로고
    • Microbial degradation of polyesters: A review on extracellular poly(hydroxyalkanoic acid) depolymerases
    • Jendrossek, D. Microbial degradation of polyesters: a review on extracellular poly(hydroxyalkanoic acid) depolymerases Polym. Degrad. Stab. 1998, 59, 317-325
    • (1998) Polym. Degrad. Stab. , vol.59 , pp. 317-325
    • Jendrossek, D.1
  • 20
    • 0033066633 scopus 로고    scopus 로고
    • Subtrate and binding specifities of bacterial polyhydroxybutyrate depolymerase
    • Kasuya, K.; Ohura, T.; Masuda, K.; Doi, Y. Subtrate and binding specifities of bacterial polyhydroxybutyrate depolymerase Int. J. Biol. Macromol. 1999, 24, 329-336
    • (1999) Int. J. Biol. Macromol. , vol.24 , pp. 329-336
    • Kasuya, K.1    Ohura, T.2    Masuda, K.3    Doi, Y.4
  • 21
    • 0034279048 scopus 로고    scopus 로고
    • Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri
    • Hiraishi, T.; Ohura, T.; Ito, S.; Kasuya, K.; Doi, Y. Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri Biomacromolecules 2000, 1, 320-324
    • (2000) Biomacromolecules , vol.1 , pp. 320-324
    • Hiraishi, T.1    Ohura, T.2    Ito, S.3    Kasuya, K.4    Doi, Y.5
  • 25
    • 0026349480 scopus 로고
    • Nonhydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase
    • Din, N.; Gilkes, N. R.; Tekant, B.; Miller, R. C.; Warren, R. A.; Kilburn, D. G. Nonhydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase Biotechnology 1991, 9, 1096-1098
    • (1991) Biotechnology , vol.9 , pp. 1096-1098
    • Din, N.1    Gilkes, N.R.2    Tekant, B.3    Miller, R.C.4    Warren, R.A.5    Kilburn, D.G.6
  • 26
    • 0036193920 scopus 로고    scopus 로고
    • Nonhydrolytic fragmentation of a poly[(R)-3-hydroxybutyrate] single crystal revealed by use of a mutant of polyhydroxybutyrate depolymerase
    • Murase, T.; Suzuki, Y.; Doi, Y.; Iwata, T. Nonhydrolytic fragmentation of a poly[(R)-3-hydroxybutyrate] single crystal revealed by use of a mutant of polyhydroxybutyrate depolymerase Biomacromolecules 2002, 3, 312-317
    • (2002) Biomacromolecules , vol.3 , pp. 312-317
    • Murase, T.1    Suzuki, Y.2    Doi, Y.3    Iwata, T.4
  • 27
    • 65249122405 scopus 로고    scopus 로고
    • Engineering of a multifunctional hemicellulase
    • Fan, Z.; Werkman, J. R.; Yuan, L. Engineering of a multifunctional hemicellulase Biotechnol. Lett. 2009, 31, 751-757
    • (2009) Biotechnol. Lett. , vol.31 , pp. 751-757
    • Fan, Z.1    Werkman, J.R.2    Yuan, L.3
  • 28
    • 0346035834 scopus 로고    scopus 로고
    • A cellulose-binding module of the Trichoderma reesei β-mannanase Man5A increases the mannan-hydrolysis of complex substrates
    • Hägglund, P.; Eriksson, T.; Collén, A.; Nerinckx, W.; Claeyssens, M.; StaÌŠlbrand, H. A cellulose-binding module of the Trichoderma reesei β-mannanase Man5A increases the mannan-hydrolysis of complex substrates J. Biotechnol. 2003, 101, 37-48
    • (2003) J. Biotechnol. , vol.101 , pp. 37-48
    • Hägglund, P.1    Eriksson, T.2    Collén, A.3    Nerinckx, W.4    Claeyssens, M.5    Staìšlbrand, H.6
  • 29
    • 77958535213 scopus 로고    scopus 로고
    • Characterization of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins and their potential application in bioscouring
    • Zhang, Y.; Chen, S.; Xu, M.; Cavaco-Paulo, A.; Wu, J.; Chen, J. Characterization of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins and their potential application in bioscouring Appl. Environ. Microbiol. 2010, 76, 6870-6876
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 6870-6876
    • Zhang, Y.1    Chen, S.2    Xu, M.3    Cavaco-Paulo, A.4    Wu, J.5    Chen, J.6
  • 30
    • 0029144923 scopus 로고
    • Effects of pH and high ionic strength on the adsorption and activity of native and mutated cellobiohydrolase i from Trichoderma reesei
    • Reinikainen, T.; Teleman, O.; Teeri, T. T. Effects of pH and high ionic strength on the adsorption and activity of native and mutated cellobiohydrolase I from Trichoderma reesei Proteins 1995, 22, 392-403
    • (1995) Proteins , vol.22 , pp. 392-403
    • Reinikainen, T.1    Teleman, O.2    Teeri, T.T.3
  • 31
    • 0028364450 scopus 로고
    • The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: Evidence for the involvement of tryptophan residues in binding
    • Din, N.; Forsythe, I. J.; Burtnik, L. D.; Gilkes, N. R.; Millers, R. C. J.; Warren, R. A. J.; Kilburn, D. G. The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding Mol. Microbiol. 1994, 11, 747-755
    • (1994) Mol. Microbiol. , vol.11 , pp. 747-755
    • Din, N.1    Forsythe, I.J.2    Burtnik, L.D.3    Gilkes, N.R.4    Millers, R.C.J.5    Warren, R.A.J.6    Kilburn, D.G.7
  • 32
    • 0031944928 scopus 로고    scopus 로고
    • The adsorption of substrate-binding domain of PHB depolymerases to the surface of poly(3-hydroxybutyric acid)
    • Shinomiya, M.; Iwata, T.; Doi, Y. The adsorption of substrate-binding domain of PHB depolymerases to the surface of poly(3-hydroxybutyric acid) Int. J. Biol. Macromol. 1998, 22, 129-135
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 129-135
    • Shinomiya, M.1    Iwata, T.2    Doi, Y.3
  • 35
  • 39
    • 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, Z. S. Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 Å resolution Structure 1998, 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
  • 41
    • 77950673061 scopus 로고    scopus 로고
    • Practically useful: What the Rosetta protein modeling suite can do for you
    • Kaufmann, K. W.; Lemmon, G. H.; Deluca, S. L.; Sheehan, J. H.; Meiler, J. Practically useful: What the Rosetta protein modeling suite can do for you Biochemistry 2010, 49, 2987-2998
    • (2010) Biochemistry , vol.49 , pp. 2987-2998
    • Kaufmann, K.W.1    Lemmon, G.H.2    Deluca, S.L.3    Sheehan, J.H.4    Meiler, J.5
  • 42
    • 46249092554 scopus 로고    scopus 로고
    • GRGMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B.; Kutzner, C.; Van Der Spoel, D.; Lindahl, E. GRGMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 46
    • 0035220212 scopus 로고    scopus 로고
    • Microbial Degradation of Polyesters
    • In; Babel, W. Steinbüchel, A. Springer: Berlin/Heidelberg, Vol.
    • Jendrossek, D. Microbial Degradation of Polyesters. In Biopolyesters; Babel, W.; Steinbüchel, A., Eds.; Springer: Berlin/Heidelberg, 2001; Vol. 71, pp 293-325.
    • (2001) Biopolyesters , vol.71 , pp. 293-325
    • Jendrossek, D.1
  • 48
    • 0034894206 scopus 로고    scopus 로고
    • Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes faecalis T1 by using a quartz crystal microbalance
    • Yamashita, K.; Aoyagi, Y.; Abe, H.; Doi, Y. Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes faecalis T1 by using a quartz crystal microbalance Biomacromolecules 2001, 2, 25-28
    • (2001) Biomacromolecules , vol.2 , pp. 25-28
    • Yamashita, K.1    Aoyagi, Y.2    Abe, H.3    Doi, Y.4
  • 49
    • 77958535213 scopus 로고    scopus 로고
    • Characterization of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins and their potential application in bioscouring
    • Zhang, Y.; Chen, S.; Xu, M.; Cavaco-Paulo, A.; Wu, J.; Chen, J. Characterization of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins and their potential application in bioscouring Appl. Environ. Microbiol. 2010, 76, 6870-6876
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 6870-6876
    • Zhang, Y.1    Chen, S.2    Xu, M.3    Cavaco-Paulo, A.4    Wu, J.5    Chen, J.6
  • 50
    • 0346035834 scopus 로고    scopus 로고
    • A cellulose-binding module of the Trichoderma reesei [β]-mannanase Man5A increases the mannan-hydrolysis of complex substrates
    • Hägglund, P.; Eriksson, T.; Colln, A.; Nerinckx, W.; Claeyssens, M.; Stlbrand, H. A cellulose-binding module of the Trichoderma reesei [β]-mannanase Man5A increases the mannan-hydrolysis of complex substrates J. Biotechnol. 2003, 101, 37-48
    • (2003) J. Biotechnol. , vol.101 , pp. 37-48
    • Hägglund, P.1    Eriksson, T.2    Colln, A.3    Nerinckx, W.4    Claeyssens, M.5    Stlbrand, H.6
  • 51
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe, T.; Ito, Y.; Yamada, T.; Hashimoto, M.; Sekine, S.; Tanaka, H. The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation J. Bacteriol. 1994, 176, 4465-4472
    • (1994) J. Bacteriol. , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 52
    • 0028925347 scopus 로고
    • Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytically processed form
    • Blaak, H.; Schrempf, H. Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytically processed form Eur. J. Biochem. 1995, 229, 132-139
    • (1995) Eur. J. Biochem. , vol.229 , pp. 132-139
    • Blaak, H.1    Schrempf, H.2
  • 54
    • 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. 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    Brueckner, T.3    Araújo, R.4    Cavaco-Paulo, A.5    Kaufmann, F.6
  • 56
    • 0037226350 scopus 로고    scopus 로고
    • Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: Importance of the CBM to cellulose hydrolysis
    • Arai, T.; Araki, R.; Tanaka, A.; Karita, S.; Kimura, T.; Sakka, K.; Ohmiya, K. Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: Importance of the CBM to cellulose hydrolysis J. Bacteriol. 2003, 185, 504-512
    • (2003) J. Bacteriol. , vol.185 , pp. 504-512
    • Arai, T.1    Araki, R.2    Tanaka, A.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmiya, K.7
  • 57
    • 0035667422 scopus 로고    scopus 로고
    • Sequence of CelQ and properties of CelQ, a component of the Clostridium thermocellum cellulosome
    • Arai, T.; Ohara, H.; Karita, S.; Kimura, T.; Sakka, K.; Ohmiya, K. Sequence of CelQ and properties of CelQ, a component of the Clostridium thermocellum cellulosome Appl. Microbiol. Biotechnol. 2001, 57, 660-666
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 660-666
    • Arai, T.1    Ohara, H.2    Karita, S.3    Kimura, T.4    Sakka, K.5    Ohmiya, K.6
  • 58
    • 0030700658 scopus 로고    scopus 로고
    • CelG from Clostridium cellulolyticum: A multidomain endoglucanase acting efficiently on crystalline cellulose
    • Gal, L.; Gaudin, C.; Belaich, A.; Pages, S.; Tardif, C.; Belaich, J. P. CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose J. Bacteriol. 1997, 179, 6595-6601
    • (1997) J. Bacteriol. , vol.179 , pp. 6595-6601
    • Gal, L.1    Gaudin, C.2    Belaich, A.3    Pages, S.4    Tardif, C.5    Belaich, J.P.6
  • 59
    • 73949098418 scopus 로고    scopus 로고
    • Degradation and adsorption characteristics of PHB depolymerase as revealed by kinetics of mutant enzymes with amino acid substitution in substrate-binding domain
    • Hiraishi, T.; Komiya, N.; Matsumoto, N.; Abe, H.; Fujita, M.; Maeda, M. Degradation and adsorption characteristics of PHB depolymerase as revealed by kinetics of mutant enzymes with amino acid substitution in substrate-binding domain Biomacromolecules 2009, 11, 113-119
    • (2009) Biomacromolecules , vol.11 , pp. 113-119
    • Hiraishi, T.1    Komiya, N.2    Matsumoto, N.3    Abe, H.4    Fujita, M.5    Maeda, M.6
  • 60
    • 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.; Araujo, R.; Cavaco-Paulo, A.; Kaufmann, F.; Kroutil, W.; Guebitz, G. M. 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    Brueckner, T.3    Araujo, R.4    Cavaco-Paulo, A.5    Kaufmann, F.6    Kroutil, W.7    Guebitz, G.M.8
  • 61
    • 22944450656 scopus 로고    scopus 로고
    • Dynamic adsorption behavior of poly(3-hydroxybutyrate) depolymerase onto polyester surface investigated by QCM and AFM
    • Kikkawa, Y.; Yamashita, K.; Hiraishi, T.; Kanesato, M.; Doi, Y. Dynamic adsorption behavior of poly(3-hydroxybutyrate) depolymerase onto polyester surface investigated by QCM and AFM Biomacromolecules 2005, 6, 2084-2090
    • (2005) Biomacromolecules , vol.6 , pp. 2084-2090
    • Kikkawa, Y.1    Yamashita, K.2    Hiraishi, T.3    Kanesato, M.4    Doi, Y.5
  • 62
    • 16344392699 scopus 로고    scopus 로고
    • Enzymatic degradation of poly(l-lactide)film by proteinase K: Quartz crystal microbalance and atomic force microscopy study
    • Yamashita, K.; Kikkawa, Y.; Kurokawa, K.; Doi, Y. Enzymatic degradation of poly(l-lactide)film by proteinase K: quartz crystal microbalance and atomic force microscopy study Biomacromolecules 2005, 6, 850-857
    • (2005) Biomacromolecules , vol.6 , pp. 850-857
    • Yamashita, K.1    Kikkawa, Y.2    Kurokawa, K.3    Doi, Y.4
  • 63
    • 42449094181 scopus 로고    scopus 로고
    • Enzymatic kinetics of cellulose hydrolysis: A QCM-D study
    • Turon, X.; Rojas, O. J.; Deinhammer, R. S. Enzymatic kinetics of cellulose hydrolysis: a QCM-D study Langmuir 2008, 24, 3880-3887
    • (2008) Langmuir , vol.24 , pp. 3880-3887
    • Turon, X.1    Rojas, O.J.2    Deinhammer, R.S.3
  • 64
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • Nakanishi, K.; Sakiyama, T.; Imamura, K. On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon J. Biosci. Bioeng. 2001, 91, 233-244
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 65
    • 77949540160 scopus 로고    scopus 로고
    • Biochemical characterization of the cutinases from Thermobifida fusca
    • Chen, S.; Su, L.; Billig, S.; Zimmermann, W.; Chen, J.; Wu, J. Biochemical characterization of the cutinases from Thermobifida fusca J. Mol. Catal., B 2010, 63, 121-127
    • (2010) J. Mol. Catal., B , vol.63 , pp. 121-127
    • Chen, S.1    Su, L.2    Billig, S.3    Zimmermann, W.4    Chen, J.5    Wu, J.6
  • 66
    • 0042388630 scopus 로고    scopus 로고
    • Reduced mouse fibroblast cell growth by increased hydrophilicity of microbial polyhydroxyalkanoates via hyaluronan coating
    • Wang, Y. -.; Wu, Q.; Chen, G. -. Reduced mouse fibroblast cell growth by increased hydrophilicity of microbial polyhydroxyalkanoates via hyaluronan coating Biomaterials 2003, 24, 4621-4629
    • (2003) Biomaterials , vol.24 , pp. 4621
    • Wang, Y.1    Wu, Q.2    Chen, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.