메뉴 건너뛰기




Volumn 75, Issue 5, 2007, Pages 1071-1078

A Paenibacillus sp. dextranase mutant pool with improved thermostability and activity

Author keywords

Activity; Dextranase; Directed evolution; Paenibacillus sp.; Random mutagenesis; Thermostability

Indexed keywords

GENES; MUTAGENESIS; NUCLEOTIDES; THERMODYNAMIC STABILITY;

EID: 34250668434     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-0936-6     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 13844250741 scopus 로고    scopus 로고
    • High-throughput screens and selections of enzyme-encoding genes
    • Aharoni A, Griffiths AD, Tawfik DS (2005) High-throughput screens and selections of enzyme-encoding genes. Curr Opin Chem Biol 9:210-216
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 210-216
    • Aharoni, A.1    Griffiths, A.D.2    Tawfik, D.S.3
  • 2
    • 0035546157 scopus 로고    scopus 로고
    • Gene expression and molecular evolution
    • Akashi H (2001) Gene expression and molecular evolution. Curr Opin Genet Dev 11:660-666
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 660-666
    • Akashi, H.1
  • 4
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell RC, Joyce GF (1992) Randomization of genes by PCR mutagenesis. PCR Methods Appl 2:28-33
    • (1992) PCR Methods Appl , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 5
    • 33747883505 scopus 로고    scopus 로고
    • Enhancement of peridontal tissue regeneration by locally controlled delivery of insulin-like growth factor-I from dextran-co-gelatin microspheres
    • Chen FM, Zhao YM, Wu H, Deng ZH, Wang QT, Zhou W, Liu Q, Dong GY, Li K, Wu ZF, Jin Y (2006) Enhancement of peridontal tissue regeneration by locally controlled delivery of insulin-like growth factor-I from dextran-co-gelatin microspheres. J Control Release 114:209-222
    • (2006) J Control Release , vol.114 , pp. 209-222
    • Chen, F.M.1    Zhao, Y.M.2    Wu, H.3    Deng, Z.H.4    Wang, Q.T.5    Zhou, W.6    Liu, Q.7    Dong, G.Y.8    Li, K.9    Wu, Z.F.10    Jin, Y.11
  • 6
    • 13844266718 scopus 로고    scopus 로고
    • Optimization of sugarcane factory application of commercial dextranases
    • Eggleston G, Monge A (2005) Optimization of sugarcane factory application of commercial dextranases. Process Biochem 40:1881-1894
    • (2005) Process Biochem , vol.40 , pp. 1881-1894
    • Eggleston, G.1    Monge, A.2
  • 9
    • 4444351859 scopus 로고    scopus 로고
    • Isolation and characterization of genes encoding thermoactive and thermostable dextranases from two thermotolerant soil bacteria
    • Finnegan PM, Brumbley SM, O'Shea MG, Nevalainen H, Bergquist PL (2004b) Isolation and characterization of genes encoding thermoactive and thermostable dextranases from two thermotolerant soil bacteria. Curr Microbiol 49:327-333
    • (2004) Curr Microbiol , vol.49 , pp. 327-333
    • Finnegan, P.M.1    Brumbley, S.M.2    O'Shea, M.G.3    Nevalainen, H.4    Bergquist, P.L.5
  • 11
    • 0036303387 scopus 로고    scopus 로고
    • Increasing the thermal stability of an oligomeric protein, beta-glucuronidase
    • Flores H, Ellington AD (2002) Increasing the thermal stability of an oligomeric protein, beta-glucuronidase. J Mol Biol 315:325-337
    • (2002) J Mol Biol , vol.315 , pp. 325-337
    • Flores, H.1    Ellington, A.D.2
  • 13
    • 3342945272 scopus 로고    scopus 로고
    • The influence of mutanase and dextranase on the production and structure of glucans synthesized by streptococcal glucosyltransferases
    • Hayacibara MF, Koo H, Vacca Smith AM, Kopec LK, Scott-Anne K, Cury JA, Bowen WH (2004) The influence of mutanase and dextranase on the production and structure of glucans synthesized by streptococcal glucosyltransferases. Carbohydr Res 339:2127-2137
    • (2004) Carbohydr Res , vol.339 , pp. 2127-2137
    • Hayacibara, M.F.1    Koo, H.2    Vacca Smith, A.M.3    Kopec, L.K.4    Scott-Anne, K.5    Cury, J.A.6    Bowen, W.H.7
  • 14
    • 33645781503 scopus 로고    scopus 로고
    • Directed evolution strategies for improved enzymatic performance
    • DOI 10.1186/1475-2859-4-29
    • EG Hibbert PA Dalby 2005 Directed evolution strategies for improved enzymatic performance Microb Cell Fact 4 29 Hibbert EG, Dalby PA (2005) Directed evolution strategies for improved enzymatic performance. Microb Cell Fact 4:29. DOI 10.1186/1475-2859-4-29
    • (2005) Microb Cell Fact , vol.4 , pp. 29
    • Hibbert, E.G.1    Dalby, P.A.2
  • 16
    • 18044384442 scopus 로고    scopus 로고
    • 8-barrel enzymes
    • 8-barrel enzymes. Biomol Eng 22:31-38
    • (2005) Biomol Eng , vol.22 , pp. 31-38
    • Höcker, B.1
  • 18
    • 0004393194 scopus 로고
    • Enzymatic beakdown of dextran
    • Ingelman B (1948) Enzymatic beakdown of dextran. Acta Chem Scand 2:803-812
    • (1948) Acta Chem Scand , vol.2 , pp. 803-812
    • Ingelman, B.1
  • 19
    • 33744512606 scopus 로고    scopus 로고
    • Directed evolution of enzymes and biosynthetic pathways
    • Johannes TW, Zhao H (2006) Directed evolution of enzymes and biosynthetic pathways. Curr Opin Microbiol 9:261-267
    • (2006) Curr Opin Microbiol , vol.9 , pp. 261-267
    • Johannes, T.W.1    Zhao, H.2
  • 20
    • 20544444776 scopus 로고    scopus 로고
    • Microbial dextran-hydrolyzing enzymes: Fundamentals and applications
    • Khalikova E, Susi P, Korpela T (2005) Microbial dextran-hydrolyzing enzymes: fundamentals and applications. Microbiol Mol Biol Rev 69:306-325
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 306-325
    • Khalikova, E.1    Susi, P.2    Korpela, T.3
  • 22
    • 1842610093 scopus 로고    scopus 로고
    • Immobilization of dextransucrase and its use with soluble dextranase for glucooligosaccharides synthesis
    • Kubic C, Sikora B, Bielecki S (2004) Immobilization of dextransucrase and its use with soluble dextranase for glucooligosaccharides synthesis. Enzyme Microb Technol 34:555-560
    • (2004) Enzyme Microb Technol , vol.34 , pp. 555-560
    • Kubic, C.1    Sikora, B.2    Bielecki, S.3
  • 23
    • 27544466682 scopus 로고    scopus 로고
    • Use of directed evolution of mammalian cytochromes P450 for investigating the molecular basis of enzyme function and generating novel biocatalysts
    • Kumar S, Halpert JR (2005) Use of directed evolution of mammalian cytochromes P450 for investigating the molecular basis of enzyme function and generating novel biocatalysts. Biochem Biophys Res Commun 338:456-464
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 456-464
    • Kumar, S.1    Halpert, J.R.2
  • 24
    • 0042334876 scopus 로고    scopus 로고
    • Dextranase from Penicillium minioluteum: Reaction course, crystal structure, and product complex
    • Larsson AM, Andersson R, Ståhlberg J, Kenne L, Jones TA (2003) Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex. Structure 11:1111-1121
    • (2003) Structure , vol.11 , pp. 1111-1121
    • Larsson, A.M.1    Andersson, R.2    Ståhlberg, J.3    Kenne, L.4    Jones, T.A.5
  • 25
    • 0015333650 scopus 로고
    • A new reaction for colorimetric determination of carbohydrates
    • Lever M (1972) A new reaction for colorimetric determination of carbohydrates. Anal Biochem 47:273-279
    • (1972) Anal Biochem , vol.47 , pp. 273-279
    • Lever, M.1
  • 26
    • 0036737661 scopus 로고    scopus 로고
    • Degradation of dental plaque glucans and prevention of glucan formation using commercial enzymes
    • Marotta M, Martino A, De Rosa A, Farina E, Carteni M, De Rosa M (2002) Degradation of dental plaque glucans and prevention of glucan formation using commercial enzymes. Process Biochem 38:101-108
    • (2002) Process Biochem , vol.38 , pp. 101-108
    • Marotta, M.1    Martino, A.2    De Rosa, A.3    Farina, E.4    Carteni, M.5    De Rosa, M.6
  • 27
    • 0036038582 scopus 로고    scopus 로고
    • Analysis of a dextran-binding domain of the dextranase of Streptococcus mutans
    • Morisaki H, Igarashi T, Yamamoto A, Goto N (2002) Analysis of a dextran-binding domain of the dextranase of Streptococcus mutans. Lett Appl Microbiol 35:223-227
    • (2002) Lett Appl Microbiol , vol.35 , pp. 223-227
    • Morisaki, H.1    Igarashi, T.2    Yamamoto, A.3    Goto, N.4
  • 28
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • Morley KL, Kazlauskas RJ (2005) Improving enzyme properties: when are closer mutations better? Trends Biotechnol 23:231-237
    • (2005) Trends Biotechnol , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 29
    • 18044390504 scopus 로고    scopus 로고
    • Directed evolution: Selecting today's biocatalysts
    • Otten LG, Quax WJ (2005) Directed evolution: selecting today's biocatalysts. Biomol Eng 22:1-9
    • (2005) Biomol Eng , vol.22 , pp. 1-9
    • Otten, L.G.1    Quax, W.J.2
  • 30
    • 0023254924 scopus 로고
    • Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region
    • Schauder B, Blöcker H, Frank R, McCarthy JEG (1987) Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region. Gene 52:279-283
    • (1987) Gene , vol.52 , pp. 279-283
    • Schauder, B.1    Blöcker, H.2    Frank, R.3    McCarthy, J.E.G.4
  • 32
    • 0029869449 scopus 로고    scopus 로고
    • An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
    • Zaccolo M, Williams DM, Brown DM, Gherardi E (1996) An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues. J Mol Biol 255:589-603
    • (1996) J Mol Biol , vol.255 , pp. 589-603
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gherardi, E.4
  • 33
    • 0025988826 scopus 로고
    • Random mutagenesis of gene-sized DNA molecules by use of PCR with Taq DNA polymerase
    • Zhou YH, Zhang X, Ebright RH (1991) Random mutagenesis of gene-sized DNA molecules by use of PCR with Taq DNA polymerase. Nucleic Acids Res 19:6052
    • (1991) Nucleic Acids Res , vol.19 , pp. 6052
    • Zhou, Y.H.1    Zhang, X.2    Ebright, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.