메뉴 건너뛰기




Volumn 95, Issue 8, 2010, Pages 1370-1374

Y443F mutation in the substrate-binding domain of extracellular PHB depolymerase enhances its PHB adsorption and disruption abilities

Author keywords

Adsorption; Amino acid substitution; Disruption; PHB depolymerase; poly (R) 3 hydroxybutyrate (PHB); Substrate binding domain (SBD)

Indexed keywords

AMINO ACID SUBSTITUTION; DEPOLYMERASE; POLY--3-HYDROXYBUTYRATE; POLY[(R)-3-HYDROXYBUTYRATE] (PHB); SUBSTRATE-BINDING DOMAINS;

EID: 77955307969     PISSN: 01413910     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.polymdegradstab.2010.01.022     Document Type: Conference Paper
Times cited : (19)

References (30)
  • 2
    • 0037008507 scopus 로고    scopus 로고
    • Biodegradable polymers for the environment
    • R.A. Gross, and B. Kalra Biodegradable polymers for the environment Science 297 2002 803 807
    • (2002) Science , vol.297 , pp. 803-807
    • Gross, R.A.1    Kalra, B.2
  • 3
    • 0036406855 scopus 로고    scopus 로고
    • Microbial degradation of polyhydroxyalkanoates
    • D. Jendrossek, and R. Handrick Microbial degradation of polyhydroxyalkanoates Annu Rev Microbiol 56 2002 403 432
    • (2002) Annu Rev Microbiol , vol.56 , pp. 403-432
    • Jendrossek, D.1    Handrick, R.2
  • 5
    • 0038521067 scopus 로고    scopus 로고
    • Biodegradation of microbial and synthetic polyesters by fungi
    • D.Y. Kim, and Y.H. Rhee Biodegradation of microbial and synthetic polyesters by fungi Appl Microbiol Biotechnol 61 2003 300 308
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 300-308
    • Kim, D.Y.1    Rhee, Y.H.2
  • 6
    • 70149091692 scopus 로고    scopus 로고
    • Enzyme-catalyzed synthesis and degradation of biopolymers
    • T. Hiraishi, and S. Taguchi Enzyme-catalyzed synthesis and degradation of biopolymers Mini-Rev Org Chem 6 2009 44 54
    • (2009) Mini-Rev Org Chem , vol.6 , pp. 44-54
    • Hiraishi, T.1    Taguchi, S.2
  • 7
    • 3342970514 scopus 로고    scopus 로고
    • Biodegradation of poly(l-lactide)
    • Y. Tokiwa, and A. Jarerat Biodegradation of poly(l-lactide) Biotechnol Lett 26 2004 771 777
    • (2004) Biotechnol Lett , vol.26 , pp. 771-777
    • Tokiwa, Y.1    Jarerat, A.2
  • 8
    • 0344430075 scopus 로고    scopus 로고
    • Control of racemization for feedstock recycling of PLLA
    • Y. Fan, H. Nishida, Y. Shirai, and T. Endo Control of racemization for feedstock recycling of PLLA Green Chem 5 2003 575 579
    • (2003) Green Chem , vol.5 , pp. 575-579
    • Fan, Y.1    Nishida, H.2    Shirai, Y.3    Endo, T.4
  • 9
    • 33746316821 scopus 로고    scopus 로고
    • Thermal degradation of environmentally degradable poly(hydroxyalkanoic acid)s
    • H. Abe Thermal degradation of environmentally degradable poly(hydroxyalkanoic acid)s Macromol Biosci 6 2006 469 486
    • (2006) Macromol Biosci , vol.6 , pp. 469-486
    • Abe, H.1
  • 10
    • 0026837512 scopus 로고
    • Anionic polymerization of β-lactones initiated with alkali-metal alkoxides: Reinvestigation of the polymerization mechanism
    • P. Kurcok, M. Kowalczuk, K. Hennek, and Z. Jedlinski Anionic polymerization of β-lactones initiated with alkali-metal alkoxides: reinvestigation of the polymerization mechanism Macromolecules 25 1992 2017 2020
    • (1992) Macromolecules , vol.25 , pp. 2017-2020
    • Kurcok, P.1    Kowalczuk, M.2    Hennek, K.3    Jedlinski, Z.4
  • 11
    • 14644392804 scopus 로고    scopus 로고
    • Hydrolytic degradation of poly[(R)-3-hydroxybutyric acid] in the melt
    • DOI 10.1016/j.polymer.2005.01.030, PII S0032386105000716
    • T. Saeki, T. Tsukegi, H. Tsuji, H. Daimon, and K. Fujie Hydrolytic degradation of poly[(R)-3-hydroxybutyric acid] in the melt Polymer 46 2005 2157 2162 (Pubitemid 40320456)
    • (2005) Polymer , vol.46 , Issue.7 , pp. 2157-2162
    • Saeki, T.1    Tsukegi, T.2    Tsuji, H.3    Daimon, H.4    Fujie, K.5
  • 12
    • 0032731656 scopus 로고    scopus 로고
    • Biocatalysis for industrial production of fine chemicals
    • B. Schulze, and M.G. Wubbolts Biocatalysis for industrial production of fine chemicals Curr Opin Biotechnol 10 1999 609 615
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 609-615
    • Schulze, B.1    Wubbolts, M.G.2
  • 13
    • 41549114161 scopus 로고    scopus 로고
    • Recent applications of biocatalysis in developing green chemistry for chemical synthesis at the industrial scale
    • N. Ran, L. Zhao, Z. Chen, and J. Tao Recent applications of biocatalysis in developing green chemistry for chemical synthesis at the industrial scale Green Chem 10 2008 361 372
    • (2008) Green Chem , vol.10 , pp. 361-372
    • Ran, N.1    Zhao, L.2    Chen, Z.3    Tao, J.4
  • 14
    • 29444446408 scopus 로고    scopus 로고
    • Interaction between poly[(R)-3-hydroxybutyrate] depolymerase and biodegradable polyesters evaluated by atomic force microscopy
    • M. Fujita, Y. Kobori, Y. Aoki, N. Matsumoto, H. Abe, and Y. Doi Interaction between poly[(R)-3-hydroxybutyrate] depolymerase and biodegradable polyesters evaluated by atomic force microscopy Langmuir 21 2005 11829 11835
    • (2005) Langmuir , vol.21 , pp. 11829-11835
    • Fujita, M.1    Kobori, Y.2    Aoki, Y.3    Matsumoto, N.4    Abe, H.5    Doi, Y.6
  • 15
    • 57049136085 scopus 로고    scopus 로고
    • Adsorption characteristics of P(3HB) depolymerase as evaluated by surface plasmon resonance and atomic force microscopy
    • N. Matsumoto, M. Fujita, T. Hiraishi, H. Abe, and M. Maeda Adsorption characteristics of P(3HB) depolymerase as evaluated by surface plasmon resonance and atomic force microscopy Biomacromolecules 9 2008 3201 3207
    • (2008) Biomacromolecules , vol.9 , pp. 3201-3207
    • Matsumoto, N.1    Fujita, M.2    Hiraishi, T.3    Abe, H.4    Maeda, M.5
  • 16
    • 33750990228 scopus 로고    scopus 로고
    • Effects of mutations in the substrate-binding domain of poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation
    • DOI 10.1128/AEM.01187-06
    • T. Hiraishi, Y. Hirahara, Y. Doi, M. Maeda, and S. Taguchi Effects of mutations in the substrate-binding domain of poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation Appl Environ Microbiol 72 2006 7331 7338 (Pubitemid 44748450)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.11 , pp. 7331-7338
    • Hiraishi, T.1    Hirahara, Y.2    Doi, Y.3    Maeda, M.4    Taguchi, S.5
  • 17
    • 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
    • T. Hiraishi, N. Komiya, N. Matsumoto, H. Abe, M. Fujita, and M. Maeda Degradation and adsorption characteristics of PHB depolymerase as revealed by kinetics of mutant enzymes with amino acid substitution in substrate-binding domain Biomacromolecules 11 2010 113 119
    • (2010) Biomacromolecules , vol.11 , pp. 113-119
    • Hiraishi, T.1    Komiya, N.2    Matsumoto, N.3    Abe, H.4    Fujita, M.5    Maeda, M.6
  • 18
    • 0032098584 scopus 로고    scopus 로고
    • Simple kinetic model for the heterogeneous enzymatic hydrolysis of natural poly(3-hydroxybutyrate)
    • M. Scandola, M.L. Focarete, and G. Frisoni Simple kinetic model for the heterogeneous enzymatic hydrolysis of natural poly(3-hydroxybutyrate) Macromolecules 31 1998 3846 3851
    • (1998) Macromolecules , vol.31 , pp. 3846-3851
    • Scandola, M.1    Focarete, M.L.2    Frisoni, G.3
  • 19
    • 0032510716 scopus 로고    scopus 로고
    • Interfacial activation of triglyceride lipase from Thermomyces (Humicola) lanuginosa: Kinetic parameters and a basis for control of the lid
    • O.G. Berg, Y. Cajal, G.L. Butterfoss, R.L. Grey, M.A. Alsina, and B.-Z. Yu Interfacial activation of triglyceride lipase from Thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid Biochemistry 37 1998 6615 6627
    • (1998) Biochemistry , vol.37 , pp. 6615-6627
    • Berg, O.G.1    Cajal, Y.2    Butterfoss, G.L.3    Grey, R.L.4    Alsina, M.A.5    Yu, B.-Z.6
  • 20
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: A protein structure and structural feature prediction server
    • J. Cheng, A.Z. Randall, M.J. Sweredoski, and P. Baldi SCRATCH: a protein structure and structural feature prediction server Nucleic Acids Res 33 2005 W72 W76
    • (2005) Nucleic Acids Res , vol.33
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of protein J Mol Biol 157 1982 105 132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • P.Y. Chou, and G.D. Fasman Prediction of the secondary structure of proteins from their amino acid sequence Adv Enzymol 47 1978 45 147
    • (1978) Adv Enzymol , vol.47 , pp. 45-147
    • Chou, P.Y.1    Fasman, G.D.2
  • 23
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0027438347 scopus 로고
    • Kinetics and mechanism of heterogeneous hydrolysis of poly[(R)-3-hydroxybutyrate] film by PHA depolymerases
    • K. Mukai, K. Yamada, and Y. Doi Kinetics and mechanism of heterogeneous hydrolysis of poly[(R)-3-hydroxybutyrate] film by PHA depolymerases Int J Biol Macromol 15 1993 361 366
    • (1993) Int J Biol Macromol , vol.15 , pp. 361-366
    • Mukai, K.1    Yamada, K.2    Doi, Y.3
  • 27
    • 33745161547 scopus 로고    scopus 로고
    • Carbohydrate binding modules: Biochemical properties and novel applications
    • O. Shoseyov, Z. Shani, and I. Levy Carbohydrate binding modules: biochemical properties and novel applications Microbiol Mol Biol Rev 70 2006 283 295
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 283-295
    • Shoseyov, O.1    Shani, Z.2    Levy, I.3
  • 28
    • 0036193920 scopus 로고    scopus 로고
    • Nonhydrolytic fragmentation of a poly[(R)-3-hydroxybutyrate] single crystal revealed by use of a mutant of polyhydroxybutyrate depolymerase
    • T. Murase, Y. Suzuki, Y. Doi, and T. Iwata Nonhydrolytic fragmentation of a poly[(R)-3-hydroxybutyrate] single crystal revealed by use of a mutant of polyhydroxybutyrate depolymerase Biomacromolecules 3 2002 312 317
    • (2002) Biomacromolecules , vol.3 , pp. 312-317
    • Murase, T.1    Suzuki, Y.2    Doi, Y.3    Iwata, T.4
  • 29
    • 5044233606 scopus 로고    scopus 로고
    • Direct observation of poly(3-hydroxybutyrate) depolymerase adsorbed on polyester thin film by atomic force microscopy
    • Y. Kikkawa, M. Fujita, T. Hiraishi, M. Yoshimoto, and Y. Doi Direct observation of poly(3-hydroxybutyrate) depolymerase adsorbed on polyester thin film by atomic force microscopy Biomacromolecules 5 2004 1642 1646
    • (2004) Biomacromolecules , vol.5 , pp. 1642-1646
    • Kikkawa, Y.1    Fujita, M.2    Hiraishi, T.3    Yoshimoto, M.4    Doi, Y.5
  • 30
    • 22944450656 scopus 로고    scopus 로고
    • Dynamic adsorption behavior of poly(3-hydroxybutyrate) depolymerase onto polyester surface investigated by QCM and AFM
    • Y. Kikkawa, K. Yamashita, T. Hiraishi, M. Kanesato, and Y. Doi Dynamic adsorption behavior of poly(3-hydroxybutyrate) depolymerase onto polyester surface investigated by QCM and AFM Biomacromolecules 6 2005 2084 2090
    • (2005) Biomacromolecules , vol.6 , pp. 2084-2090
    • Kikkawa, Y.1    Yamashita, K.2    Hiraishi, T.3    Kanesato, M.4    Doi, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.