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Volumn 67, Issue 6, 2005, Pages 778-788

Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; BIODEGRADATION; CARBOXYLIC ACIDS; EMULSIFICATION; FERMENTATION; FUNGI; ORGANIC POLYMERS; PLASTICS;

EID: 21344469738     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1853-6     Document Type: Article
Times cited : (202)

References (56)
  • 1
    • 0032108797 scopus 로고    scopus 로고
    • Biodegradability of poly (tetramethylene succinate-co-tetramethylene adipate). I. Enzymatic hydrolysis
    • Ando Y, Yoshikawa K, Yoshikawa T, Nishioka M, Ishioka R, Yakabe Y (1998) Biodegradability of poly (tetramethylene succinate-co-tetramethylene adipate). I. Enzymatic hydrolysis. Polym Degrad Stabil 61:129-137
    • (1998) Polym Degrad Stabil , vol.61 , pp. 129-137
    • Ando, Y.1    Yoshikawa, K.2    Yoshikawa, T.3    Nishioka, M.4    Ishioka, R.5    Yakabe, Y.6
  • 4
    • 0018721369 scopus 로고
    • Substrate inhibition
    • Cleland WW (1979) Substrate inhibition. Methods Enzymol 63:500-513
    • (1979) Methods Enzymol , vol.63 , pp. 500-513
    • Cleland, W.W.1
  • 6
    • 0033646650 scopus 로고    scopus 로고
    • Fusarium solani pisi cutinase
    • Egmond MR, de Vlieg J (2000) Fusarium solani pisi cutinase. Biochimie 82:1015-1021
    • (2000) Biochimie , vol.82 , pp. 1015-1021
    • Egmond, M.R.1    De Vlieg, J.2
  • 7
  • 8
    • 0018727624 scopus 로고
    • Use of competitive inhibitors to study substrate binding order
    • Fromm HJ (1979) Use of competitive inhibitors to study substrate binding order. Methods Enzymol 63:467-486
    • (1979) Methods Enzymol , vol.63 , pp. 467-486
    • Fromm, H.J.1
  • 9
    • 0031599284 scopus 로고    scopus 로고
    • Processability and properties of aliphatic polyesters, 'BIONOLLE', synthesized by polycondensation reaction
    • Fujimaki T (1998) Processability and properties of aliphatic polyesters, 'BIONOLLE', synthesized by polycondensation reaction. Polym Degrad Stabil 59:209-214
    • (1998) Polym Degrad Stabil , vol.59 , pp. 209-214
    • Fujimaki, T.1
  • 10
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: Progress, limitations and prospects
    • Gouka RJ, Punt PJ, van den Hondel CA (1997) Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl Microbiol Biotechnol 47:1-11
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    Van Den Hondel, C.A.3
  • 11
    • 0032610014 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding the laccase from Schizophyllum commune
    • Hatamoto O, Sekine H, Nakano E, Abe K (1999) Cloning and expression of a cDNA encoding the laccase from Schizophyllum commune. Biosci Biotechnol Biochem 63:58-64
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 58-64
    • Hatamoto, O.1    Sekine, H.2    Nakano, E.3    Abe, K.4
  • 12
    • 0035862440 scopus 로고    scopus 로고
    • Induction of cutinolytic esterase activity during saprophytic growth of cucurbit pathogens, Fusarium solani fsp. cucurbitae races one and two (Nectria haematococca MPI and MPV, respectively)
    • Hawthorne BT, Rees-George J, Crowhurst RN (2001) Induction of cutinolytic esterase activity during saprophytic growth of cucurbit pathogens, Fusarium solani fsp. cucurbitae races one and two (Nectria haematococca MPI and MPV, respectively). FEMS Microbiol Lett 194:135-141
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 135-141
    • Hawthorne, B.T.1    Rees-George, J.2    Crowhurst, R.N.3
  • 13
    • 0025145811 scopus 로고
    • Microsequencing of proteins electrotransferred onto immobilizing matrices from polyacrylamide gel electrophoresis: Application to an insoluble protein
    • Hirano H, Watanabe T (1990) Microsequencing of proteins electrotransferred onto immobilizing matrices from polyacrylamide gel electrophoresis: application to an insoluble protein. Electrophoresis 11:573-580
    • (1990) Electrophoresis , vol.11 , pp. 573-580
    • Hirano, H.1    Watanabe, T.2
  • 14
    • 0000713852 scopus 로고
    • Polymer waste management-biodegradation, incineration, and recycling
    • Huang SJ (1995) Polymer waste management-biodegradation, incineration, and recycling. J Macromol Sci Pure A 32:593-597
    • (1995) J Macromol Sci Pure A , vol.32 , pp. 593-597
    • Huang, S.J.1
  • 15
  • 16
    • 0034849347 scopus 로고    scopus 로고
    • Biodegradation of poly (tetramethylene succinate-co-tetramethylene adipate) and poly (tetramethylene succinate) through water-soluble products
    • Kitakuni E, Yoshikawa K, Nakano K, Sasuga J, Nobiki M, Naoi H, Yokota Y, Ishioka R, Yakabe Y (2001) Biodegradation of poly (tetramethylene succinate-co-tetramethylene adipate) and poly (tetramethylene succinate) through water-soluble products. Environ Toxicol Chem 20:941-946
    • (2001) Environ Toxicol Chem , vol.20 , pp. 941-946
    • Kitakuni, E.1    Yoshikawa, K.2    Nakano, K.3    Sasuga, J.4    Nobiki, M.5    Naoi, H.6    Yokota, Y.7    Ishioka, R.8    Yakabe, Y.9
  • 17
    • 0031804477 scopus 로고    scopus 로고
    • Biodegradation of aliphatic-aromatic copolyesters by Thermomonospora fusca and other thermophilic compost isolates
    • Kleeberg I, Hetz C, Kroppenstedt RM, Muller RJ, Deckwer WD (1998) Biodegradation of aliphatic-aromatic copolyesters by Thermomonospora fusca and other thermophilic compost isolates. Appl Environ Microbiol 64:1731-1735
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1731-1735
    • Kleeberg, I.1    Hetz, C.2    Kroppenstedt, R.M.3    Muller, R.J.4    Deckwer, W.D.5
  • 18
    • 0021159573 scopus 로고
    • Detection of an N-terminal glucuronamide linkage in proteins
    • Kolattukudy PE (1984) Detection of an N-terminal glucuronamide linkage in proteins. Methods Enzymol 106:210-217
    • (1984) Methods Enzymol , vol.106 , pp. 210-217
    • Kolattukudy, P.E.1
  • 20
    • 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
  • 21
    • 0017607681 scopus 로고
    • Glucuronyl glycine, a novel N-terminus in a glycoprotein
    • Lin TS, Kolattukudy PE (1977) Glucuronyl glycine, a novel N-terminus in a glycoprotein. Biochem Biophys Res Commun 75:87-93
    • (1977) Biochem Biophys Res Commun , vol.75 , pp. 87-93
    • Lin, T.S.1    Kolattukudy, P.E.2
  • 22
    • 0019012501 scopus 로고
    • Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus
    • Lin TS, Kolattukudy PE (1980) Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus. Eur J Biochem 106:341-351
    • (1980) Eur J Biochem , vol.106 , pp. 341-351
    • Lin, T.S.1    Kolattukudy, P.E.2
  • 23
    • 0031574909 scopus 로고    scopus 로고
    • Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: Stereochemical analysis
    • Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C (1997a) Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. J Mol Biol 268:779-799
    • (1997) J Mol Biol , vol.268 , pp. 779-799
    • Longhi, S.1    Czjzek, M.2    Lamzin, V.3    Nicolas, A.4    Cambillau, C.5
  • 26
    • 0036360821 scopus 로고    scopus 로고
    • Progress of Aspergillus oryzae genomics
    • Machida M (2002) Progress of Aspergillus oryzae genomics. Adv Appl Microbiol 51:81-106
    • (2002) Adv Appl Microbiol , vol.51 , pp. 81-106
    • Machida, M.1
  • 28
    • 0029065498 scopus 로고
    • Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity
    • Mannesse ML, Cox RC, Koops BC, Verheij HM, de Haas GH, Egmond MR, van der Hijden HT, de Vlieg J (1995) Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity. Biochemistry 34:6400-6407
    • (1995) Biochemistry , vol.34 , pp. 6400-6407
    • Mannesse, M.L.1    Cox, R.C.2    Koops, B.C.3    Verheij, H.M.4    De Haas, G.H.5    Egmond, M.R.6    Van Der Hijden, H.T.7    De Vlieg, J.8
  • 29
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C (1992) Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356:615-618
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 30
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262:10035-10038
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 31
    • 0001374815 scopus 로고
    • Biodegradable materials: Balancing degradability and performance
    • Mayer JM, Kaplin DL (1994) Biodegradable materials: balancing degradability and performance. Trends Polym Sci 2:227-235
    • (1994) Trends Polym Sci , vol.2 , pp. 227-235
    • Mayer, J.M.1    Kaplin, D.L.2
  • 33
    • 0035158548 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular poly(L-lactic acid) depolymerase from a soil isolate, Amycolatopsis sp. strain K104-1
    • Nakamura K, Tomita T, Abe N, Kamio Y (2001) Purification and characterization of an extracellular poly(L-lactic acid) depolymerase from a soil isolate, Amycolatopsis sp. strain K104-1. Appl Environ Microbiol 67:345-353
    • (2001) Appl Environ Microbiol , vol.67 , pp. 345-353
    • Nakamura, K.1    Tomita, T.2    Abe, N.3    Kamio, Y.4
  • 35
    • 0028567747 scopus 로고
    • Purification and characterization of a novel lipolytic enzyme from Aspergillus oryzae
    • Ohnishi K, Yoshida Y, Toida J, Sekiguchi J (1994) Purification and characterization of a novel lipolytic enzyme from Aspergillus oryzae. J Ferment Bioeng 78:413-419
    • (1994) J Ferment Bioeng , vol.78 , pp. 413-419
    • Ohnishi, K.1    Yoshida, Y.2    Toida, J.3    Sekiguchi, J.4
  • 36
    • 0028883212 scopus 로고
    • Genome structure and nucleotide sequence of a lipolytic enzyme gene of Aspergillus oryzae
    • Ohnishi K, Toida J, Nakazawa H, Sekiguchi J (1995) Genome structure and nucleotide sequence of a lipolytic enzyme gene of Aspergillus oryzae. FEMS Microbiol Lett 126:145-150
    • (1995) FEMS Microbiol Lett , vol.126 , pp. 145-150
    • Ohnishi, K.1    Toida, J.2    Nakazawa, H.3    Sekiguchi, J.4
  • 39
    • 0016694722 scopus 로고
    • Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi
    • Purdy RE, Kolattukudy PE (1975a) Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi. Biochemistry 14:2832-2840
    • (1975) Biochemistry , vol.14 , pp. 2832-2840
    • Purdy, R.E.1    Kolattukudy, P.E.2
  • 40
    • 0016682066 scopus 로고
    • Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi
    • Purdy RE, Kolattukudy PE (1975b) Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 14:2824-2831
    • (1975) Biochemistry , vol.14 , pp. 2824-2831
    • Purdy, R.E.1    Kolattukudy, P.E.2
  • 41
    • 0018727622 scopus 로고
    • Product inhibition and abortive complex formation
    • Rudolph FB (1979) Product inhibition and abortive complex formation. Methods Enzymol 63:411-436
    • (1979) Methods Enzymol , vol.63 , pp. 411-436
    • Rudolph, F.B.1
  • 42
    • 0018690805 scopus 로고
    • Plotting methods for analyzing enzyme rate data
    • Rudolph FB, Fromm HJ (1979) Plotting methods for analyzing enzyme rate data. Methods Enzymol 63:138-159
    • (1979) Methods Enzymol , vol.63 , pp. 138-159
    • Rudolph, F.B.1    Fromm, H.J.2
  • 43
    • 0026770274 scopus 로고
    • Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase
    • Saito K, Miura N, Yamazaki M, Hirano H, Murakoshi I (1992) Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase. Proc Natl Acad Sci USA 89:8078-8082
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8078-8082
    • Saito, K.1    Miura, N.2    Yamazaki, M.3    Hirano, H.4    Murakoshi, I.5
  • 44
    • 0027314290 scopus 로고
    • The role of cutinase in fungal pathogenicity
    • Schafer W (1993) The role of cutinase in fungal pathogenicity. Trends Microbiol 1:69-71
    • (1993) Trends Microbiol , vol.1 , pp. 69-71
    • Schafer, W.1
  • 45
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 46
    • 0026936942 scopus 로고
    • Overproduction of an alpha-amylase/glucoamylase fusion protein in Aspergillus oryzae using a high expression vector
    • Shibuya I, Tsuchiya K, Tamura G, Ishikawa T, Hara S (1992) Overproduction of an alpha-amylase/glucoamylase fusion protein in Aspergillus oryzae using a high expression vector. Biosci Biotechnol Biochem 56:1674-1675
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1674-1675
    • Shibuya, I.1    Tsuchiya, K.2    Tamura, G.3    Ishikawa, T.4    Hara, S.5
  • 47
    • 0032522931 scopus 로고    scopus 로고
    • Bacterial isolates degrading aliphatic polycarbonates
    • Suyama T, Hosoya H, Tokiwa Y (1998a) Bacterial isolates degrading aliphatic polycarbonates. FEMS Microbiol Lett 161:255-261
    • (1998) FEMS Microbiol Lett , vol.161 , pp. 255-261
    • Suyama, T.1    Hosoya, H.2    Tokiwa, Y.3
  • 48
    • 0032402842 scopus 로고    scopus 로고
    • Phylogenetic affiliation of soil bacteria that degrade aliphatic polyesters available commercially as biodegradable plastics
    • Suyama T, Tokiwa Y, Ouichanpagdee P, Kanagawa T, Kamagata Y (1998b) Phylogenetic affiliation of soil bacteria that degrade aliphatic polyesters available commercially as biodegradable plastics. Appl Environ Microbiol 64:5008-5011
    • (1998) Appl Environ Microbiol , vol.64 , pp. 5008-5011
    • Suyama, T.1    Tokiwa, Y.2    Ouichanpagdee, P.3    Kanagawa, T.4    Kamagata, Y.5
  • 49
    • 0026533312 scopus 로고
    • Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea
    • Sweigard JA, Chumley FG, Valent B (1992a) Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea. Mol Gen Genet 232:174-182
    • (1992) Mol Gen Genet , vol.232 , pp. 174-182
    • Sweigard, J.A.1    Chumley, F.G.2    Valent, B.3
  • 50
    • 0026598103 scopus 로고
    • Disruption of a Magnaporthe grisea cutinase gene
    • Sweigard JA, Chumley FG, Valent B (1992b) Disruption of a Magnaporthe grisea cutinase gene. Mol Gen Genet 232:183-190
    • (1992) Mol Gen Genet , vol.232 , pp. 183-190
    • Sweigard, J.A.1    Chumley, F.G.2    Valent, B.3
  • 55
    • 0034255871 scopus 로고    scopus 로고
    • Properties of a bacterium which degrades solid poly (tetramethylene succinate)-co-adipate, a biodegradable plastic
    • Uchida H, Nakajima-Kambe T, Shigeno-Akutsu Y, Nomura N, Tokiwa Y, Nakahara T (2000) Properties of a bacterium which degrades solid poly (tetramethylene succinate)-co-adipate, a biodegradable plastic. FEMS Microbiol Lett 189:25-29
    • (2000) FEMS Microbiol Lett , vol.189 , pp. 25-29
    • Uchida, H.1    Nakajima-Kambe, T.2    Shigeno-Akutsu, Y.3    Nomura, N.4    Tokiwa, Y.5    Nakahara, T.6


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