메뉴 건너뛰기




Volumn 99, Issue 17, 2008, Pages 8088-8094

Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1

Author keywords

Bacillus pumilus DKS1; Pectate lyase; Thermodynamic activation and inactivation parameters

Indexed keywords

BACTERIOLOGY; CALCIUM; CHROMATOGRAPHIC ANALYSIS; COLLOIDS; ENZYMES; FILTRATION; FOOD ADDITIVES; GEL PERMEATION CHROMATOGRAPHY; GELATION; ION CHROMATOGRAPHY; ION EXCHANGE; MANGANESE; NICKEL; POLYSACCHARIDES; POROUS MATERIALS; PURIFICATION; THERMODYNAMICS; ZINC; ZINC SULFIDE;

EID: 47749091686     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2008.03.032     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 47749099463 scopus 로고    scopus 로고
    • Bjornvad, M.E., Kongsbak, L.N., Lange, E.K., Martin, S., Husain, P.A., 2003. .
    • Bjornvad, M.E., Kongsbak, L.N., Lange, E.K., Martin, S., Husain, P.A., 2003. .
  • 2
    • 0028319223 scopus 로고
    • Pectinolytic enzymes from Actinomycetes for the degumming of ramie bast fibers
    • Bruhlmann F., Kim K.S., Zimmermann W., and Fiechter A. Pectinolytic enzymes from Actinomycetes for the degumming of ramie bast fibers. Appl. Environ. Microbiol. 60 (1994) 2107-2112
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2107-2112
    • Bruhlmann, F.1    Kim, K.S.2    Zimmermann, W.3    Fiechter, A.4
  • 3
    • 0027006839 scopus 로고
    • Screening of pectinase producer from alkalophilic bacteria and study on its potential applications in degumming of ramie
    • Cao J., Zheng L., and Chen S. Screening of pectinase producer from alkalophilic bacteria and study on its potential applications in degumming of ramie. Enzyme Microbiol. Technol. 14 (1992) 1013-1016
    • (1992) Enzyme Microbiol. Technol. , vol.14 , pp. 1013-1016
    • Cao, J.1    Zheng, L.2    Chen, S.3
  • 4
    • 0015135189 scopus 로고
    • Purification and properties of a polygalacturonic acid trans-eliminase produced by Bacillus pumilus
    • Dave B.A., and Vaughn R.H. Purification and properties of a polygalacturonic acid trans-eliminase produced by Bacillus pumilus. J. Bacteriol. 108 (1971) 166-174
    • (1971) J. Bacteriol. , vol.108 , pp. 166-174
    • Dave, B.A.1    Vaughn, R.H.2
  • 5
    • 0001952007 scopus 로고
    • Pectic enzymes produced by Erwinia chrysanthemi and their effect on plant tissue
    • Garibaldi A., and Bateman D.F. Pectic enzymes produced by Erwinia chrysanthemi and their effect on plant tissue. Physiol. Plant Pathol. 1 (1971) 25-40
    • (1971) Physiol. Plant Pathol. , vol.1 , pp. 25-40
    • Garibaldi, A.1    Bateman, D.F.2
  • 6
    • 3042932314 scopus 로고
    • Characterization of pectate lyase from alkalitolerant Bacillus sp. YA-14
    • Han H.-J., Park H.-K., Bai D.-H., and Yu J.-H. Characterization of pectate lyase from alkalitolerant Bacillus sp. YA-14. J. Microbiol. Biotechnol. 2 (1992) 260-267
    • (1992) J. Microbiol. Biotechnol. , vol.2 , pp. 260-267
    • Han, H.-J.1    Park, H.-K.2    Bai, D.-H.3    Yu, J.-H.4
  • 7
    • 35148839893 scopus 로고    scopus 로고
    • Microbial evolution, diversity and ecology: a decade of ribosomal RNA analysis of uncultivated microorganisms
    • Head I.M., Saunders J.R., and Pickup R.W. Microbial evolution, diversity and ecology: a decade of ribosomal RNA analysis of uncultivated microorganisms. Microbiol. Ecol. 23 (1998) 45-54
    • (1998) Microbiol. Ecol. , vol.23 , pp. 45-54
    • Head, I.M.1    Saunders, J.R.2    Pickup, R.W.3
  • 9
    • 0034808018 scopus 로고    scopus 로고
    • A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS)
    • Kamen D.E., and Woody R.W. A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS). Protein Sci. 10 (2001) 2123-2130
    • (2001) Protein Sci. , vol.10 , pp. 2123-2130
    • Kamen, D.E.1    Woody, R.W.2
  • 10
    • 0033927724 scopus 로고    scopus 로고
    • Production, purification and characterization of pectinase from a Bacillus sp. DT7
    • Kashyap D.R., Chandra S., Kaul A., and Tewari R. Production, purification and characterization of pectinase from a Bacillus sp. DT7. World J. Microbiol. Biotechnol. 16 (2000) 277-282
    • (2000) World J. Microbiol. Biotechnol. , vol.16 , pp. 277-282
    • Kashyap, D.R.1    Chandra, S.2    Kaul, A.3    Tewari, R.4
  • 11
    • 0024335334 scopus 로고
    • Chemical modification of a xylanase from a thermotolerant Streptomyces. Evidence for essential tryptophan and cysteine residues at the active site
    • Keskar S.S., Srinivasan M.C., and Deshpande V.V. Chemical modification of a xylanase from a thermotolerant Streptomyces. Evidence for essential tryptophan and cysteine residues at the active site. Biochem. J. 261 (1989) 49-55
    • (1989) Biochem. J. , vol.261 , pp. 49-55
    • Keskar, S.S.1    Srinivasan, M.C.2    Deshpande, V.V.3
  • 13
    • 0023831870 scopus 로고
    • Approach to maceration mechanism in enzymatic pulping of bast fibres by alkalophilic pectinolytic enzymes produced by Erwinia species
    • Kobayashi Y., Komae K., Tanabe H., and Matsuo R. Approach to maceration mechanism in enzymatic pulping of bast fibres by alkalophilic pectinolytic enzymes produced by Erwinia species. Biotechnol. Adv. 6 (1988) 29-37
    • (1988) Biotechnol. Adv. , vol.6 , pp. 29-37
    • Kobayashi, Y.1    Komae, K.2    Tanabe, H.3    Matsuo, R.4
  • 14
    • 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., Hatada Y., Higaki N., Lusterio D.D., Ozawa T., Koike K., Kawai S., and Ito S. Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate. Biochem. Biophys. Acta 1427 (1999) 145-154
    • (1999) Biochem. 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
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 16
    • 0030855808 scopus 로고    scopus 로고
    • Biochemical characterization of pectate lyases produced by fluorescent Pseudomonads associated with spoilage of fresh fruits and vegetables
    • Liao C.-H., Sullivan J., Grady J., and Wong L.-J.C. Biochemical characterization of pectate lyases produced by fluorescent Pseudomonads associated with spoilage of fresh fruits and vegetables. J. Appl. Microbiol. 83 (1997) 10-16
    • (1997) J. Appl. Microbiol. , vol.83 , pp. 10-16
    • Liao, C.-H.1    Sullivan, J.2    Grady, J.3    Wong, L.-J.C.4
  • 20
    • 0004522659 scopus 로고    scopus 로고
    • The use of 16S rDNA methods in soil microbial ecology
    • Macrae A. The use of 16S rDNA methods in soil microbial ecology. Braz. J. Microbiol. 31 (2000) 77-82
    • (2000) Braz. J. Microbiol. , vol.31 , pp. 77-82
    • Macrae, A.1
  • 21
    • 0014634440 scopus 로고
    • Metabolic regulation polygalacturonic acid trans-eliminase in Erwinia
    • Moran F., and Starr M.P. Metabolic regulation polygalacturonic acid trans-eliminase in Erwinia. Eur. J. Biochem. 11 (1969) 291-295
    • (1969) Eur. J. Biochem. , vol.11 , pp. 291-295
    • Moran, F.1    Starr, M.P.2
  • 22
    • 0001724709 scopus 로고
    • The characteristics of a polygalacturonase produced by Bacillus polymyxa
    • Nagel C.W., and Vaughn R.H. The characteristics of a polygalacturonase produced by Bacillus polymyxa. Arch. Biochem. Biophys. 93 (1961) 344-352
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 344-352
    • Nagel, C.W.1    Vaughn, R.H.2
  • 23
    • 0007373240 scopus 로고
    • Chemical modification of tryptophan residues in Abrin-a
    • Ohba H., Yamasaki N., and Fumatsu G. Chemical modification of tryptophan residues in Abrin-a. Agric. Biol. Chem. 55 (1991) 1579-1585
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1579-1585
    • Ohba, H.1    Yamasaki, N.2    Fumatsu, G.3
  • 24
    • 0001287340 scopus 로고
    • Enzymatic and physicochemical properties of an exo-(1 → 3)-β-d-glucanase from Rhizoctonia solani
    • Ohio N., Nono I., and Yadomae T. Enzymatic and physicochemical properties of an exo-(1 → 3)-β-d-glucanase from Rhizoctonia solani. Carbohydr. Res. 194 (1989) 261-271
    • (1989) Carbohydr. Res. , vol.194 , pp. 261-271
    • Ohio, N.1    Nono, I.2    Yadomae, T.3
  • 25
    • 85004246984 scopus 로고
    • An isomalto-dextranase accompanied by isopullulanase activity from Arthrobacter globiformis T6
    • Okada G., Takayanagi T., Miyahara S., and Teruo S. An isomalto-dextranase accompanied by isopullulanase activity from Arthrobacter globiformis T6. Agric. Biol. Chem. 52 (1988) 829-836
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 829-836
    • Okada, G.1    Takayanagi, T.2    Miyahara, S.3    Teruo, S.4
  • 27
    • 0026083734 scopus 로고
    • Purification and properties of an acid endo-1,4-beta-glucanase from Bacillus sp. KSM-330
    • Ozaki K., and Ito S. Purification and properties of an acid endo-1,4-beta-glucanase from Bacillus sp. KSM-330. J. Gen. Microbiol 137 (1991) 41-48
    • (1991) J. Gen. Microbiol , vol.137 , pp. 41-48
    • Ozaki, K.1    Ito, S.2
  • 28
    • 0029845535 scopus 로고    scopus 로고
    • Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae
    • Rao N.M., Kembhavi A.A., and Pant A. Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae. Biochem. J. 319 (1996) 159-164
    • (1996) Biochem. J. , vol.319 , pp. 159-164
    • Rao, N.M.1    Kembhavi, A.A.2    Pant, A.3
  • 29
    • 0022460629 scopus 로고
    • Requirement for two or more Erwinia carotovora subsp. Carotovora pectolytic gene products for Maceration of potato tuber tissue by Escherichia coli
    • Roberts D.P., Berman P.M., Allen C., Stromberg V.K., Lacy G.H., and Mount M.S. Requirement for two or more Erwinia carotovora subsp. Carotovora pectolytic gene products for Maceration of potato tuber tissue by Escherichia coli. J. Bacteriol. 167 (1986) 279-284
    • (1986) J. Bacteriol. , vol.167 , pp. 279-284
    • Roberts, D.P.1    Berman, P.M.2    Allen, C.3    Stromberg, V.K.4    Lacy, G.H.5    Mount, M.S.6
  • 30
    • 0002877656 scopus 로고
    • Pectinases and other cell wall degrading enzymes of industrial importance
    • Rombouts F.M., and Pilnik W. Pectinases and other cell wall degrading enzymes of industrial importance. Symbiosis 2 (1986) 79-90
    • (1986) Symbiosis , vol.2 , pp. 79-90
    • Rombouts, F.M.1    Pilnik, W.2
  • 31
    • 0027818642 scopus 로고
    • Pectin, pectinase, and protopectinase: production, properties, and applications
    • Sakai T., Sakamoto T., Hallaert J., and Vandamme E.J. Pectin, pectinase, and protopectinase: production, properties, and applications. Adv. Appl. Microbiol. 39 (1993) 213-294
    • (1993) Adv. Appl. Microbiol. , vol.39 , pp. 213-294
    • Sakai, T.1    Sakamoto, T.2    Hallaert, J.3    Vandamme, E.J.4
  • 33
    • 29144507093 scopus 로고    scopus 로고
    • Marked enhancement in the production of a highly alkaline and thermostable pectinase by Bacillus pumilus dcsr1 in submerged fermentation by using statistical methods
    • Sharma D.C., and Satyanarayana T.A. Marked enhancement in the production of a highly alkaline and thermostable pectinase by Bacillus pumilus dcsr1 in submerged fermentation by using statistical methods. Biores. Technol. 97 (2006) 727-731
    • (2006) Biores. Technol. , vol.97 , pp. 727-731
    • Sharma, D.C.1    Satyanarayana, T.A.2
  • 34
    • 0029081224 scopus 로고
    • Circular dichroism of the parallel β helical proteins pectate lyase C and E
    • Sieber V., Jurnak F., and Moe G.R. Circular dichroism of the parallel β helical proteins pectate lyase C and E. Protein Struct. Funct. Genet. 23 (1995) 32-37
    • (1995) Protein Struct. Funct. Genet. , vol.23 , pp. 32-37
    • Sieber, V.1    Jurnak, F.2    Moe, G.R.3
  • 37
    • 0033972605 scopus 로고    scopus 로고
    • An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization
    • Soriano M., Blanco A., Díaz P., and Pastor F.I.J. An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization. Microbiology 146 (2000) 89-95
    • (2000) Microbiology , vol.146 , pp. 89-95
    • Soriano, M.1    Blanco, A.2    Díaz, P.3    Pastor, F.I.J.4
  • 38
    • 77956994950 scopus 로고
    • Determination of the tryptophan content of proteins with N-bromosuccinimide
    • Spande T.F., and Witkop B. Determination of the tryptophan content of proteins with N-bromosuccinimide. Meth. Enzymol. 11 (1967) 498-506
    • (1967) Meth. Enzymol. , vol.11 , pp. 498-506
    • Spande, T.F.1    Witkop, B.2
  • 39
    • 0023250950 scopus 로고
    • Inducible thermoalkalophilic polygalacturonate lyase from Thermomonospora fusca
    • Stutzenberger F.J. Inducible thermoalkalophilic polygalacturonate lyase from Thermomonospora fusca. J. Bacteriol. 169 (1987) 2774-2780
    • (1987) J. Bacteriol. , vol.169 , pp. 2774-2780
    • Stutzenberger, F.J.1
  • 40
    • 0029075044 scopus 로고
    • A silver stain protocol for proteins yielding high resolution and transparent background in sodium dodecyl sulfate-polyacrylamide gels
    • Swain M., and Ross N.W. A silver stain protocol for proteins yielding high resolution and transparent background in sodium dodecyl sulfate-polyacrylamide gels. Electrophoresis 16 (1994) 948-951
    • (1994) Electrophoresis , vol.16 , pp. 948-951
    • Swain, M.1    Ross, N.W.2
  • 41
    • 0033931985 scopus 로고    scopus 로고
    • Characterization of atrazine-degrading Pseudaminobacter sp. isolated from Canadian and French agricultural soils
    • Topp E., Zhu H., Nour S.M., Houot S., Lewis M., and Cuppels D. Characterization of atrazine-degrading Pseudaminobacter sp. isolated from Canadian and French agricultural soils. Appl. Environ. Microbiol. 66 (2000) 2773-2782
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2773-2782
    • Topp, E.1    Zhu, H.2    Nour, S.M.3    Houot, S.4    Lewis, M.5    Cuppels, D.6
  • 42
    • 0027329090 scopus 로고
    • New domain motif: the structure of pectate lyase C, a secreted plant virulence factor
    • Yodder M.D., Keen N.T., and Jurnak F. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260 (1993) 1503-1507
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yodder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 43
    • 0035145669 scopus 로고    scopus 로고
    • Degumming of ramie fibers by alkalophilic bacteria and their polysaccharide-degrading enzymes
    • Zheng L., Du Y., and Zhang J. Degumming of ramie fibers by alkalophilic bacteria and their polysaccharide-degrading enzymes. Biores. Technol. 78 (2001) 89-94
    • (2001) Biores. Technol. , vol.78 , pp. 89-94
    • Zheng, L.1    Du, Y.2    Zhang, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.