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Volumn 15, Issue 3, 2008, Pages 453-463

Purification and characterization of exo-type cellouronate lyase

Author keywords

Biodegradation; Cellouronate; Glucuronan; Lyase; TEMPO

Indexed keywords

CHARACTERIZATION; DIMERS; MOLECULAR MASS; MONOMERS; OLIGOMERS; PROTEINS; PURIFICATION; SIZE EXCLUSION CHROMATOGRAPHY;

EID: 42649106856     PISSN: 09690239     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10570-007-9195-z     Document Type: Article
Times cited : (27)

References (35)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0030495331 scopus 로고    scopus 로고
    • Oxidation of primary alcohol groups of naturally occurring polysaccharides with 2,2,6,6,-tetramethyl-1-piperidine oxoammonium ion
    • Chang PS, Robyt JFJ (1996) Oxidation of primary alcohol groups of naturally occurring polysaccharides with 2,2,6,6,-tetramethyl-1-piperidine oxoammonium ion. Carbohydr Chem 15:819-830
    • (1996) Carbohydr Chem , vol.15 , pp. 819-830
    • Chang, P.S.1    Robyt, J.F.J.2
  • 5
    • 0037289904 scopus 로고    scopus 로고
    • Acetyl substitution of glucuronan influences glucuronan cleavage by GlyA from Shinorhizobium meliloti M5N1CS (NCIMB 40472)
    • Da Costa A, Michaud P, Heyraud A, Colin-Morel P, Courtois B, Courtois J (2003) Acetyl substitution of glucuronan influences glucuronan cleavage by GlyA from Shinorhizobium meliloti M5N1CS (NCIMB 40472). Carbohydr Polym 51:223-228
    • (2003) Carbohydr Polym , vol.51 , pp. 223-228
    • Da Costa, A.1    Michaud, P.2    Heyraud, A.3    Colin-Morel, P.4    Courtois, B.5    Courtois, J.6
  • 6
    • 23044485937 scopus 로고    scopus 로고
    • Production of glucuronan oligosaccharides using a new glucuronan lyase activity from a Trichoderma sp. strain
    • Delattre C, Michaud P, Lion JM, Courtois B, Courtois J (2005) Production of glucuronan oligosaccharides using a new glucuronan lyase activity from a Trichoderma sp. strain. J Biotechnol 118:448-457
    • (2005) J Biotechnol , vol.118 , pp. 448-457
    • Delattre, C.1    Michaud, P.2    Lion, J.M.3    Courtois, B.4    Courtois, J.5
  • 9
    • 0028929558 scopus 로고
    • Highly selective nitroxyl radical-mediated oxidation of primary alcohol groups in water-soluble glucans
    • de Nooy AEJ, Besemer AC, Bekkum H (1995) Highly selective nitroxyl radical-mediated oxidation of primary alcohol groups in water-soluble glucans. Carbohydr Res 269:89-98
    • (1995) Carbohydr Res , vol.269 , pp. 89-98
    • de Nooy, A.E.J.1    Besemer, A.C.2    Bekkum, H.3
  • 10
    • 0031664395 scopus 로고    scopus 로고
    • Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains
    • Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K (1998) Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains. Appl Environ Microbiol 64:3765-3768
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3765-3768
    • Hashimoto, W.1    Miki, H.2    Tsuchiya, N.3    Nankai, H.4    Murata, K.5
  • 11
    • 0033905713 scopus 로고    scopus 로고
    • Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate
    • Hashimoto W, Miyake O, Momma K, Kawai S, Murata K (2000) Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. J Bacteriol 182:4572-4577
    • (2000) J Bacteriol , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 12
    • 0035143725 scopus 로고    scopus 로고
    • Polysaccharide lyase: Molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1
    • Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K (2001) Polysaccharide lyase: Molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1. Appl Environ Microbiol 67:713-720
    • (2001) Appl Environ Microbiol , vol.67 , pp. 713-720
    • Hashimoto, W.1    Miki, H.2    Tsuchiya, N.3    Nankai, H.4    Murata, K.5
  • 13
    • 0027551659 scopus 로고
    • Structural characterization and rheological properties of an extracellular glucuronan produced by a Rhizobium meliloti M5N1 mutant strain
    • Heyraud A, Courtois J, Dantas L, Colin-Morel R, Courtois B (1993) Structural characterization and rheological properties of an extracellular glucuronan produced by a Rhizobium meliloti M5N1 mutant strain. Carbohydr Res 240:71-78
    • (1993) Carbohydr Res , vol.240 , pp. 71-78
    • Heyraud, A.1    Courtois, J.2    Dantas, L.3    Colin-Morel, R.4    Courtois, B.5
  • 14
    • 0000630381 scopus 로고    scopus 로고
    • Preparation of polyuronic acid from cellulose by TEMPO-mediated oxidation
    • Isogai A, Kato Y (1998) Preparation of polyuronic acid from cellulose by TEMPO-mediated oxidation. Cellulose 5:153-164
    • (1998) Cellulose , vol.5 , pp. 153-164
    • Isogai, A.1    Kato, Y.2
  • 16
    • 0037209419 scopus 로고    scopus 로고
    • Oxidation process of water-soluble starch in TEMPO-mediated system
    • Kato Y, Matsuo R, Isogai A (2003) Oxidation process of water-soluble starch in TEMPO-mediated system. Carbohydr Polym 51:69-75
    • (2003) Carbohydr Polym , vol.51 , pp. 69-75
    • Kato, Y.1    Matsuo, R.2    Isogai, A.3
  • 17
    • 9644268974 scopus 로고    scopus 로고
    • TEMPO-mediated oxidation of chitin, regenerated chitin and N-acetylated chitosan
    • Kato Y, Kaminaga J, Matsuo R, Isogai A (2004) TEMPO-mediated oxidation of chitin, regenerated chitin and N-acetylated chitosan. Carbohydr Polym 58:421-426
    • (2004) Carbohydr Polym , vol.58 , pp. 421-426
    • Kato, Y.1    Kaminaga, J.2    Matsuo, R.3    Isogai, A.4
  • 18
    • 24344508539 scopus 로고    scopus 로고
    • Oxygen permeability and biodegradability of polyuronic acids prepared from polysaccharides by TEMPO-mediated oxidation
    • Kato Y, Kaminaga J, Matsuo R, Isogai A (2005) Oxygen permeability and biodegradability of polyuronic acids prepared from polysaccharides by TEMPO-mediated oxidation. J Polym Environ 13:261-266
    • (2005) J Polym Environ , vol.13 , pp. 261-266
    • Kato, Y.1    Kaminaga, J.2    Matsuo, R.3    Isogai, A.4
  • 20
    • 27644594650 scopus 로고    scopus 로고
    • Characterization and mode of action of an exopolygalacturonase from the hyperthermophilic bacterium Thermotoga maritima
    • Kluskens LD, Van Alebeek GJWM, Walther J, Voragen AGJ, de Vos WM, van der Oost J (2005) Characterization and mode of action of an exopolygalacturonase from the hyperthermophilic bacterium Thermotoga maritima. FEBS J 272:5464-5473
    • (2005) FEBS J , vol.272 , pp. 5464-5473
    • Kluskens, L.D.1    Van Alebeek, G.J.W.M.2    Walther, J.3    Voragen, A.G.J.4    de Vos, W.M.5    van der Oost, J.6
  • 21
    • 33646858999 scopus 로고    scopus 로고
    • Cellouronate (β-1,4-linked polyglucuronate) lyase from Brevundimonas sp. SH203: purification and characterization
    • Konno N, Habu N, Maeda I, Azuma N, Isogai A (2006) Cellouronate (β-1,4-linked polyglucuronate) lyase from Brevundimonas sp. SH203: purification and characterization. Carbohydr Polym 64:589-596
    • (2006) Carbohydr Polym , vol.64 , pp. 589-596
    • Konno, N.1    Habu, N.2    Maeda, I.3    Azuma, N.4    Isogai, A.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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.1
  • 23
    • 33747181070 scopus 로고    scopus 로고
    • A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: Molecular identification of Atu3025 as an exotype family PL-15 alginate lyase
    • Ochiai A, Hashimoto W, Murata K (2006) A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: Molecular identification of Atu3025 as an exotype family PL-15 alginate lyase. Res Microbiol 157:642-649
    • (2006) Res Microbiol , vol.157 , pp. 642-649
    • Ochiai, A.1    Hashimoto, W.2    Murata, K.3
  • 24
    • 0037345228 scopus 로고    scopus 로고
    • Comparative characterization of bovine testicular hyaluronidase and a hyaluronate lyase from Streptococcus agalactiae in pharmaceutical preparations
    • Oettl M, Hoechstetter J, Asen I, Bernhardt G, Buschauer A (2003) Comparative characterization of bovine testicular hyaluronidase and a hyaluronate lyase from Streptococcus agalactiae in pharmaceutical preparations. Eur J Pharm Sci 18:267-277
    • (2003) Eur J Pharm Sci , vol.18 , pp. 267-277
    • Oettl, M.1    Hoechstetter, J.2    Asen, I.3    Bernhardt, G.4    Buschauer, A.5
  • 25
    • 33646045596 scopus 로고    scopus 로고
    • Purification and characterization of pectate lyase from banana (Musa acuminata) fruits
    • Payasi A, Misra PC, Sanwal GG (2006) Purification and characterization of pectate lyase from banana (Musa acuminata) fruits. Phytochemistry 67:861-869
    • (2006) Phytochemistry , vol.67 , pp. 861-869
    • Payasi, A.1    Misra, P.C.2    Sanwal, G.G.3
  • 26
    • 0032473875 scopus 로고    scopus 로고
    • Biochemical characterization of the pectate lyase PelZ of Erwinia chrysanthemi 3937
    • Pissavin C, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1998) Biochemical characterization of the pectate lyase PelZ of Erwinia chrysanthemi 3937. Biochim Biophys Acta 1383:188-196
    • (1998) Biochim Biophys Acta , vol.1383 , pp. 188-196
    • Pissavin, C.1    Robert-Baudouy, J.2    Hugouvieux-Cotte-Pattat, N.3
  • 27
    • 0034674165 scopus 로고    scopus 로고
    • Mechanism of hyaluronan binding and degradation: Structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 Å resolution
    • Ponnuraj K, Jedrzejas MJ (2000) Mechanism of hyaluronan binding and degradation: Structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 Å resolution. J Mol Biol 299:885-895
    • (2000) J Mol Biol , vol.299 , pp. 885-895
    • Ponnuraj, K.1    Jedrzejas, M.J.2
  • 28
    • 0032146735 scopus 로고    scopus 로고
    • Alginate lyase from Pseudomonas aeruginosa CF1/M1 prefers the hexameric oligomannuronate as substrate
    • Rehm BHA (1998) Alginate lyase from Pseudomonas aeruginosa CF1/M1 prefers the hexameric oligomannuronate as substrate. FEMS Microbiol Lett 165:175-180
    • (1998) FEMS Microbiol Lett , vol.165 , pp. 175-180
    • Rehm, B.H.A.1
  • 30
    • 0032988009 scopus 로고    scopus 로고
    • The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937
    • Shevchik VE, Condemine G, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1999b) The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J Bacteriol 181:3912-3919
    • (1999) J Bacteriol , vol.181 , pp. 3912-3919
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 31
    • 0037829154 scopus 로고    scopus 로고
    • Depolymerization of cellouronic acid during TEMPO-mediated oxidation
    • Shibata I, Isogai A (2003) Depolymerization of cellouronic acid during TEMPO-mediated oxidation. Cellulose 10:151-158
    • (2003) Cellulose , vol.10 , pp. 151-158
    • Shibata, I.1    Isogai, A.2
  • 32
    • 33645472471 scopus 로고    scopus 로고
    • SEC-MALS analysis of cellouronic acid prepared from regenerated cellulose by TEMPO-mediated oxidation
    • Shibata I, Yanagisawa M, Saito T, Isogai A (2006) SEC-MALS analysis of cellouronic acid prepared from regenerated cellulose by TEMPO-mediated oxidation. Cellulose 13:73-80
    • (2006) Cellulose , vol.13 , pp. 73-80
    • Shibata, I.1    Yanagisawa, M.2    Saito, T.3    Isogai, A.4
  • 33
    • 33744982423 scopus 로고    scopus 로고
    • A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner
    • Suzuki H, Suzuki K, Inoue A, Ojima T (2006) A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner. Carbohydr Res 341:1809-1819
    • (2006) Carbohydr Res , vol.341 , pp. 1809-1819
    • Suzuki, H.1    Suzuki, K.2    Inoue, A.3    Ojima, T.4
  • 34
    • 78651113725 scopus 로고
    • The formation of 2-keto-3-deoxyheptonic acid in extracts of Escherichia coli B
    • Weissbach A, Hurwitz J (1958) The formation of 2-keto-3-deoxyheptonic acid in extracts of Escherichia coli B. J Biol Chem 234:705-709
    • (1958) J Biol Chem , vol.234 , pp. 705-709
    • Weissbach, A.1    Hurwitz, J.2
  • 35
    • 0034084571 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases
    • Yoon HJ, Hashimoto W, Miyake O, Okamoto M, Miyake B, Murata K (2000) Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases. Protein Expr Purif 19:84-90
    • (2000) Protein Expr Purif , vol.19 , pp. 84-90
    • Yoon, H.J.1    Hashimoto, W.2    Miyake, O.3    Okamoto, M.4    Miyake, B.5    Murata, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.