메뉴 건너뛰기




Volumn 34, Issue 3, 2007, Pages 213-218

Introduction of a disulfide bridge enhances the thermostability of a Streptomyces olivaceoviridis xylanase mutant

Author keywords

Disulfide bridge; N terminus replacement; Synergistic effect; Thermostability; Xylanase

Indexed keywords

BACTERIAL ENZYME; DISULFIDE; RECOMBINANT ENZYME; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 33846885626     PISSN: 13675435     EISSN: 14765535     Source Type: Journal    
DOI: 10.1007/s10295-006-0188-y     Document Type: Article
Times cited : (39)

References (34)
  • 1
    • 0022321245 scopus 로고
    • Determination of sepharose-bound protein with coomassie brilliant blue G-250
    • Asryants RA, Duszenkova IV, Nagradova NK (1985) Determination of sepharose-bound protein with coomassie brilliant blue G-250. Anal Biochem 151:571-574
    • (1985) Anal Biochem , vol.151 , pp. 571-574
    • Asryants, R.A.1    Duszenkova, I.V.2    Nagradova, N.K.3
  • 2
    • 0028913985 scopus 로고
    • A modular xylanase containing a novel non-catalytic xylan-specific binding domain
    • Black GW, Hazlewood GP, Millward SJ, Laurie JI, Gilbert HJ (1995) A modular xylanase containing a novel non-catalytic xylan-specific binding domain. Biochem J 307:191-195
    • (1995) Biochem J , vol.307 , pp. 191-195
    • Black, G.W.1    Hazlewood, G.P.2    Millward, S.J.3    Laurie, J.I.4    Gilbert, H.J.5
  • 3
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T, Gerday C, Feller G (2005) Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 29:3-23
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 4
    • 0026833792 scopus 로고
    • Protein folding pathways determined using disulphide bonds
    • Creighton TE (1992) Protein folding pathways determined using disulphide bonds. Bioessays 14:195-199
    • (1992) Bioessays , vol.14 , pp. 195-199
    • Creighton, T.E.1
  • 5
    • 0842281285 scopus 로고    scopus 로고
    • A de novo designed N-terminal disulphide bridge stabilizes the Trichoderma reesei endo-1, 4-xylanase II
    • Fenel F, Leisola M, Janis J, Turunen O (2004) A de novo designed N-terminal disulphide bridge stabilizes the Trichoderma reesei endo-1, 4-xylanase II. J Biotechnol 108:137-143
    • (2004) J Biotechnol , vol.108 , pp. 137-143
    • Fenel, F.1    Leisola, M.2    Janis, J.3    Turunen, O.4
  • 6
    • 0343293808 scopus 로고    scopus 로고
    • An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: Structural basis and molecular study
    • Georis J, de Lemos Esteves F, Lamotte-Brasseur J, Bougnet V, Devreese B, Giannotta F, Granier B, Frere JM (2000) An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study. Protein Sci 9:466-475
    • (2000) Protein Sci , vol.9 , pp. 466-475
    • Georis, J.1    de Lemos Esteves, F.2    Lamotte-Brasseur, J.3    Bougnet, V.4    Devreese, B.5    Giannotta, F.6    Granier, B.7    Frere, J.M.8
  • 7
    • 33745498780 scopus 로고    scopus 로고
    • Glycosylation of proteins expressed in Pichia pastoris
    • Gu Y, Zhu XP, Wang SH (2004) Glycosylation of proteins expressed in Pichia pastoris. Chem Life 4:353-355
    • (2004) Chem Life , vol.4 , pp. 353-355
    • Gu, Y.1    Zhu, X.P.2    Wang, S.H.3
  • 8
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 9
    • 2942594230 scopus 로고    scopus 로고
    • Engineering the thermostability of Trichoderma reesei endo-1,4-xylanase II by combination of disulphide bridges
    • Hairong X, Fenel F, Matti L, Ossi T (2004) Engineering the thermostability of Trichoderma reesei endo-1,4-xylanase II by combination of disulphide bridges. Extremophiles 8:393-400
    • (2004) Extremophiles , vol.8 , pp. 393-400
    • Hairong, X.1    Fenel, F.2    Matti, L.3    Ossi, T.4
  • 10
    • 0344406096 scopus 로고    scopus 로고
    • Three-dimensional structures of thermophilic β-1, 4- xylanases from Chaetomium thermophilum and Nonomuraea flexuosa: Comparison of twelve xylanases in relation to their thermal stability
    • Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J (2003) Three-dimensional structures of thermophilic β-1, 4- xylanases from Chaetomium thermophilum and Nonomuraea flexuosa: comparison of twelve xylanases in relation to their thermal stability. Eur J Biochem 270:1399-1412
    • (2003) Eur J Biochem , vol.270 , pp. 1399-1412
    • Hakulinen, N.1    Turunen, O.2    Janis, J.3    Leisola, M.4    Rouvinen, J.5
  • 11
  • 12
    • 0028294637 scopus 로고
    • Characterization and sequence of a Thermomonospora fusca xylanase
    • Irwin D, Jung ED, Wilson DB (1994) Characterization and sequence of a Thermomonospora fusca xylanase. Appl Environ Microbiol 60: 763-770
    • (1994) Appl Environ Microbiol , vol.60 , pp. 763-770
    • Irwin, D.1    Jung, E.D.2    Wilson, D.B.3
  • 13
    • 0034695422 scopus 로고    scopus 로고
    • The tertiary structure at 1.59 Å resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti Bainier
    • Kumar PR, Eswaramoorthy S, Vithayathil PJ, Viswamitra MA (2000) The tertiary structure at 1.59 Å resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti Bainier. J Mol Biol 295: 581-593
    • (2000) J Mol Biol , vol.295 , pp. 581-593
    • Kumar, P.R.1    Eswaramoorthy, S.2    Vithayathil, P.J.3    Viswamitra, M.A.4
  • 14
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar S, Tsai CJ, Nussinov R (2000) Factors enhancing protein thermostability. Protein Eng 13:179-191
    • (2000) Protein Eng , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 15
    • 0035424955 scopus 로고    scopus 로고
    • Engineering proteins for thermostability: The use of sequence alignments versus rational design and directed evolution
    • Lehmann M, Wyss M (2001) Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution. Curr Opin Biotechnol 12:371-375
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 371-375
    • Lehmann, M.1    Wyss, M.2
  • 16
  • 17
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfold
    • Matthews BW, Nicholson H, Becktel WJ (1987) Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfold. Proc Natl Acad Sci USA 84:6663-6667
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 18
    • 33744515651 scopus 로고    scopus 로고
    • Thermal stabilization of Bacillus subtilis family-11 xylanase by directed evolution
    • Miyazaki K, Takenouchi M, Kondo H, Noro N, Suzuki M, Tsuda S (2006) Thermal stabilization of Bacillus subtilis family-11 xylanase by directed evolution. J Biol Chem. 281:10236-10242
    • (2006) J Biol Chem , vol.281 , pp. 10236-10242
    • Miyazaki, K.1    Takenouchi, M.2    Kondo, H.3    Noro, N.4    Suzuki, M.5    Tsuda, S.6
  • 20
    • 0030334262 scopus 로고    scopus 로고
    • Xylanases: From biology to biotechnology
    • Prade RA (1996) Xylanases: from biology to biotechnology. Biotechnol Genet Eng Rev 13:101-131
    • (1996) Biotechnol Genet Eng Rev , vol.13 , pp. 101-131
    • Prade, R.A.1
  • 21
    • 0037045873 scopus 로고    scopus 로고
    • The endoxylanases from family 11: Computer analysis of protein sequences reveals important structural and phylogenetic relationships
    • Sapag A, Wouters J, Lambert C, de Ioannes P, Eyzaguirre J, Depiereux E (2002) The endoxylanases from family 11: computer analysis of protein sequences reveals important structural and phylogenetic relationships. J Biotechnol 95:109-131
    • (2002) J Biotechnol , vol.95 , pp. 109-131
    • Sapag, A.1    Wouters, J.2    Lambert, C.3    de Ioannes, P.4    Eyzaguirre, J.5    Depiereux, E.6
  • 22
    • 0034661506 scopus 로고    scopus 로고
    • Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling
    • Shibuya H, Kaneko S, Hayashi K (2000) Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling. Biochem J 349:651-656
    • (2000) Biochem J , vol.349 , pp. 651-656
    • Shibuya, H.1    Kaneko, S.2    Hayashi, K.3
  • 23
    • 33846876444 scopus 로고    scopus 로고
    • Directed evolution of the thermostable xylanase from Thermomyces lanuginosus
    • Jun 30 [Epub ahead of print
    • Stephens DE, Rumbold K, Permaul K, Prior BA, Singh S. (2006) Directed evolution of the thermostable xylanase from Thermomyces lanuginosus. J Biotechnol. Jun 30 [Epub ahead of print]
    • (2006) J Biotechnol
    • Stephens, D.E.1    Rumbold, K.2    Permaul, K.3    Prior, B.A.4    Singh, S.5
  • 24
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: Enzymology, molecular biology, and application
    • Subramaniyan S, Prema P (2002) Biotechnology of microbial xylanases: enzymology, molecular biology, and application. Crit Rev Biotechnol 22:33-64
    • (2002) Crit Rev Biotechnol , vol.22 , pp. 33-64
    • Subramaniyan, S.1    Prema, P.2
  • 25
    • 20444388735 scopus 로고    scopus 로고
    • Improvement of the thermostability and catalytic activity of a mesophilic family 11 xylanase by N-terminus replacement
    • Sun JY, Liu MQ, Xu YL, Xu ZR, Pan L, Gao H (2005) Improvement of the thermostability and catalytic activity of a mesophilic family 11 xylanase by N-terminus replacement. Protein Expr Purif 42:122-130
    • (2005) Protein Expr Purif , vol.42 , pp. 122-130
    • Sun, J.Y.1    Liu, M.Q.2    Xu, Y.L.3    Xu, Z.R.4    Pan, L.5    Gao, H.6
  • 26
    • 0034653516 scopus 로고    scopus 로고
    • The thermostabilizing domain, XynA, of Caldibacillus cellulovorans xylanase is a xylan binding domain
    • Sunna A, Gibbs MD, Bergquist PL (2000) The thermostabilizing domain, XynA, of Caldibacillus cellulovorans xylanase is a xylan binding domain. Biochem J 346:583-586
    • (2000) Biochem J , vol.346 , pp. 583-586
    • Sunna, A.1    Gibbs, M.D.2    Bergquist, P.L.3
  • 27
    • 0035370202 scopus 로고    scopus 로고
    • A combination of weakly stabilizing mutations with a disulfide bridge in the R-helix region of Trichoderma reesei endo-1,4-xylanase II increases the thermal stability through synergism
    • Turunen O, Etuaho K, Fenel F, Vehmaanpera J, Wu X, Rouvinen J, Leisola M (2001) A combination of weakly stabilizing mutations with a disulfide bridge in the R-helix region of Trichoderma reesei endo-1,4-xylanase II increases the thermal stability through synergism. J Biotechnol 88:37-46
    • (2001) J Biotechnol , vol.88 , pp. 37-46
    • Turunen, O.1    Etuaho, K.2    Fenel, F.3    Vehmaanpera, J.4    Wu, X.5    Rouvinen, J.6    Leisola, M.7
  • 28
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G, Woell G, Argos P (1997) Protein thermal stability, hydrogen bonds, and ion pairs. J.Mol Biol 269:631-643
    • (1997) J.Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, G.2    Argos, P.3
  • 29
    • 0028080502 scopus 로고
    • Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds
    • Wakarchuk W, Sung W, Campbell R, Cunningham A, Watson D, Yaguchi M (1994) Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds. Protein Eng 7:1379-1386
    • (1994) Protein Eng , vol.7 , pp. 1379-1386
    • Wakarchuk, W.1    Sung, W.2    Campbell, R.3    Cunningham, A.4    Watson, D.5    Yaguchi, M.6
  • 30
    • 0028130117 scopus 로고
    • Multiple proline substitution cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1, 6-glucosidase. Irrefragable proof supporting the proline rule
    • Watanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y (1994) Multiple proline substitution cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1, 6-glucosidase. Irrefragable proof supporting the proline rule. Eur J Biochem 226:277-283
    • (1994) Eur J Biochem , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5
  • 31
    • 24744465631 scopus 로고    scopus 로고
    • Construction, expression, and characterization of a thermostable xylanase
    • Weng XY, Sun JY (2005) Construction, expression, and characterization of a thermostable xylanase. Curr Microbiol 51:188-192
    • (2005) Curr Microbiol , vol.51 , pp. 188-192
    • Weng, X.Y.1    Sun, J.Y.2
  • 32
    • 33846871467 scopus 로고
    • A comparison of blood sugar analyses by the Folin-Wu and Somogyi-Nelson procedures
    • Wilkerson HL, Cohen AS, Kantor N, Francis JO (1962) A comparison of blood sugar analyses by the Folin-Wu and Somogyi-Nelson procedures. Diabetes 11:204-208
    • (1962) Diabetes , vol.11 , pp. 204-208
    • Wilkerson, H.L.1    Cohen, A.S.2    Kantor, N.3    Francis, J.O.4
  • 34
    • 33745492617 scopus 로고    scopus 로고
    • Characterization, gene cloning and expression of new xylanase XYNB with high specific activity
    • Zhang HL, Yao B, Wang YR (2003) Characterization, gene cloning and expression of new xylanase XYNB with high specific activity. Chin J Biotechnol 48:761-765
    • (2003) Chin J Biotechnol , vol.48 , pp. 761-765
    • Zhang, H.L.1    Yao, B.2    Wang, Y.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.