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Volumn 46, Issue 10, 2011, Pages 1921-1926

A novel low-temperature active alkaline pectate lyase from Klebsiella sp. Y1 with potential in textile industry

Author keywords

Alkaline pectate lyase; Bioscouring; Escherichia coli; Klebsiella sp. Y1

Indexed keywords

ACID POLYPEPTIDE; ALKALINE PH; BIOSCOURING; CATALYTIC DOMAINS; ELECTROPHORETIC HOMOGENEITY; HETEROLOGOUS EXPRESSION; INTRINSIC VISCOSITY; KLEBSIELLA SP; KLEBSIELLA SP. Y1; LOW TEMPERATURES; NOVOZYMES; PECTATE LYASE; PECTINASES; POLYGALACTURONIC ACID; RECOMBINANT ENZYMES; SIGNAL PEPTIDE; SINGLE-STEP;

EID: 80052747859     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.06.023     Document Type: Article
Times cited : (23)

References (47)
  • 1
    • 0000129074 scopus 로고
    • The pectic polysaccharides of primary cell walls
    • D.M. Dey, Academic Press London
    • M. O'Neill, P. Albersheim, and A. Darvill The pectic polysaccharides of primary cell walls D.M. Dey, Methods in plant biochemistry 1990 Academic Press London 415 441
    • (1990) Methods in Plant Biochemistry , pp. 415-441
    • O'Neill, M.1    Albersheim, P.2    Darvill, A.3
  • 4
    • 84862945350 scopus 로고    scopus 로고
    • In silico characterization of pectate lyase protein sequences from different source organisms
    • A.K. Dubey, S. Yadav, M. Kumar, V.K. Singh, B.K. Sarangi, and D. Yadav In silico characterization of pectate lyase protein sequences from different source organisms Enzyme Res 2010 230 950
    • (2010) Enzyme Res , pp. 230-950
    • Dubey, A.K.1    Yadav, S.2    Kumar, M.3    Singh, V.K.4    Sarangi, B.K.5    Yadav, D.6
  • 5
    • 0031439907 scopus 로고    scopus 로고
    • Assembly and enlargement of the primary cell wall in plants
    • DOI 10.1146/annurev.cellbio.13.1.171
    • D.J. Cosgrove Assembly and enlargement of the primary cell wall in plants Ann Rev Cell Dev Biol 13 1997 171 201 (Pubitemid 28034524)
    • (1997) Annual Review of Cell and Developmental Biology , vol.13 , pp. 171-201
    • Cosgrove, D.J.1
  • 6
    • 0016375984 scopus 로고
    • Pectinases and pectic polysaccharides
    • W.M. Fogarty, and O.P. Ward Pectinases and pectic polysaccharides Prog Ind Microbiol 13 1974 59 119
    • (1974) Prog Ind Microbiol , vol.13 , pp. 59-119
    • Fogarty, W.M.1    Ward, O.P.2
  • 7
    • 0031932651 scopus 로고    scopus 로고
    • Industrial applications of pectic enzymes: A review
    • DOI 10.1016/S0032-9592(97)00046-0, PII S0032959297000460
    • I. Alkorta, C. Garbisu, M.J. Llama, and J.L. Serra Industrial applications of pectic enzymes: a review Process Biochem 33 1998 21 28 (Pubitemid 28128138)
    • (1998) Process Biochemistry , vol.33 , Issue.1 , pp. 21-28
    • Alkorta, I.1    Garbisu, C.2    Llama, M.J.3    Serra, J.L.4
  • 9
    • 1642300672 scopus 로고    scopus 로고
    • Purified pectinase lowers cationic demand in peroxide-bleached mechanical pulp
    • DOI 10.1016/j.enzmictec.2003.12.005, PII S0141022904000043
    • M. Ricard, and I.D. Reid Purified pectinase lowers cationic demand in peroxide-bleached mechanical pulp Enzyme Microb Technol 34 2004 499 504 (Pubitemid 38373793)
    • (2004) Enzyme and Microbial Technology , vol.34 , Issue.5 , pp. 499-504
    • Ricard, M.1    Reid, I.D.2
  • 10
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: A review
    • DOI 10.1016/j.procbio.2005.03.026, PII S1359511305001765
    • R.S. Jayani, S. Saxena, and R. Gupta Microbial pectinolytic enzymes: a review Process Biochem 40 2005 2931 2944 (Pubitemid 41009190)
    • (2005) Process Biochemistry , vol.40 , Issue.9 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 11
    • 0036038901 scopus 로고    scopus 로고
    • Microbial alkaline pectinases and their industrial applications: A review
    • DOI 10.1007/s00253-002-1061-1
    • G.S. Hoondal, R.P. Tiwari, R. Tewari, N. Dahiya, and Q.K. Beg Microbial alkaline pectinases and their industrial applications: a review Appl Microbiol Biotechnol 59 2002 409 418 (Pubitemid 35002174)
    • (2002) Applied Microbiology and Biotechnology , vol.59 , Issue.4-5 , pp. 409-418
    • Hoondal, G.1    Tiwari, R.2    Tewari, R.3    Dahiya, N.4    Beg, Q.5
  • 13
    • 78149413176 scopus 로고    scopus 로고
    • Molecular identification and pectate lyase production by Bacillus strains involved in cocoa fermentation
    • H.G. Ouattara, S. Reverchon, S.L. Niamke, and W. Nasser Molecular identification and pectate lyase production by Bacillus strains involved in cocoa fermentation Food Microbiol 28 2011 1 8
    • (2011) Food Microbiol , vol.28 , pp. 1-8
    • Ouattara, H.G.1    Reverchon, S.2    Niamke, S.L.3    Nasser, W.4
  • 14
    • 20044386726 scopus 로고    scopus 로고
    • Characterization of cold-active pectate lyases from psychrophilic Mrakia frigida
    • DOI 10.1111/j.1472-765X.2005.01704.x
    • R. Margesin, V. Fauster, and P.A. Fonteyne Characterization of cold-active pectate lyases from psychrophilic Mrakia frigida Lett Appl Microbiol 40 2005 453 459 (Pubitemid 40769938)
    • (2005) Letters in Applied Microbiology , vol.40 , Issue.6 , pp. 453-459
    • Margesin, R.1    Fauster, V.2    Fonteyne, P.-A.3
  • 15
    • 0026513432 scopus 로고
    • Purification of the acidic pectate lyase and nucleotide sequence of the corresponding gene (pelA) of Erwinia chrysanthemi strain 3937
    • S. Favey, C. Bourson, Y. Bertheau, A. Kotoujansky, and M. Boccara Purification of the acidic pectate lyase and nucleotide sequence of the corresponding gene (pelA) of Erwinia chrysanthemi strain 3937 J Gen Microbiol 38 1992 499 508
    • (1992) J Gen Microbiol , vol.38 , pp. 499-508
    • Favey, S.1    Bourson, C.2    Bertheau, Y.3    Kotoujansky, A.4    Boccara, M.5
  • 16
    • 0023410604 scopus 로고
    • Characterization of the Erwinia carotovora pel B gene and its product pectate lyase B
    • S.P. Lei, H.C. Lin, S.S. Wang, and G. Wilcox Characterization of the Erwinia carotovora pel B gene and its product pectate lyase B J Bacteriol 169 1987 4379 4383
    • (1987) J Bacteriol , vol.169 , pp. 4379-4383
    • Lei, S.P.1    Lin, H.C.2    Wang, S.S.3    Wilcox, G.4
  • 17
    • 0018733966 scopus 로고
    • Characterization of intracellular polygalacturonic acid trans-eliminase from Klebsiella oxytoca, Yersinia enterocolitica, and Erwinia chrysanthemi
    • S.T. Bagley, and M.P. Starr Characterization of intracellular polygalacturonic acid trans-eliminase from Klebsiella oxytoca, Yersinia enterocolitica, and Erwinia chrysanthemi Curr Microbiol 2 1979 381 386 (Pubitemid 10213878)
    • (1979) Current Microbiology , vol.2 , Issue.6 , pp. 381-386
    • Bagley, S.T.1    Starr, M.P.2
  • 18
    • 0025875884 scopus 로고
    • Cloning of pectate lyase gene pel from Pseudomonas fluorescens and detection of sequences homologous to pel in Pseudomonas viridiflava and Pseudomonas putida
    • C.H. Liao Cloning of pectate lyase gene pel from Pseudomonas fluorescens and detection of sequences homologous to pel in Pseudomonas viridiflava and Pseudomonas putida J Bacteriol 173 1991 4386 4393
    • (1991) J Bacteriol , vol.173 , pp. 4386-4393
    • Liao, C.H.1
  • 20
    • 41549126253 scopus 로고    scopus 로고
    • Purification and characterization of an alkaline pectin lyase from Aspergillus flavus
    • S. Yadav, P.K. Yadav, D. Yadav, and K.D. Yadav Purification and characterization of an alkaline pectin lyase from Aspergillus flavus Process Biochem 43 2008 547 552
    • (2008) Process Biochem , vol.43 , pp. 547-552
    • Yadav, S.1    Yadav, P.K.2    Yadav, D.3    Yadav, K.D.4
  • 21
    • 0035310348 scopus 로고    scopus 로고
    • Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module
    • DOI 10.1042/0264-6021:3550155
    • I.E. Brown, M.H. Mallen, S.J. Charnock, G.J. Davies, and G.W. Black Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module Biochem J 355 2001 155 165 (Pubitemid 32304246)
    • (2001) Biochemical Journal , vol.355 , Issue.1 , pp. 155-165
    • Brown, I.E.1    Mallen, M.H.2    Charnock, S.J.3    Davies, G.J.4    Black, G.W.5
  • 22
    • 0035316450 scopus 로고    scopus 로고
    • Enzymatic properties of the highly thermophilic and alkaline pectate lyase Pel-4B from alkaliphilic Bacillus sp. strain P-4-N and the entire nucleotide and amino acid sequences
    • DOI 10.1007/s007920100182
    • Y. Hatada, T. Kobayashi, and S. Ito Enzymatic properties of the highly thermophilic and alkaline pectate lyase Pel-4B from alkaliphilic Bacillus sp. strain P-4-N and the entire nucleotide and amino acid sequences Extremophiles 5 2001 127 133 (Pubitemid 33725472)
    • (2001) Extremophiles , vol.5 , Issue.2 , pp. 127-133
    • Hatada, Y.1    Kobayashi, T.2    Ito, S.3
  • 23
    • 0023434016 scopus 로고
    • Pectate lyase from Fusarium solani f. sp. pisi: Purification characterization, in vitro translation of the mRNA, and involvement in pathogenicity
    • M.S. Crawford, and P.E. Kolattukudy Pectate lyase from Fusarium solani f. sp. pisi: purification characterization, in vitro translation of the mRNA, and involvement in pathogenicity Arch Biochem Biophys 258 1987 196 205
    • (1987) Arch Biochem Biophys , vol.258 , pp. 196-205
    • Crawford, M.S.1    Kolattukudy, P.E.2
  • 24
    • 42949179630 scopus 로고    scopus 로고
    • Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris
    • B. Zhuge, G. Du, W. Shen, J. Zhuge, and J. Chen Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris Biochem Eng J 40 2008 92 98
    • (2008) Biochem Eng J , vol.40 , pp. 92-98
    • Zhuge, B.1    Du, G.2    Shen, W.3    Zhuge, J.4    Chen, J.5
  • 28
    • 78650249603 scopus 로고    scopus 로고
    • Cloning, expression and characterization of an acidic endo-polygalacturonase from Bispora sp. MEY-1 and its potential application in juice clarification
    • J. Yang, H. Luo, J. Li, K. Wang, H. Cheng, Y. Bai, T. Yuan, Y. Fan, and B. Yao Cloning, expression and characterization of an acidic endo-polygalacturonase from Bispora sp. MEY-1 and its potential application in juice clarification Process Biochem 46 2010 272 277
    • (2010) Process Biochem , vol.46 , pp. 272-277
    • Yang, J.1    Luo, H.2    Li, J.3    Wang, K.4    Cheng, H.5    Bai, Y.6    Yuan, T.7    Fan, Y.8    Yao, B.9
  • 29
    • 33845688815 scopus 로고    scopus 로고
    • Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry
    • K.R. Celestino, R.B. Cunha, and C.R. Felix Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry BMC Biochem 7 2006 7 8
    • (2006) BMC Biochem , vol.7 , pp. 7-8
    • Celestino, K.R.1    Cunha, R.B.2    Felix, C.R.3
  • 32
    • 36849087799 scopus 로고    scopus 로고
    • A family 2 pectate lyase displays a rare fold and transition metal-assisted β-elimination
    • DOI 10.1074/jbc.M705511200
    • D.W. Abbott, and A.B. Boraston A family 2 pectate lyase displays a rare fold and transition metal-assisted β-elimination J Biol Chem 282 2007 35328 35336 (Pubitemid 350232426)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 35328-35336
    • Abbott, D.W.1    Boraston, A.B.2
  • 33
    • 78650518886 scopus 로고    scopus 로고
    • Arg 235 is an essential catalytic residue of Bacillus pumilus DKS1 pectate lyase to degum ramie fibre
    • S. Basu, A. Roy, A. Ghosh, A. Bera, D. Chattopadhyay, and K. Chakrabarti Arg 235 is an essential catalytic residue of Bacillus pumilus DKS1 pectate lyase to degum ramie fibre Biodegradation 22 2010 153 161
    • (2010) Biodegradation , vol.22 , pp. 153-161
    • Basu, S.1    Roy, A.2    Ghosh, A.3    Bera, A.4    Chattopadhyay, D.5    Chakrabarti, K.6
  • 34
    • 0021989499 scopus 로고
    • Habitat association of Klebsiella species
    • S.T. Bagley Habitat association of Klebsiella species Infect Control 6 1985 52 58 (Pubitemid 15146591)
    • (1985) Infection Control , vol.6 , Issue.2 , pp. 52-58
    • Bagley, S.T.1
  • 35
    • 0031792165 scopus 로고    scopus 로고
    • Klebsiella spp. as nosocomial pathogens: Epidemiology, taxonomy, typing methods, and pathogenicity factors
    • R. Podschun, and U. Ullmann Klebsiella spp. as nosocomial pathogens: epidemiology, taxonomy, typing methods, and pathogenicity factors Clin Microbiol Rev 11 1998 589 603 (Pubitemid 28497563)
    • (1998) Clinical Microbiology Reviews , vol.11 , Issue.4 , pp. 589-603
    • Podschun, R.1    Ullmann, U.2
  • 36
    • 0141491878 scopus 로고    scopus 로고
    • Cloning and structural analysis of the Klebsiella oxytoca VN13 peh gene
    • G. Kovtunovych, O. Lar, and N. Kozyrovska Cloning and structural analysis of the Klebsiella oxytoca VN13 peh gene Biopolim Kletka 16 2000 356 363
    • (2000) Biopolim Kletka , vol.16 , pp. 356-363
    • Kovtunovych, G.1    Lar, O.2    Kozyrovska, N.3
  • 37
    • 0141756058 scopus 로고    scopus 로고
    • Identification of Klebsiella oxytoca using a specific PCR assay targeting the polygalacturonase pehX gene
    • DOI 10.1016/S0923-2508(03)00148-7
    • G. Kovtunovych, T. Lytvynenko, V. Negrutska, O. Lar, S. Brisse, and N. Kozyrovska Identification of Klebsiella oxytoca using a specific PCR assay targeting the polygalacturonase pehX gene Res Microbiol 154 2003 587 592 (Pubitemid 37177003)
    • (2003) Research in Microbiology , vol.154 , Issue.8 , pp. 587-592
    • Kovtunovych, G.1    Lytvynenko, T.2    Negrutska, V.3    Lar, O.4    Brisse, S.5    Kozyrovska, N.6
  • 39
    • 0032587947 scopus 로고    scopus 로고
    • KdgR(Ecc) Negatively regulates genes for pectinases, cellulase, protease, Harpin(Ecc), and a global RNA regulator in Erwinia carotovora subsp. carotovora
    • Y. Liu, G. Jiang, Y. Cui, A. Mukherjee, W.L. Ma, and A.K. Chatterjee kdgREcc negatively regulates genes for pectinases, cellulase, protease, harpinEcc, and a global RNA regulator in Erwinia carotovora subsp. carotovora J Bacteriol 181 1999 2411 2421 (Pubitemid 29181563)
    • (1999) Journal of Bacteriology , vol.181 , Issue.8 , pp. 2411-2421
    • Liu, Y.1    Jiang, G.2    Cui, Y.3    Mukherjee, A.4    Ma, W.L.5    Chatterjee, A.K.6
  • 40
    • 0037040884 scopus 로고    scopus 로고
    • The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family
    • DOI 10.1074/jbc.M109193200
    • N. Blot, C. Berrier, N. Hugouvieux-Cotte-Pattat, A. Ghazi, and G. Condemine The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family J Biol Chem 277 2002 7936 7944 (Pubitemid 34968244)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 7936-7944
    • Blot, N.1    Berrier, C.2    Hugouvieux-Cotte-Pattat, N.3    Ghazi, A.4    Condemine, G.5
  • 41
    • 0036381073 scopus 로고    scopus 로고
    • Cold-active pectinolytic activity of psychrophilic-basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1
    • T. Nakagawa, K. Yamada, T. Miyaji, and N. Tomizuka Cold-active pectinolytic activity of psychrophilic-basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1 J Biosci Bioeng 94 2002 175 177
    • (2002) J Biosci Bioeng , vol.94 , pp. 175-177
    • Nakagawa, T.1    Yamada, K.2    Miyaji, T.3    Tomizuka, N.4
  • 42
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • N.J. Russell Toward a molecular understanding of cold activity of enzymes from psychrophiles Extremophiles 4 2000 83 90
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russell, N.J.1
  • 43
    • 65249146105 scopus 로고    scopus 로고
    • Purification, characterization, and overexpression of thermophilic pectate lyase of Bacillus sp. RN1 isolated from a hot spring in Thailand
    • W. Sukhumsiirchart, S. Kawanishi, W. Deesukon, K. Chansiri, H. Kawasaki, and T. Sakamoto Purification, characterization, and overexpression of thermophilic pectate lyase of Bacillus sp. RN1 isolated from a hot spring in Thailand Biosci Biotechnol Biochem 73 2009 268 273
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 268-273
    • Sukhumsiirchart, W.1    Kawanishi, S.2    Deesukon, W.3    Chansiri, K.4    Kawasaki, H.5    Sakamoto, T.6
  • 45
    • 77957153923 scopus 로고    scopus 로고
    • Structural insights into the acidophilic pH adaptation of a novel endo-1,4-β-xylanase from Scytalidium acidophilum
    • C. Michaux, J. Pouyez, A. Mayard, P. Vandurm, I. Housen, and J. Wouters Structural insights into the acidophilic pH adaptation of a novel endo-1,4-β-xylanase from Scytalidium acidophilum Biochimie 92 2010 1407 1415
    • (2010) Biochimie , vol.92 , pp. 1407-1415
    • Michaux, C.1    Pouyez, J.2    Mayard, A.3    Vandurm, P.4    Housen, I.5    Wouters, J.6
  • 46
    • 67651236276 scopus 로고    scopus 로고
    • An alkaline active xylanase: Insights into mechanisms of high pH catalytic adaptation
    • G. Mamo, M. Thunnissen, R. Hatti-Kaul, and B. Mattiasson An alkaline active xylanase: insights into mechanisms of high pH catalytic adaptation Biochimie 91 2009 1187 1196
    • (2009) Biochimie , vol.91 , pp. 1187-1196
    • Mamo, G.1    Thunnissen, M.2    Hatti-Kaul, R.3    Mattiasson, B.4


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