메뉴 건너뛰기




Volumn 43, Issue 5, 2008, Pages 531-539

Production and chromatographic behaviour of polygalacturonase from Pleurotus ostreatus on immobilized metal chelates

Author keywords

Immobilized metal affinity chromatography; Lignocellulosic enzymes; Pleurotus ostreatus; Polygalacturonase; Production and purification; Tomato pomace

Indexed keywords

ADSORPTION; AFFINITY CHROMATOGRAPHY; CHELATION; ENZYME ACTIVITY;

EID: 41549156814     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.01.010     Document Type: Article
Times cited : (12)

References (39)
  • 1
    • 0034792201 scopus 로고    scopus 로고
    • Value of a tomato byproduct as a source of dietary fiber in rats
    • Alvarado A., Pacheco-Delahaye E., and Hevia P. Value of a tomato byproduct as a source of dietary fiber in rats. Plant Foods Hum Nutr 56 (2001) 335-348
    • (2001) Plant Foods Hum Nutr , vol.56 , pp. 335-348
    • Alvarado, A.1    Pacheco-Delahaye, E.2    Hevia, P.3
  • 2
    • 18944365242 scopus 로고    scopus 로고
    • Analyses of tomato peel and seed byproducts and their use as a source of carotenoids
    • Knoblich M., Anderson B., and Latshaw D. Analyses of tomato peel and seed byproducts and their use as a source of carotenoids. J Sci Food Agric 75 (2005) 1166-1170
    • (2005) J Sci Food Agric , vol.75 , pp. 1166-1170
    • Knoblich, M.1    Anderson, B.2    Latshaw, D.3
  • 3
    • 33745345816 scopus 로고    scopus 로고
    • Chemical characterization of tomato pomace
    • Valle M.D., Cámara M., and Torija M.E. Chemical characterization of tomato pomace. J Sci Food Agric 86 (2006) 1232-1236
    • (2006) J Sci Food Agric , vol.86 , pp. 1232-1236
    • Valle, M.D.1    Cámara, M.2    Torija, M.E.3
  • 5
    • 19344362684 scopus 로고    scopus 로고
    • Effect of cultural conditions on xylanase production by Streptomyces sp. (strain lb 24D) and its potential to utilize tomato pomace
    • Rawashdeh R., Saadoun I., and Mahasneh A. Effect of cultural conditions on xylanase production by Streptomyces sp. (strain lb 24D) and its potential to utilize tomato pomace. Afr J Biotechnol 4 (2005) 251-255
    • (2005) Afr J Biotechnol , vol.4 , pp. 251-255
    • Rawashdeh, R.1    Saadoun, I.2    Mahasneh, A.3
  • 7
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: a review
    • Jayani R.S., Saxena S., and Gupta R. Microbial pectinolytic enzymes: a review. Process Biochem 40 (2005) 2931-2944
    • (2005) Process Biochem , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 8
    • 0037899941 scopus 로고    scopus 로고
    • Purification and biochemical properties of microbial pectinases-a review
    • Gummadi S.N., and Panda T. Purification and biochemical properties of microbial pectinases-a review. Process Biochem 38 (2003) 987-996
    • (2003) Process Biochem , vol.38 , pp. 987-996
    • Gummadi, S.N.1    Panda, T.2
  • 9
    • 0031871445 scopus 로고    scopus 로고
    • Culture conditions for the production of pectinolytic enzymes by the white-rot fungus Coriolus troggi on a laboratory scale
    • Levin L., and Forchiassin F. Culture conditions for the production of pectinolytic enzymes by the white-rot fungus Coriolus troggi on a laboratory scale. Acta Biotechnol 18 (1998) 157-166
    • (1998) Acta Biotechnol , vol.18 , pp. 157-166
    • Levin, L.1    Forchiassin, F.2
  • 10
    • 33847718289 scopus 로고    scopus 로고
    • Immobilized metal-ion affinity chromatography: status and trends
    • Gutiérrez R., Valle E.M.M., and Galán M.A. Immobilized metal-ion affinity chromatography: status and trends. Sep Purif Rev 36 (2007) 71-111
    • (2007) Sep Purif Rev , vol.36 , pp. 71-111
    • Gutiérrez, R.1    Valle, E.M.M.2    Galán, M.A.3
  • 11
    • 0028830716 scopus 로고    scopus 로고
    • Study of variables involved in fungal pectic enzyme fractionation by immobilized metal ion affinity chromatography
    • Camperi S.A., Auday R.M., Canizo A.N., and Cascone O. Study of variables involved in fungal pectic enzyme fractionation by immobilized metal ion affinity chromatography. Process Biochem 31 (1996) 81-87
    • (1996) Process Biochem , vol.31 , pp. 81-87
    • Camperi, S.A.1    Auday, R.M.2    Canizo, A.N.3    Cascone, O.4
  • 12
    • 0033771057 scopus 로고    scopus 로고
    • High-speed enzyme fractionation by immobilised metal ion affinity membranes
    • Camperi S.A., Grasselli M., and Cascone O. High-speed enzyme fractionation by immobilised metal ion affinity membranes. Bioseparation 9 (2000) 173-177
    • (2000) Bioseparation , vol.9 , pp. 173-177
    • Camperi, S.A.1    Grasselli, M.2    Cascone, O.3
  • 13
    • 1942456637 scopus 로고    scopus 로고
    • Preparation and characterisation of immobilised metal ion hollow-fibre polysulphone membranes. Their application in high-speed pectic enzyme fractionation
    • Camperi S.A., Grasselli M., Smolko E.E., and Cascone O. Preparation and characterisation of immobilised metal ion hollow-fibre polysulphone membranes. Their application in high-speed pectic enzyme fractionation. Process Biochem 39 (2004) 1017-1024
    • (2004) Process Biochem , vol.39 , pp. 1017-1024
    • Camperi, S.A.1    Grasselli, M.2    Smolko, E.E.3    Cascone, O.4
  • 14
    • 34249853843 scopus 로고    scopus 로고
    • Separation and utilization of pectin lyase from commercial pectic enzyme via highly methoxylated cross-linked alcohol-insoluble solid chromatography for wine methanol reduction
    • Wu M.C., Jiang C.M., Huang P.H., Wu M.Y., and Wang Y.T. Separation and utilization of pectin lyase from commercial pectic enzyme via highly methoxylated cross-linked alcohol-insoluble solid chromatography for wine methanol reduction. J Agric Food Chem 55 (2007) 1557-1562
    • (2007) J Agric Food Chem , vol.55 , pp. 1557-1562
    • Wu, M.C.1    Jiang, C.M.2    Huang, P.H.3    Wu, M.Y.4    Wang, Y.T.5
  • 16
    • 0000717689 scopus 로고
    • Glucose oxidase: assay method
    • Bergmeyer H.U. (Ed), Academic Press, New York
    • Bergmeyer H.U. Glucose oxidase: assay method. In: Bergmeyer H.U. (Ed). Methods of enzymatic analysis vol. 1 (1974), Academic Press, New York 457-460
    • (1974) Methods of enzymatic analysis , vol.1 , pp. 457-460
    • Bergmeyer, H.U.1
  • 17
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanases activity
    • Bailey M.J., Biely P., and Poutanen K. Interlaboratory testing of methods for assay of xylanases activity. J Biotechnol 23 (1992) 257-270
    • (1992) J Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 18
    • 0032982259 scopus 로고    scopus 로고
    • Selective adsorption of poly-His tagged glutarul acylase on tailormade metal chelate supports
    • Armisén P., Mateo C., Cortés E., Barredo J.L., Salto F., Diez B., et al. Selective adsorption of poly-His tagged glutarul acylase on tailormade metal chelate supports. J Chromatogr A 848 (1999) 61-70
    • (1999) J Chromatogr A , vol.848 , pp. 61-70
    • Armisén, P.1    Mateo, C.2    Cortés, E.3    Barredo, J.L.4    Salto, F.5    Diez, B.6
  • 19
    • 33747324824 scopus 로고    scopus 로고
    • Screening of suitable immobilized metal chelates for adsorption of monoclonal antibodies against mutant amidase from Pseudomonas aeruginosa
    • Martins S., Andrade J., Karmali A., and Serralheiro M.L. Screening of suitable immobilized metal chelates for adsorption of monoclonal antibodies against mutant amidase from Pseudomonas aeruginosa. J Mol Recognit 19 (2006) 340-347
    • (2006) J Mol Recognit , vol.19 , pp. 340-347
    • Martins, S.1    Andrade, J.2    Karmali, A.3    Serralheiro, M.L.4
  • 20
    • 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
  • 21
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins. RNA and DNA in polyacrylamide gels
    • Bloom H., Beier H., and Gross H.S. Improved silver staining of plant proteins. RNA and DNA in polyacrylamide gels. Electrophoresis 8 (1987) 93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Bloom, H.1    Beier, H.2    Gross, H.S.3
  • 22
    • 0025030207 scopus 로고
    • Relationship of cellulosomal and noncellulosomal xylanases of Clostridium thermocellum to cellulose-degrading enzymes
    • Morag E., Bayer E.A., and Lamed R. Relationship of cellulosomal and noncellulosomal xylanases of Clostridium thermocellum to cellulose-degrading enzymes. J Bacteriol 172 (1990) 6098-6105
    • (1990) J Bacteriol , vol.172 , pp. 6098-6105
    • Morag, E.1    Bayer, E.A.2    Lamed, R.3
  • 23
    • 0022344608 scopus 로고
    • Activity stain for rapid characterization of pectic enzymes in isoelectric focusing and sodium dodecyl sulphate-polyacrylamide gels
    • Ried L.L., and Collmer A. Activity stain for rapid characterization of pectic enzymes in isoelectric focusing and sodium dodecyl sulphate-polyacrylamide gels. Appl Environ Microbiol 50 (1985) 615-622
    • (1985) Appl Environ Microbiol , vol.50 , pp. 615-622
    • Ried, L.L.1    Collmer, A.2
  • 24
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • Hames B.D., and Rickwood D. (Eds), IRL Press, Oxford
    • Hames B.D. An introduction to polyacrylamide gel electrophoresis. In: Hames B.D., and Rickwood D. (Eds). Gel electrophoresis of proteins (1981), IRL Press, Oxford 1-86
    • (1981) Gel electrophoresis of proteins , pp. 1-86
    • Hames, B.D.1
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0030917107 scopus 로고    scopus 로고
    • Growth conditions of Aspergillus sp. ATHUM-3482 for polygalacturonase production
    • Galiotou-Panayotou M., Kapantai M., and Kalantzi O. Growth conditions of Aspergillus sp. ATHUM-3482 for polygalacturonase production. Appl Microbiol Biotechnol 47 (1997) 425-429
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 425-429
    • Galiotou-Panayotou, M.1    Kapantai, M.2    Kalantzi, O.3
  • 27
    • 0032589464 scopus 로고    scopus 로고
    • 1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis
    • Santen Y., Kalk K.H., and Dijkstra B.W. 1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J Biol Chem 274 (1999) 30474-30480
    • (1999) J Biol Chem , vol.274 , pp. 30474-30480
    • Santen, Y.1    Kalk, K.H.2    Dijkstra, B.W.3
  • 28
    • 0242457394 scopus 로고    scopus 로고
    • Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger
    • Pouderoyen G., Snijder H.J., Benen J.A., and Dijkstra B.W. Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Lett 554 (2003) 462-466
    • (2003) FEBS Lett , vol.554 , pp. 462-466
    • Pouderoyen, G.1    Snijder, H.J.2    Benen, J.A.3    Dijkstra, B.W.4
  • 29
    • 0035818608 scopus 로고    scopus 로고
    • Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)
    • Federici L., Caprari C., Mattei B., Savini C., Matteo A.D., Lorenzo G.D., et al. Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein). Proc Natl Acad Sci U S A 98 (2001) 13425-13430
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13425-13430
    • Federici, L.1    Caprari, C.2    Mattei, B.3    Savini, C.4    Matteo, A.D.5    Lorenzo, G.D.6
  • 30
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Porath J. Immobilized metal ion affinity chromatography. Protein Expr Purif 3 (1992) 1-7
    • (1992) Protein Expr Purif , vol.3 , pp. 1-7
    • Porath, J.1
  • 31
    • 0028157408 scopus 로고
    • Multiple-site binding interactions in metal-affinity chromatography. I. Equilibrium binding of engineered histidine-containing cytochromes c
    • Todd R.J., Johnson D., and Arnold F.H. Multiple-site binding interactions in metal-affinity chromatography. I. Equilibrium binding of engineered histidine-containing cytochromes c. J Chromatogr A 662 (1994) 13-26
    • (1994) J Chromatogr A , vol.662 , pp. 13-26
    • Todd, R.J.1    Johnson, D.2    Arnold, F.H.3
  • 32
    • 1942424126 scopus 로고    scopus 로고
    • Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
    • Esquivel J.C.C., and Voget C.E. Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii. J Biotechnol 110 (2004) 21-28
    • (2004) J Biotechnol , vol.110 , pp. 21-28
    • Esquivel, J.C.C.1    Voget, C.E.2
  • 33
    • 0027402236 scopus 로고
    • Isolation and characterization of an endopolygalacturonase from Penicillium pinophilum
    • Shanley N.A., Broek L.A.M., Voragen A.G.J., and Coughlan M.P. Isolation and characterization of an endopolygalacturonase from Penicillium pinophilum. J Biotechnol 28 (1993) 179-197
    • (1993) J Biotechnol , vol.28 , pp. 179-197
    • Shanley, N.A.1    Broek, L.A.M.2    Voragen, A.G.J.3    Coughlan, M.P.4
  • 35
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinases in the commercial sector: a review
    • Kashyap D.R., Vohra P.K., Chopra S., and Tewari R. Applications of pectinases in the commercial sector: a review. Bioresour Technol 77 (2001) 215-227
    • (2001) Bioresour Technol , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 36
    • 34547512141 scopus 로고    scopus 로고
    • Enzymes with new biochemical properties in the pectinolytic complex produced by Aspergillus niger MIUG 16
    • Dinu D., Nechifor M.T., Stoian G., Costache M., and Dinischiotu A. Enzymes with new biochemical properties in the pectinolytic complex produced by Aspergillus niger MIUG 16. J Biotechnol 131 (2007) 128-137
    • (2007) J Biotechnol , vol.131 , pp. 128-137
    • Dinu, D.1    Nechifor, M.T.2    Stoian, G.3    Costache, M.4    Dinischiotu, A.5
  • 37
    • 0036208545 scopus 로고    scopus 로고
    • A simple fractionation protocol for, and a comprehensive study of the molecular properties of two major endopolygalacturonases from Aspergillus níger
    • Singh S.A., and Rao A.G.A. A simple fractionation protocol for, and a comprehensive study of the molecular properties of two major endopolygalacturonases from Aspergillus níger. Biotechnol Appl Biochem 35 (2002) 115-123
    • (2002) Biotechnol Appl Biochem , vol.35 , pp. 115-123
    • Singh, S.A.1    Rao, A.G.A.2
  • 38
    • 0033083712 scopus 로고    scopus 로고
    • Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I. II and C
    • Benen J.A., Kester H.C., and Visser J. Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I. II and C. Eur J Biochem 259 (1999) 577-585
    • (1999) Eur J Biochem , vol.259 , pp. 577-585
    • Benen, J.A.1    Kester, H.C.2    Visser, J.3
  • 39
    • 0001061012 scopus 로고
    • Some properties of endo-polygalacturonase from Trichosporon penicillatum SNO-3
    • Sakai T., Okushima M., and Sawada M. Some properties of endo-polygalacturonase from Trichosporon penicillatum SNO-3. Agric Biol Chem 46 (1982) 2223-2231
    • (1982) Agric Biol Chem , vol.46 , pp. 2223-2231
    • Sakai, T.1    Okushima, M.2    Sawada, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.