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Volumn 28, Issue 2, 2006, Pages 161-166

Purification of potato polyphenol oxidase (PPO) by partitioning in aqueous two-phase system

Author keywords

Aqueous two phase systems; Downstream processing; Enzyme purification; Polyphenol oxidase; Protein recovery

Indexed keywords

DERIVATIVES; MOLECULAR WEIGHT; PHASE COMPOSITION; PHENOLS; PLANTS (BOTANY);

EID: 31944444062     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2005.10.006     Document Type: Article
Times cited : (55)

References (30)
  • 2
    • 0023645287 scopus 로고
    • Chemical and enzymatic oxidation of 4-methylcatechol in the presence and absence of l-serine. Spectrophotometric determination of intermediates
    • J. Cabanes, F. Garcia-Canovas, and F. Garcia-Carmona Chemical and enzymatic oxidation of 4-methylcatechol in the presence and absence of l-serine. Spectrophotometric determination of intermediates Biochim. Biophys. Acta 917 1994 190 197
    • (1994) Biochim. Biophys. Acta , vol.917 , pp. 190-197
    • Cabanes, J.1    Garcia-Canovas, F.2    Garcia-Carmona, F.3
  • 3
    • 0001003175 scopus 로고    scopus 로고
    • Improvement of a continuous spectrophotometric method for determining the monophenolase and diphenolase activities for mushroom polyphenol oxidase
    • J.C. Espin, M. Morales, P.A. Garcia-Ruiz, J. Tudela, and F. Garcia-Canovas Improvement of a continuous spectrophotometric method for determining the monophenolase and diphenolase activities for mushroom polyphenol oxidase J. Agric. Food Chem. 45 1997 1084 1090
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1084-1090
    • Espin, J.C.1    Morales, M.2    Garcia-Ruiz, P.A.3    Tudela, J.4    Garcia-Canovas, F.5
  • 5
    • 0028140296 scopus 로고
    • A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone
    • J.N. Rodriquez-Lopez, J. Escribano, and F. Garcia-Canovas A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone Anal. Biochem. 216 1994 205 212
    • (1994) Anal. Biochem. , vol.216 , pp. 205-212
    • Rodriquez-Lopez, J.N.1    Escribano, J.2    Garcia-Canovas, F.3
  • 6
    • 0032031332 scopus 로고    scopus 로고
    • Production of l-DOPA from tyrosinase immobilized on nylon 6,6: Enzyme stability and scale-up
    • P. Pialis, and B.A. Saville Production of l-DOPA from tyrosinase immobilized on nylon 6,6: enzyme stability and scale-up Enzyme Microb. Technol. 22 1998 261 268
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 261-268
    • Pialis, P.1    Saville, B.A.2
  • 7
    • 0002817727 scopus 로고    scopus 로고
    • Preparative scale production of 3-substituted catechols using a novel monooxygenase from Pseudomonas azelaica HBP-1
    • M. Held, W. Suske, A. Schmid, K.-H. Engesser, H.-P.E. Kohler, and M.G. Wubbolts Preparative scale production of 3-substituted catechols using a novel monooxygenase from Pseudomonas azelaica HBP-1 J. Mol. Catal. B: Enzym. 5 1998 87 93
    • (1998) J. Mol. Catal. B: Enzym. , vol.5 , pp. 87-93
    • Held, M.1    Suske, W.2    Schmid, A.3    Engesser, K.-H.4    Kohler, H.-P.E.5    Wubbolts, M.G.6
  • 8
    • 0021348334 scopus 로고
    • The chemistry and biology of ringfluorinated biogenic amines
    • K.L. Kirk, and C.R. Creveling The chemistry and biology of ringfluorinated biogenic amines Med. Res. Rev. 4 1984 189 220
    • (1984) Med. Res. Rev. , vol.4 , pp. 189-220
    • Kirk, K.L.1    Creveling, C.R.2
  • 9
    • 0026561211 scopus 로고
    • Laccase-based biosensor for determination of polyphenols: Determination of catechols in tea
    • A.L. Ghindilis, V.P. Gavrilova, and A.I. Yaropolov Laccase-based biosensor for determination of polyphenols: determination of catechols in tea Biosens. Bioelectron. 7 1992 127 131
    • (1992) Biosens. Bioelectron. , vol.7 , pp. 127-131
    • Ghindilis, A.L.1    Gavrilova, V.P.2    Yaropolov, A.I.3
  • 10
    • 0032920461 scopus 로고    scopus 로고
    • Biosensor for phenol based on the direct electron transfer blocking of peroxidase immobilising on silica-titanium
    • S.S. Rosatto, L.T. Kubota, and G. Oliveira-Neto Biosensor for phenol based on the direct electron transfer blocking of peroxidase immobilising on silica-titanium Anal. Chim. Acta 390 1999 65 72
    • (1999) Anal. Chim. Acta , vol.390 , pp. 65-72
    • Rosatto, S.S.1    Kubota, L.T.2    Oliveira-Neto, G.3
  • 11
    • 0037158219 scopus 로고    scopus 로고
    • Development of laccase based flow injection electrochemical biosensor for the determination of phenolic compounds and its application for monitering remediation of Kraft E1 paper mill effluent
    • R.S. Freire, N. Duran, and L.T. Kubota Development of laccase based flow injection electrochemical biosensor for the determination of phenolic compounds and its application for monitering remediation of Kraft E1 paper mill effluent Anal. Chim. Acta 463 2002 229 238
    • (2002) Anal. Chim. Acta , vol.463 , pp. 229-238
    • Freire, R.S.1    Duran, N.2    Kubota, L.T.3
  • 12
    • 0001121260 scopus 로고
    • Purification of d'anjou pear (Pyrus communis L.) polyphenol oxidase
    • K.W. Wissemann, and M.W. Montgomery Purification of d'anjou pear (Pyrus communis L.) polyphenol oxidase Plant Physiol. 78 1985 256
    • (1985) Plant Physiol. , vol.78 , pp. 256
    • Wissemann, K.W.1    Montgomery, M.W.2
  • 13
    • 0042368949 scopus 로고    scopus 로고
    • Purification of a polyphenol oxidase isoform from potato (Solanum tuberosum) tubers
    • C. Marri, A. Frazzoli, A. Hochkoeppler, and V. Poggi Purification of a polyphenol oxidase isoform from potato (Solanum tuberosum) tubers Phytochemistry 63 2003 745 752
    • (2003) Phytochemistry , vol.63 , pp. 745-752
    • Marri, C.1    Frazzoli, A.2    Hochkoeppler, A.3    Poggi, V.4
  • 14
    • 0030208645 scopus 로고    scopus 로고
    • Purification of polyphenol oxidase free of the storage protein patatin from potato tuber
    • J.C. Partington, and G.P. Bolwell Purification of polyphenol oxidase free of the storage protein patatin from potato tuber Phytochemistry 42 1996 1499 1502
    • (1996) Phytochemistry , vol.42 , pp. 1499-1502
    • Partington, J.C.1    Bolwell, G.P.2
  • 15
    • 38249037033 scopus 로고
    • Fractionation of Jerusalem artichoke phenolase by immobilized copper affinity chromatography
    • J. Zawistowski, R.J. Weselake, G. Blank, and E.D. Murray Fractionation of Jerusalem artichoke phenolase by immobilized copper affinity chromatography Phytochemistry 26 1987 2905 2907
    • (1987) Phytochemistry , vol.26 , pp. 2905-2907
    • Zawistowski, J.1    Weselake, R.J.2    Blank, G.3    Murray, E.D.4
  • 16
    • 0001624237 scopus 로고
    • Purification and characterization of polyphenol oxidase from glandular trichomes of Solanum berthaultii
    • S.P. Kowalski, N.T. Eanetta, A.L. Hirzel, and J.C. Steffens Purification and characterization of polyphenol oxidase from glandular trichomes of Solanum berthaultii Plant Physiol. 100 1992 677
    • (1992) Plant Physiol. , vol.100 , pp. 677
    • Kowalski, S.P.1    Eanetta, N.T.2    Hirzel, A.L.3    Steffens, J.C.4
  • 17
    • 0028103419 scopus 로고
    • Affinity purification and properties of polyphenoloxidase from Solanum tuberosum
    • S.U. Pathak, and V.S. Ghole Affinity purification and properties of polyphenoloxidase from Solanum tuberosum Phytochemistry 36 5 1994 1165 1167
    • (1994) Phytochemistry , vol.36 , Issue.5 , pp. 1165-1167
    • Pathak, S.U.1    Ghole, V.S.2
  • 19
    • 0022093396 scopus 로고
    • Amylase production in aqueous two-phase system with Bacillus subtilis
    • E. Andersson, A. Johansson, and G.B. Hagerdal Amylase production in aqueous two-phase system with Bacillus subtilis Enzyme Microb. Technol. 7 1985 333 338
    • (1985) Enzyme Microb. Technol. , vol.7 , pp. 333-338
    • Andersson, E.1    Johansson, A.2    Hagerdal, G.B.3
  • 21
    • 0031059018 scopus 로고    scopus 로고
    • Partitioning of amino acids by aqueous two-phase systems combined with temperature induced phase formation
    • M. Li, Z.Q. Zhu, and L.H. Mei Partitioning of amino acids by aqueous two-phase systems combined with temperature induced phase formation Biotechnol. Prog. 13 1997 105 108
    • (1997) Biotechnol. Prog. , vol.13 , pp. 105-108
    • Li, M.1    Zhu, Z.Q.2    Mei, L.H.3
  • 23
    • 0032738472 scopus 로고    scopus 로고
    • Extraction and purification of a plant peroxidase by aqueous two-phase extraction coupled with gel filtration
    • N.D. Srinivas, K.R. Rashmi, and K.S.M.S. Raghavarao Extraction and purification of a plant peroxidase by aqueous two-phase extraction coupled with gel filtration Process Biochem. 35 1999 43 48
    • (1999) Process Biochem. , vol.35 , pp. 43-48
    • Srinivas, N.D.1    Rashmi, K.R.2    Raghavarao, K.S.M.S.3
  • 25
    • 2642511370 scopus 로고    scopus 로고
    • Bromelain partitioning in two-phase aqueous systems containing PEO-PPO-PEO block copolymers
    • A.P.B. Rabelo, E.B. Tambourgi, and A. Pessoa Jr. Bromelain partitioning in two-phase aqueous systems containing PEO-PPO-PEO block copolymers J. Chromatogr. B 807 2004 61 68
    • (2004) J. Chromatogr. B , vol.807 , pp. 61-68
    • Rabelo, A.P.B.1    Tambourgi, E.B.2    Pessoa Jr., A.3
  • 26
    • 0027976435 scopus 로고
    • Application of temperature-induced phase partitioning at ambient temperature for enzyme purification
    • P.A. Alred, A. Kozlowski, J. Milton Harris, and F. Tjerneld Application of temperature-induced phase partitioning at ambient temperature for enzyme purification J. Chromatogr. A 659 1994 289 298
    • (1994) J. Chromatogr. a , vol.659 , pp. 289-298
    • Alred, P.A.1    Kozlowski, A.2    Milton Harris, J.3    Tjerneld, F.4
  • 27
    • 0034705702 scopus 로고    scopus 로고
    • Extraction in aqueous two-phase systems of alkaline xylanase produced by Bacillus pumilus and its application in kraft pulp bleaching
    • M.A. Bim, and T.T. Franco Extraction in aqueous two-phase systems of alkaline xylanase produced by Bacillus pumilus and its application in kraft pulp bleaching J. Chromatogr. B 743 2000 349 356
    • (2000) J. Chromatogr. B , vol.743 , pp. 349-356
    • Bim, M.A.1    Franco, T.T.2
  • 28
    • 0030569905 scopus 로고    scopus 로고
    • Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: Effect of surface hydrophobicity
    • T.T. Franco, A.T. Andrews, and J.A. Asenjo Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: effect of surface hydrophobicity Biotech. Bioeng. 49 1996 300 308
    • (1996) Biotech. Bioeng. , vol.49 , pp. 300-308
    • Franco, T.T.1    Andrews, A.T.2    Asenjo, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.