메뉴 건너뛰기




Volumn 20, Issue 4, 2010, Pages 670-677

Cloning, expression, and characterization of a highly active alkaline pectate lyase from alkaliphilic Bacillus sp. N16-5

Author keywords

Alkaliphile; Bacillus sp.; N16 5; Pectate lyase; Pectin

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; CALCIUM ION; DIGALACTURONATE; GALACTURONIC ACID; PECTATE LYASE; PECTIN; POLYGALACTURONIC ACID; POLYPEPTIDE; POLYSACCHARIDE LYASE; POLYSACCHARIDE LYASE FAMILY 1; SIGNAL PEPTIDE; TRIGALACTURONATE; UNCLASSIFIED DRUG;

EID: 77954994527     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0911.11019     Document Type: Article
Times cited : (30)

References (34)
  • 1
    • 2542478112 scopus 로고    scopus 로고
    • Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
    • Berensmeier, S., S. A. Singh, J. Meens, and K. Buchholz. 2004. Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase. Appl. Microbiol. Biotechnol. 64: 560-567.
    • (2004) Appl. Microbiol. Biotechnol , vol.64 , pp. 560-567
    • Berensmeier, S.1    Singh, S.A.2    Meens, J.3    Buchholz, K.4
  • 3
    • 0028803413 scopus 로고
    • Purification and characterization of an extracellular pectate lyase from an Amycolata sp
    • Bruhlmann, F. 1995. Purification and characterization of an extracellular pectate lyase from an Amycolata sp. Appl. Environ. Microbiol. 61: 3580-3585.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 3580-3585
    • Bruhlmann, F.1
  • 4
    • 0027006839 scopus 로고
    • Screening of pectinase producer from alkalophilic bacteria and study on its potential application in degumming of ramie
    • Cao, J., Z. L. and S. Chen. 1992. Screening of pectinase producer from alkalophilic bacteria and study on its potential application in degumming of ramie. Enzyme Microb. Technol. 4: 1013-1016.
    • (1992) Enzyme Microb. Technol , vol.4 , pp. 1013-1016
    • Cao, J.Z.L.1    Chen, S.2
  • 5
    • 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
    • Hatada, Y., T. Kobayashi, and S. Ito. 2001. 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: 127-133.
    • (2001) Extremophiles , vol.5 , pp. 127-133
    • Hatada, Y.1    Kobayashi, T.2    Ito, S.3
  • 6
    • 0029257437 scopus 로고
    • Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat, B., S. E. Heffron, M. D. Yoder, S. E. Lietzke, and F. Jurnak. 1995. Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 107: 963-976.
    • (1995) Plant Physiol , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzke, S.E.4    Jurnak, F.5
  • 9
    • 84954946520 scopus 로고
    • Production of alkaline enzymes by alkalophilic microorganisms. Part I. Alkaline protease produced by Bacillus no. 221
    • Horikoshi, K. 1971. Production of alkaline enzymes by alkalophilic microorganisms. Part I. Alkaline protease produced by Bacillus no. 221. Agric. Biol. Chem. 36: 1407-1414.
    • (1971) Agric. Biol. Chem , vol.36 , pp. 1407-1414
    • Horikoshi, K.1
  • 10
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: A review
    • Jayani, R. S., S. Saxena, and R. Gupta. 2005. Microbial pectinolytic enzymes: A review. Process Biochem. 40: 2931-2944.
    • (2005) Process Biochem , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 11
    • 0035069389 scopus 로고    scopus 로고
    • Application of an alkaline and thermostable polygalacturonase from Bacillus sp. MG-cp-2 in degumming of ramie (Boehmeria nivea) and sunn hemp (Crotalaria juncea) bast fibres
    • Kapoor, M., Q. K. Beg, B. Bhushan, K. Singh, K. S. Dadhich, and G. S. Hoondal. 2001. Application of an alkaline and thermostable polygalacturonase from Bacillus sp. MG-cp-2 in degumming of ramie (Boehmeria nivea) and sunn hemp (Crotalaria juncea) bast fibres. Process Biochem. 36: 803-807.
    • (2001) Process Biochem , vol.36 , pp. 803-807
    • Kapoor, M.1    Beg, Q.K.2    Bhushan, B.3    Singh, K.4    Dadhich, K.S.5    Hoondal, G.S.6
  • 12
    • 0033666181 scopus 로고    scopus 로고
    • Production and partial purification and characterization of a thermo-alkali stable polygalacturonase from Bacillus sp. MG-cp-2
    • Kapoor, M., Q. Khalil Beg, B. Bhushan, K. S. Dadhich, and G. S. Hoondal. 2000. Production and partial purification and characterization of a thermo-alkali stable polygalacturonase from Bacillus sp. MG-cp-2. Process Biochem. 36: 467-473.
    • (2000) Process Biochem , vol.36 , pp. 467-473
    • Kapoor, M.1    Khalil, B.Q.2    Bhushan, B.3    Dadhich, K.S.4    Hoondal, G.S.5
  • 13
    • 0034867729 scopus 로고    scopus 로고
    • Degumming of buel (Grewia optiva) bast fibres by pectinolytic enzyme from Bacillus sp. DT7
    • Kashayp, D. R., P. K. Vohra, S. K. Soni, and R. Tewari. 2001. Degumming of buel (Grewia optiva) bast fibres by pectinolytic enzyme from Bacillus sp. DT7. Biotechnol. Lett. 23: 1297-1301.
    • (2001) Biotechnol. Lett , vol.23 , pp. 1297-1301
    • Kashayp, D.R.1    Vohra, P.K.2    Soni, S.K.3    Tewari, R.4
  • 14
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinases in the commercial sector: A review
    • Kashyap, D. R., P. K. Vohra, S. Chopra, and R. Tewari. 2001. Applications of pectinases in the commercial sector: A review. Bioresour. Technol. 77: 215-227.
    • (2001) Bioresour. Technol , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 15
    • 0029861087 scopus 로고    scopus 로고
    • Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity
    • Kita, N., C. M. Boyd, M. R. Garrett, F. Jurnak, and N. T. Keen. 1996. Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity. J. Biol. Chem. 271: 26529-26535.
    • (1996) J. Biol. Chem , vol.271 , pp. 26529-26535
    • Kita, N.1    Boyd, C.M.2    Garrett, M.R.3    Jurnak, F.4    Keen, N.T.5
  • 17
    • 0032908426 scopus 로고    scopus 로고
    • Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate
    • Kobayashi, T., Y. Hatada, N. Higaki, D. D. Lusterio, T. Ozawa, K. Koike, S. Kawai, and S. Ito. 1999. Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate. Biochim. Biophys. Acta 1427: 145-154.
    • (1999) Biochim. Biophys. Acta , vol.1427 , pp. 145-154
    • Kobayashi, T.1    Hatada, Y.2    Higaki, N.3    Lusterio, D.D.4    Ozawa, T.5    Koike, K.6    Kawai, S.7    Ito, S.8
  • 18
    • 0034571727 scopus 로고    scopus 로고
    • Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: Its catalytic properties and deduced amino acid sequence
    • Kobayashi, T., Y. Hatada, A. Suzumatsu, K. Saeki, Y. Hakamada, and S. Ito. 2000. Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: Its catalytic properties and deduced amino acid sequence. Extremophiles 4: 377-383.
    • (2000) Extremophiles , vol.4 , pp. 377-383
    • Kobayashi, T.1    Hatada, Y.2    Suzumatsu, A.3    Saeki, K.4    Hakamada, Y.5    Ito, S.6
  • 19
    • 0035811977 scopus 로고    scopus 로고
    • Purification and properties of a high-molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus
    • Kobayashi, T., N. Higaki, A. Suzumatsu, K. Sawada, H. Hagihara, S. Kawai, and S. Ito. 2001. Purification and properties of a high-molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus. Enzyme Microb. Technol. 29: 70-75.
    • (2001) Enzyme Microb. Technol , vol.29 , pp. 70-75
    • Kobayashi, T.1    Higaki, N.2    Suzumatsu, A.3    Sawada, K.4    Hagihara, H.5    Kawai, S.6    Ito, S.7
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., L. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.L.1
  • 21
    • 0003063088 scopus 로고    scopus 로고
    • The refined three-dimensional structure of pectate lyase E from Erwinia chrysanthemi at 2.2 A resolution
    • Lietzke, S. E., R. D. Scavetta, M. D. Yoder, and F. Jurnak. 1996. The refined three-dimensional structure of pectate lyase E from Erwinia chrysanthemi at 2.2 A resolution. Plant Physiol. 111: 73-92.
    • (1996) Plant Physiol , vol.111 , pp. 73-92
    • Lietzke, S.E.1    Scavetta, R.D.2    Yoder, M.D.3    Jurnak, F.4
  • 22
    • 0346551767 scopus 로고
    • Production and some properties of alkaline β-mannanase [in Chinese
    • Ma, Y., X. Tian, P. Zhou, and D. Wang. 1991. Production and some properties of alkaline β-mannanase [in Chinese]. Acta Microbiol. Sin. 31: 443-448.
    • (1991) Acta Microbiol. Sin , vol.31 , pp. 443-448
    • Ma, Y.1    Tian, X.2    Zhou, P.3    Wang, D.4
  • 23
    • 12544256289 scopus 로고    scopus 로고
    • Characterization and gene cloning of a novel beta-mannanase from alkaliphilic Bacillus sp. N16-5
    • Ma, Y., Y. Xue, Y. Dou, Z. Xu, W. Tao, and P. Zhou. 2004. Characterization and gene cloning of a novel beta-mannanase from alkaliphilic Bacillus sp. N16-5. Extremophiles 8: 447-454.
    • (2004) Extremophiles , vol.8 , pp. 447-454
    • Ma, Y.1    Xue, Y.2    Dou, Y.3    Xu, Z.4    Tao, W.5    Zhou, P.6
  • 24
    • 0031570284 scopus 로고    scopus 로고
    • Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases
    • Mayans, O., M. Scott, I. Connerton, T. Gravesen, J. Benen, J. Visser, R. Pickersgill, and J. Jenkins. 1997. Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5: 677-689.
    • (1997) Structure , vol.5 , pp. 677-689
    • Mayans, O.1    Scott, M.2    Connerton, I.3    Gravesen, T.4    Benen, J.5    Visser, J.6    Pickersgill, R.7    Jenkins, J.8
  • 25
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10: 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 27
    • 0004136246 scopus 로고
    • 2nd Ed. Cold Spring Harbor Laboratory, Press Cold Spring Harbor, NY
    • Sambrook J, F. E. and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual, 2nd Ed. Cold Spring Harbor Laboratory, Press Cold Spring Harbor, NY.
    • (1989) Molecular Cloning: A Laboratory Manual
    • Sambrook, J.1
  • 28
    • 0035814473 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of the gene encoding an exopolygalacturonase of a Bacillus isolate and properties of its recombinant enzyme
    • Sawada, K., A. Suzumatsu, T. Kobayashi, and S. Ito. 2001. Molecular cloning and sequencing of the gene encoding an exopolygalacturonase of a Bacillus isolate and properties of its recombinant enzyme. Biochim. Biophys. Acta 1568: 162-170.
    • (2001) Biochim. Biophys. Acta , vol.1568 , pp. 162-170
    • Sawada, K.1    Suzumatsu, A.2    Kobayashi, T.3    Ito, S.4
  • 30
    • 20144364220 scopus 로고    scopus 로고
    • Discovery of pectin-degrading enzymes and directed evolution of a novel pectate lyase for processing cotton fabric
    • Solbak, A. I., T. H. Richardson, R. T. McCann, K. A. Kline, F. Bartnek, G. Tomlinson, et al. 2005. Discovery of pectin-degrading enzymes and directed evolution of a novel pectate lyase for processing cotton fabric. J. Biol. Chem. 280: 9431-9438.
    • (2005) J. Biol. Chem , vol.280 , pp. 9431-9438
    • Solbak, A.I.1    Richardson, T.H.2    McCann, R.T.3    Kline, K.A.4    Bartnek, F.5    Tomlinson, G.6
  • 31
    • 0034327380 scopus 로고    scopus 로고
    • Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis
    • Takami, H., K. Nakasone, Y. Takaki, G. Maeno, R. Sasaki, N. Masui, et al. 2000. Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis. Nucleic Acids Res. 28: 4317-4331.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4317-4331
    • Takami, H.1    Nakasone, K.2    Takaki, Y.3    Maeno, G.4    Sasaki, R.5    Masui, N.6
  • 32
    • 0030944441 scopus 로고    scopus 로고
    • Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: Enzyme characteristics and potential inhibitors
    • Tardy, F., W. Nasser, J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1997. Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: Enzyme characteristics and potential inhibitors. J. Bacteriol. 179: 2503-2511.
    • (1997) J. Bacteriol , vol.179 , pp. 2503-2511
    • Tardy, F.1    Nasser, W.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 34
    • 0029141684 scopus 로고
    • The refined three-dimensional structure of pectate lyase C from Erwinia chrysanthemi at 2.2 Angstrom resolution (implications for an enzymatic mechanism)
    • Yoder, M. D. and F. Jurnak. 1995. The refined three-dimensional structure of pectate lyase C from Erwinia chrysanthemi at 2.2 Angstrom resolution (implications for an enzymatic mechanism). Plant Physiol. 107: 349-364.
    • (1995) Plant Physiol , vol.107 , pp. 349-364
    • Yoder, M.D.1    Jurnak, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.