메뉴 건너뛰기




Volumn 56, Issue , 2002, Pages 403-432

Microbial degradation of polyhydroxyalkanoates

Author keywords

Extracellular PHB depolymerase; Intracellular PHB depolymerase; Paucimonas lemoignei; Polyhydroxybutyrate

Indexed keywords

BIOMATERIAL; CARBOXYLESTERASE; POLY(3 HYDROXYBUTYRIC ACID); POLYESTER; POLYHYDROXYALKANOIC ACID;

EID: 0036406855     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.56.012302.160838     Document Type: Review
Times cited : (552)

References (116)
  • 1
    • 0030412875 scopus 로고    scopus 로고
    • Enzymatic and environmental degradation of racemic poly (3-hydroxybutyric acid)s with different stereoregulatoris
    • Abe H, Doi Y. 1996. Enzymatic and environmental degradation of racemic poly (3-hydroxybutyric acid)s with different stereoregulatoris. Macromolecules 29:8683-88
    • (1996) Macromolecules , vol.29 , pp. 8683-8688
    • Abe, H.1    Doi, Y.2
  • 2
    • 0026416984 scopus 로고
    • Poly(3-hydroxybutyrate) in vivo: NMR and X-ray characterization of the elastomeric state
    • Amor SR, Rayment T, Sanders JKM. 1991. Poly(3-hydroxybutyrate) in vivo: NMR and X-ray characterization of the elastomeric state. Macromolecules 24:4583-88
    • (1991) Macromolecules , vol.24 , pp. 4583-4588
    • Amor, S.R.1    Rayment, T.2    Sanders, J.K.M.3
  • 3
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial use of bacterial polyhydroxyalkanoates
    • Anderson AJ, Dawes EA. 1990. Occurrence, metabolism, metabolic role, and industrial use of bacterial polyhydroxyalkanoates. Microbiol. Rev. 54:450-72
    • (1990) Microbiol. Rev. , vol.54 , pp. 450-472
    • Anderson, A.J.1    Dawes, E.A.2
  • 4
    • 0032633718 scopus 로고    scopus 로고
    • Investigation of the enzymatic cleavage of diastereomeric oligo(3-hydroxybutanoates) containing two to eight HB units. A model for the stereoselectivity of PHB depolymerase from Alcaligenes faecalis T1
    • Bachmann BM, Seebach D. 1999. Investigation of the enzymatic cleavage of diastereomeric oligo(3-hydroxybutanoates) containing two to eight HB units. A model for the stereoselectivity of PHB depolymerase from Alcaligenes faecalis T1. Macromolecules 32:1777-84
    • (1999) Macromolecules , vol.32 , pp. 1777-1784
    • Bachmann, B.M.1    Seebach, D.2
  • 6
    • 0030271442 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site
    • Behrends A, Klingbeil B, Jendrossek D. 1996. Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site. FEMS Microbiol. Lett. 143:191-94
    • (1996) FEMS Microbiol. Lett. , vol.143 , pp. 191-194
    • Behrends, A.1    Klingbeil, B.2    Jendrossek, D.3
  • 7
    • 0032378846 scopus 로고    scopus 로고
    • Biological basis of enzyme-catalyzed polyester degradation: 59 C-terminal amino acids of poly(3-hydroxybutyrate) (PHB) depolymerase A from Pseudomonas lemoignei are sufficient for PHB-binding
    • Briese B-H, Jendrossek D. 1998. Biological basis of enzyme-catalyzed polyester degradation: 59 C-terminal amino acids of poly(3-hydroxybutyrate) (PHB) depolymerase A from Pseudomonas lemoignei are sufficient for PHB-binding. Macromol. Symp. 130:205-16
    • (1998) Macromol. Symp. , vol.130 , pp. 205-216
    • Briese, B.-H.1    Jendrossek, D.2
  • 8
    • 0028280507 scopus 로고
    • Degradation of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) by aerobic sewage sludge
    • Briese B-H, Jendrossek D, Schlegel HG. 1994. Degradation of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) by aerobic sewage sludge. FEMS Microbiol. Lett. 117:107-12
    • (1994) FEMS Microbiol. Lett. , vol.117 , pp. 107-112
    • Briese, B.-H.1    Jendrossek, D.2    Schlegel, H.G.3
  • 9
    • 0028405281 scopus 로고
    • Pseudomonas lemoignei has five poly(hydroxyalkanoic acid) (PHA) depolymerase genes: A comparative study of bacterial and eukaryotic depolymerases
    • Briese B-H, Schmidt B, Jendrossek D. 1994. Pseudomonas lemoignei has five poly(hydroxyalkanoic acid) (PHA) depolymerase genes: A comparative study of bacterial and eukaryotic depolymerases. J. Environ. Polym. Degrad. 2:75-87
    • (1994) J. Environ. Polym. Degrad. , vol.2 , pp. 75-87
    • Briese, B.-H.1    Schmidt, B.2    Jendrossek, D.3
  • 10
    • 0006418656 scopus 로고    scopus 로고
    • Production of poly(3-hydroxybutyric acidco-4-hydroxybutyric acid) and poly(4-hydroxybutyric acid) without subsequent degradation by Hydrogenophaga pseudoflava
    • Choi MH, Yoon SC, Lenz RW. 1999. Production of poly(3-hydroxybutyric acidco-4-hydroxybutyric acid) and poly(4-hydroxybutyric acid) without subsequent degradation by Hydrogenophaga pseudoflava. Appl. Environ. Microbiol. 65:1570-77
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1570-1577
    • Choi, M.H.1    Yoon, S.C.2    Lenz, R.W.3
  • 11
    • 33846429434 scopus 로고
    • Poly-β-hydroxybuttersäure abbauende bakterien und exoenzym
    • Chowdhury AA. 1963. Poly-β-hydroxybuttersäure abbauende bakterien und exoenzym. Arch. Mikrobiol. 47:167-200
    • (1963) Arch. Mikrobiol. , vol.47 , pp. 167-200
    • Chowdhury, A.A.1
  • 12
    • 0009740934 scopus 로고
    • The amorphous state of bacterial poly[(r)-3-hydroxyalkanoate)] in vivo
    • de Koning GJM, Lemstra PJ. 1992. The amorphous state of bacterial poly[(R)-3-hydroxyalkanoate)] in vivo. Polymer 33:3304-6
    • (1992) Polymer , vol.33 , pp. 3304-3306
    • De Koning, G.J.M.1    Lemstra, P.J.2
  • 13
    • 0000770107 scopus 로고
    • A biodegradable rubber by cross linking polyhydroxyalkanoates from Pseudomonas oleovorans
    • de Koning GJM, van Bilsen HMM, Lemstra PJ, Hazenberg W, Witholt B, et al. 1994. A biodegradable rubber by cross linking polyhydroxyalkanoates from Pseudomonas oleovorans. Polymer 35:2090-97
    • (1994) Polymer , vol.35 , pp. 2090-2097
    • De Koning, G.J.M.1    Van Bilsen, H.M.M.2    Lemstra, P.J.3    Hazenberg, W.4    Witholt, B.5
  • 16
    • 0011102515 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 17
    • 0029634559 scopus 로고
    • Microbial synthesis and characterization of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate)
    • Doi Y, Kitamura S, Abe H. 1995. Microbial synthesis and characterization of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate). Macromolecules 28:4822-28
    • (1995) Macromolecules , vol.28 , pp. 4822-4828
    • Doi, Y.1    Kitamura, S.2    Abe, H.3
  • 18
    • 0000965928 scopus 로고
    • Structural effects on biodegradation of microbial and synthetic poly(hydroxyalkanoates)
    • ed. M Vert. London: R. Soc. Chem.
    • Doi Y, Kumagai Y, Tanahashi N, Mukai K. 1992. Structural effects on biodegradation of microbial and synthetic poly(hydroxyalkanoates). In Biodegradable Polymers and Plastics, ed. M Vert, pp. 139-48. London: R. Soc. Chem.
    • (1992) Biodegradable Polymers and Plastics , pp. 139-148
    • Doi, Y.1    Kumagai, Y.2    Tanahashi, N.3    Mukai, K.4
  • 19
    • 0025020367 scopus 로고
    • Cyclic nature of poly(3-hydroxyalkanoate) metabolism in Alcaligenes eutrophus
    • Doi Y, Segawa A, Kawaguchi Y, Kunioka M. 1990. Cyclic nature of poly(3-hydroxyalkanoate) metabolism in Alcaligenes eutrophus. FEMS Microbiol. Lett. 67:165-70
    • (1990) FEMS Microbiol. Lett. , vol.67 , pp. 165-170
    • Doi, Y.1    Segawa, A.2    Kawaguchi, Y.3    Kunioka, M.4
  • 20
    • 0033154117 scopus 로고    scopus 로고
    • Bioassimilation of oligomers of atactic poly [(R,S)-3-hydroxybutyrate] by selected bacterial strains
    • Focarete ML, Scandola M, Jendrossek D, Adamus G, Sikorska W, Kowalczuk M. 1999. Bioassimilation of oligomers of atactic poly [(R,S)-3-hydroxybutyrate] by selected bacterial strains. Macromolecules 32:4814-18
    • (1999) Macromolecules , vol.32 , pp. 4814-4818
    • Focarete, M.L.1    Scandola, M.2    Jendrossek, D.3    Adamus, G.4    Sikorska, W.5    Kowalczuk, M.6
  • 21
    • 0028223775 scopus 로고
    • Quantitative determination of intracellular depolymerase activity in Pseudomonas oleovorans inclusions containing poly-3-hydroxyalkanoates with long alkyl substituents
    • Foster LJR, Lenz RW, Fuller RC. 1994. Quantitative determination of intracellular depolymerase activity in Pseudomonas oleovorans inclusions containing poly-3-hydroxyalkanoates with long alkyl substituents. FEMS Microbiol. Lett. 118:279-82
    • (1994) FEMS Microbiol. Lett. , vol.118 , pp. 279-282
    • Foster, L.J.R.1    Lenz, R.W.2    Fuller, R.C.3
  • 22
    • 0030271852 scopus 로고    scopus 로고
    • Intracellular depolymerase and polyhydroxyoctanoate granule integrity in Pseudomonas oleovorans
    • Foster LJR, Stuart ES, Tehrani A, Lenz RW, Fuller RC. 1996. Intracellular depolymerase and polyhydroxyoctanoate granule integrity in Pseudomonas oleovorans. Int. J. Biol. Macromol. 19:177-83
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 177-183
    • Foster, L.J.R.1    Stuart, E.S.2    Tehrani, A.3    Lenz, R.W.4    Fuller, R.C.5
  • 23
    • 0029158337 scopus 로고
    • The biodegradation of poly-3-hydroxyalkanoates. PHAs, with long alkyl substituents by Pseudomonas maculicola
    • Foster LJR, Zervas SJ, Lenz RW, Fuller RC. 1995. The biodegradation of poly-3-hydroxyalkanoates, PHAs, with long alkyl substituents by Pseudomonas maculicola. Biodegradation 6:67-73
    • (1995) Biodegradation , vol.6 , pp. 67-73
    • Foster, L.J.R.1    Zervas, S.J.2    Lenz, R.W.3    Fuller, R.C.4
  • 24
    • 0024299118 scopus 로고
    • Effect of limited tryptic modification of a bacterial poly(3-hydroxybutyrate) depolymerase on its catalytic activity
    • Fukui T, Narikawa T, Miwa K, Shirakura Y, Saito T, Tomita K. 1988. Effect of limited tryptic modification of a bacterial poly(3-hydroxybutyrate) depolymerase on its catalytic activity. Biochim. Biophys. Acta 952:164-71
    • (1988) Biochim. Biophys. Acta. , vol.952 , pp. 164-171
    • Fukui, T.1    Narikawa, T.2    Miwa, K.3    Shirakura, Y.4    Saito, T.5    Tomita, K.6
  • 25
    • 0035868599 scopus 로고    scopus 로고
    • Identification of the intracellular polyhydroxyalkanoate depolymerase gene of Paracoccus denitrificans and some properties of the gene product
    • Gao S, Maehara A, Yamane T, Ueda S. 2001. Identification of the intracellular polyhydroxyalkanoate depolymerase gene of Paracoccus denitrificans and some properties of the gene product. FEMS Microbiol. Lett. 196:159-64
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 159-164
    • Gao, S.1    Maehara, A.2    Yamane, T.3    Ueda, S.4
  • 26
    • 0034656883 scopus 로고    scopus 로고
    • Fungal degradation of thermoplastic polymers under simulated deep sea conditions
    • Gonda KE, Jendrossek D, Molitoris HP. 2000. Fungal degradation of thermoplastic polymers under simulated deep sea conditions. Hydrobiologia 426:73-183
    • (2000) Hydrobiologia , vol.426 , pp. 73-183
    • Gonda, K.E.1    Jendrossek, D.2    Molitoris, H.P.3
  • 27
    • 0015145951 scopus 로고
    • Metabolism of poly-β-hydroxybutyrate: Effect of mild alkaline extraction on native polyβ-hydroxybutyrate granules
    • Griebel RJ, Merrick JM. 1971. Metabolism of poly-β-hydroxybutyrate: Effect of mild alkaline extraction on native polyβ-hydroxybutyrate granules. J. Bacteriol. 108:782-89
    • (1971) J. Bacteriol. , vol.108 , pp. 782-789
    • Griebel, R.J.1    Merrick, J.M.2
  • 28
    • 0014340156 scopus 로고
    • Metabolism of poly-β-hydroxybutyrate. I. Purification, composition, and properties of native poly-β-hydroxybutyrate granules from Bacillus megaterium
    • Griebel RJ, Smith Z, Merrick JM. 1968. Metabolism of poly-β-hydroxybutyrate. I. Purification, composition, and properties of native poly-β-hydroxybutyrate granules from Bacillus megaterium. Biochemistry 7:3676-81
    • (1968) Biochemistry , vol.7 , pp. 3676-3681
    • Griebel, R.J.1    Smith, Z.2    Merrick, J.M.3
  • 29
    • 3042922145 scopus 로고    scopus 로고
    • Purification and properties of extracellular poly (3-hydroxybutyrate) depolymerase produced by Penicillium pinophilum
    • Han J-S, Son Y-J, Chang C-S, Kim M-N. 1998. Purification and properties of extracellular poly (3-hydroxybutyrate) depolymerase produced by Penicillium pinophilum. J. Microbiol. 36:67-73
    • (1998) J. Microbiol. , vol.36 , pp. 67-73
    • Han, J.-S.1    Son, Y.-J.2    Chang, C.-S.3    Kim, M.-N.4
  • 31
    • 0035965210 scopus 로고    scopus 로고
    • A new type of thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of shortchain-length hydroxyalkanoic acids
    • Handrick R, Reinhardt S, Focarete ML, Scandola M, Adamus G, et al. 2001. A new type of thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of shortchain-length hydroxyalkanoic acids. J. Biol. Chem. 276:36215-24
    • (2001) J. Biol. Chem. , vol.276 , pp. 36215-36224
    • Handrick, R.1    Reinhardt, S.2    Focarete, M.L.3    Scandola, M.4    Adamus, G.5
  • 32
    • 0033814278 scopus 로고    scopus 로고
    • Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha
    • Handrick R, Reinhard S, Jendrossek D. 2000. Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha. J. Bacteriol. 182:5916-18
    • (2000) J. Bacteriol. , vol.182 , pp. 5916-5918
    • Handrick, R.1    Reinhard, S.2    Jendrossek, D.3
  • 33
    • 0011068691 scopus 로고
    • Synthesis and breakdown of poly-β-hydroxybutyric acid by bacteria
    • Hayward AC, Forsyth WGC, Roberts JB. 1959. Synthesis and breakdown of poly-β-hydroxybutyric acid by bacteria. J. Gen. Microbiol. 20:510-18
    • (1959) J. Gen. Microbiol. , vol.20 , pp. 510-518
    • Hayward, A.C.1    Forsyth, W.G.C.2    Roberts, J.B.3
  • 34
    • 0014220278 scopus 로고
    • Aufbau und wiederverwertung von poly-β-hydroxybuttersäure durch Hydrogenomonas H16
    • Hippe H. 1967. Aufbau und wiederverwertung von poly-β-hydroxybuttersäure durch Hydrogenomonas H16. Arch. Mikrobiol. 56:248-77
    • (1967) Arch. Mikrobiol. , vol.56 , pp. 248-277
    • Hippe, H.1
  • 35
    • 0014220233 scopus 로고
    • Hydrolyse von PHBS durch intrazelluläre depolymerase von Hydrogenomonas H16
    • Hippe H, Schlegel HG. 1967. Hydrolyse von PHBS durch intrazelluläre Depolymerase von Hydrogenomonas H16. Arch. Mikrobiol. 56:278-99
    • (1967) Arch. Mikrobiol. , vol.56 , pp. 278-299
    • Hippe, H.1    Schlegel, H.G.2
  • 36
    • 0034279048 scopus 로고    scopus 로고
    • Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri
    • Hiraishi T, Ohura T, Ito S, Kassuya K-I, Doi Y. 2000. Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri. Biomacromolecules 1:320-24
    • (2000) Biomacromolecules , vol.1 , pp. 320-324
    • Hiraishi, T.1    Ohura, T.2    Ito, S.3    Kassuya, K.-I.4    Doi, Y.5
  • 38
    • 0029164364 scopus 로고
    • Biomimetic, amorphous granules of polyhydroxyalkanoates: Composition, mobility, and stabilization in vivo by proteins
    • Horowitz DM, Sanders JKM. 1995. Biomimetic, amorphous granules of polyhydroxyalkanoates: Composition, mobility, and stabilization in vivo by proteins. Can. J. Microbiol. 41(Suppl. 1):115-123
    • (1995) Can. J. Microbiol. , vol.41 , Issue.SUPPL. 1 , pp. 115-123
    • Horowitz, D.M.1    Sanders, J.K.M.2
  • 39
    • 0025772866 scopus 로고
    • Metabolism of poly(3-hydroxyalkanoates) (PHA) by Pseudomonas oleovorans
    • Huisman GW, Wonink E, Meima R, Terpstra B, Witholt B. 1991. Metabolism of poly(3-hydroxyalkanoates) (PHA) by Pseudomonas oleovorans. J. Biol. Chem. 266:2191-98
    • (1991) J. Biol. Chem. , vol.266 , pp. 2191-2198
    • Huisman, G.W.1    Wonink, E.2    Meima, R.3    Terpstra, B.4    Witholt, B.5
  • 40
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications
    • Jaeger K-E, Dijkstra BW, Reetz MT. 1999. Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications. Annu. Rev. Microbiol. 53:315-35
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 315-335
    • Jaeger, K.-E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 42
    • 0029092045 scopus 로고
    • Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: Bacterial lipases hydrolyze poly(ω)-hydroxyalkanoates)
    • Jaeger K-E, Steinbüchel A, Jendrossek D. 1995. Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: Bacterial lipases hydrolyze poly(ω)-hydroxyalkanoates). Appl. Environ. Microbiol. 61:3113-18
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3113-3118
    • Jaeger, K.-E.1    Steinbüchel, A.2    Jendrossek, D.3
  • 43
    • 0032974709 scopus 로고    scopus 로고
    • Poly-3-hydroxybutyrate in Legionella pneumophila, an energy source for survival in low-nutrient environments
    • James BW, Mauchline WS, Dennis PJ, Keevil CW, Wait R. 1999. Poly-3-hydroxybutyrate in Legionella pneumophila, an energy source for survival in low-nutrient environments. Appl. Environ. Microbiol. 65:822-27
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 822-827
    • James, B.W.1    Mauchline, W.S.2    Dennis, P.J.3    Keevil, C.W.4    Wait, R.5
  • 46
    • 0034985476 scopus 로고    scopus 로고
    • Transfer of [Pseudomanas] lemoignei, a gram-negative rod with restricted catabolic capacity, to Paucimonas gen. nov. with one species. Paucimonas lemoignei comb. nov.
    • Jendrossek D. 2001. Transfer of [Pseudomanas] lemoignei, a gram-negative rod with restricted catabolic capacity, to Paucimonas gen. nov. with one species, Paucimonas lemoignei comb. nov. Int. J. Syst. Evol. Microbiol. 51:905-8
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 905-908
    • Jendrossek, D.1
  • 47
    • 0029082038 scopus 로고
    • Characterization of the extracellular poly(3-hydroxybutyrate) depolymerase of Comamonas sp. and of its structural gene
    • Jendrossek D, Backhaus M, Andermann M. 1995. Characterization of the extracellular poly(3-hydroxybutyrate) depolymerase of Comamonas sp. and of its structural gene. Can. J. Microbiol. 41(Suppl. 1):160-69
    • (1995) Can. J. Microbiol. , vol.41 , Issue.SUPPL. 1 , pp. 160-169
    • Jendrossek, D.1    Backhaus, M.2    Andermann, M.3
  • 48
    • 0028961638 scopus 로고
    • Biochemical and molecular characterization of the Pseudomonas lemoignei depolymerase system
    • Jendrossek D, Frisse A, Behrends A, Andermann M, Kratzin HD, et al. 1995. Biochemical and molecular characterization of the Pseudomonas lemoignei depolymerase system. J. Bacteriol. 177:596-607
    • (1995) J. Bacteriol. , vol.177 , pp. 596-607
    • Jendrossek, D.1    Frisse, A.2    Behrends, A.3    Andermann, M.4    Kratzin, H.D.5
  • 49
    • 0027271730 scopus 로고
    • Degradation of poly(3-hydroxybutyrate), PHB, by bacteria and purification of a novel PHB depolymerase from Comamonas sp.
    • Jendrossek D, Knoke I, Habibian RB, Steinbüchel A, Schlegel HG. 1993. Degradation of poly(3-hydroxybutyrate), PHB, by bacteria and purification of a novel PHB depolymerase from Comamonas sp. J. Environ. Polym. Degrad. 1:53-63
    • (1993) J. Environ. Polym. Degrad. , vol.1 , pp. 53-63
    • Jendrossek, D.1    Knoke, I.2    Habibian, R.B.3    Steinbüchel, A.4    Schlegel, H.G.5
  • 50
    • 0027146571 scopus 로고
    • Cloning and characterization of the poly(hydroxyalkanoic acid)-depolymerase gene locus, phaZ1, of Pseudomonas lemoignei and its gene product
    • Jendrossek D, Müller B, Schlegel HG. 1993. Cloning and characterization of the poly(hydroxyalkanoic acid)-depolymerase gene locus, phaZ1, of Pseudomonas lemoignei and its gene product. Eur. J. Biochem. 218:701-10
    • (1993) Eur. J. Biochem. , vol.218 , pp. 701-710
    • Jendrossek, D.1    Müller, B.2    Schlegel, H.G.3
  • 51
    • 0011126489 scopus 로고    scopus 로고
    • Recent advances in characterization of bacterial PHA depolymerases
    • ed. G Eggink, A Steinbüchel, Y Poirier, B Witholt. Ottawa, Can.: NRC Res
    • Jendrossek D, Schirmer A, Handrick R. 1997. Recent advances in characterization of bacterial PHA depolymerases. In International Symposium on Bacterial Polyhydroxyalkanoates, ed. G Eggink, A Steinbüchel, Y Poirier, B Witholt, pp. 89-101. Ottawa, Can.: NRC Res.
    • (1997) International Symposium on Bacterial Polyhydroxyalkanoates , pp. 89-101
    • Jendrossek, D.1    Schirmer, A.2    Handrick, R.3
  • 52
    • 0030777589 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the polyhydroxybutyrate depolymerase of Comamonas acidovoransYM1609, isolated from freshwater
    • Kasuya K, Inoune Y, Tanaka T, Akehata T, Iwata T, et al. 1997. Biochemical and molecular characterization of the polyhydroxybutyrate depolymerase of Comamonas acidovoransYM1609, isolated from freshwater. Appl. Environ. Microbiol. 63:4844-52
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4844-4852
    • Kasuya, K.1    Inoune, Y.2    Tanaka, T.3    Akehata, T.4    Iwata, T.5
  • 53
    • 0033066633 scopus 로고    scopus 로고
    • Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases
    • Kasuya K, Ohura T, Masuda K, Doi Y. 1999. Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases. Int. Biol. Macromol. 24:329-36
    • (1999) Int. Biol. Macromol. , vol.24 , pp. 329-336
    • Kasuya, K.1    Ohura, T.2    Masuda, K.3    Doi, Y.4
  • 55
    • 0034027138 scopus 로고    scopus 로고
    • Characterization of an extracellular poly(3-hydroxy-5-phenylvalerate) depolymerase from Xanthomonas sp. JS02
    • Kim H, Ju H-S, Kim J. 2000. Characterization of an extracellular poly(3-hydroxy-5-phenylvalerate) depolymerase from Xanthomonas sp. JS02. Appl. Microbiol. Biotechnol. 53:323-27
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 323-327
    • Kim, H.1    Ju, H.-S.2    Kim, J.3
  • 56
    • 0031002291 scopus 로고    scopus 로고
    • Cloningme of poly (3-hydroxybutyrate) depolymerase from a marine bacterium. Alcaligenes faecalis AE122, and characterization of its gene product
    • Kita K, Mashiba S, Nagita M, Ishimaru K, Okamoto K, et al. 1997. Cloningme of poly (3-hydroxybutyrate) depolymerase from a marine bacterium, Alcaligenes faecalis AE122, and characterization of its gene product. Biochim. Biophys. Acta 1352:113-22
    • (1997) Biochim. Biophys. Acta , vol.1352 , pp. 113-122
    • Kita, K.1    Mashiba, S.2    Nagita, M.3    Ishimaru, K.4    Okamoto, K.5
  • 57
    • 0030246972 scopus 로고    scopus 로고
    • Taxonomical identification of Streptomyces exfoliatus K10 and characterization of its poly(3-hydroxybutyrate) depolymerase gene
    • Klingbeil B, Kroppenstedt R, Jendrossek D. 1996. Taxonomical identification of Streptomyces exfoliatus K10 and characterization of its poly(3-hydroxybutyrate) depolymerase gene. FEMS Microbiol. Lett. 142:215-21
    • (1996) FEMS Microbiol. Lett. , vol.142 , pp. 215-221
    • Klingbeil, B.1    Kroppenstedt, R.2    Jendrossek, D.3
  • 58
    • 0011069241 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 59
    • 0011066794 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 60
    • 0032687110 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of an extracellular poly(3-hydroxybutyrate) depolymerase from Acidovorax sp. strain TP4
    • Kobayashi T, Sugiyama A, Kawase Y, Saito T, Mergaert J, Swings J. 1999. Biochemical and genetic characterization of an extracellular poly(3-hydroxybutyrate) depolymerase from Acidovorax sp. strain TP4. J. Environ. Polym. Degrad. 7:9-18
    • (1999) J. Environ. Polym. Degrad. , vol.7 , pp. 9-18
    • Kobayashi, T.1    Sugiyama, A.2    Kawase, Y.3    Saito, T.4    Mergaert, J.5    Swings, J.6
  • 61
    • 0034680566 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate)-depolymerase from Pseudomonas lemoignei: Catalysis of esterifications in organic media
    • Kumar A, Gross RA, Jendrossek D. 2000. Poly(3-hydroxybutyrate)-depolymerase from Pseudomonas lemoignei: Catalysis of esterifications in organic media. J. Org. Chem. 65:7800-6
    • (2000) J. Org. Chem. , vol.65 , pp. 7800-7806
    • Kumar, A.1    Gross, R.A.2    Jendrossek, D.3
  • 62
    • 0000188357 scopus 로고
    • Etudes sur l'autolyse microbienne - Acidification par formation d'acide β oxybutyrique
    • Lemoigne M. 1925. Etudes sur l'autolyse microbienne - Acidification par formation d'acide β oxybutyrique. Ann. Inst. Pastuer 39:144-55
    • (1925) Ann. Inst. Pastuer , vol.39 , pp. 144-155
    • Lemoigne, M.1
  • 63
    • 0027943212 scopus 로고
    • Tracing the spread of fibronectin type III domains in bacterial glycohydrolases
    • Little E, Bork P, Doolittle RF. 1994. Tracing the spread of fibronectin type III domains in bacterial glycohydrolases. J. Mol. Evol. 39:631-43
    • (1994) J. Mol. Evol. , vol.39 , pp. 631-643
    • Little, E.1    Bork, P.2    Doolittle, R.F.3
  • 64
    • 0001124196 scopus 로고
    • Poly-β-hydroxybutyrate metabolism in washed suspensions of Bacillus cereus and Bacillus megaterium
    • Macrae RM, Wilkinson JF. 1958. Poly-β-hydroxybutyrate metabolism in washed suspensions of Bacillus cereus and Bacillus megaterium. J. Gen. Microbiol. 19:210-22
    • (1958) J. Gen. Microbiol. , vol.19 , pp. 210-222
    • Macrae, R.M.1    Wilkinson, J.F.2
  • 65
    • 0033046562 scopus 로고    scopus 로고
    • Metabolic engineering of poly(3-hydroxyalkanoates): From DNA to plastic
    • Madison LL, Huisman GW. 1999. Metabolic engineering of poly(3-hydroxyalkanoates): From DNA to plastic. Microbiol. Mol. Biol. Rev. 63:21-53
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 21-53
    • Madison, L.L.1    Huisman, G.W.2
  • 66
    • 0029125403 scopus 로고
    • Artificial granule suspensions of long side chain poly(3-hydroxyalkanoate)
    • Marchessault RH, Morin FG, Wong S, Saracovan I. 1995. Artificial granule suspensions of long side chain poly(3-hydroxyalkanoate). Can. J. Microbiol. 41 (Suppl. 1):138-42
    • (1995) Can. J. Microbiol. , vol.41 , Issue.SUPPL. 1 , pp. 138-142
    • Marchessault, R.H.1    Morin, F.G.2    Wong, S.3    Saracovan, I.4
  • 67
    • 0026620790 scopus 로고
    • Fungal degradation of polyhydroxyalkanoates and a semiquantitative assay for screening their degradation by terrestrial fungi
    • Matavulj M, Molitoris HP. 1992. Fungal degradation of polyhydroxyalkanoates and a semiquantitative assay for screening their degradation by terrestrial fungi. FEMS Microbiol. Rev. 103:323-32
    • (1992) FEMS Microbiol. Rev. , vol.103 , pp. 323-332
    • Matavulj, M.1    Molitoris, H.P.2
  • 70
    • 78651166101 scopus 로고
    • Depolymerisation of poly-β-hydroxybutyrate by an intracellular enzyme system
    • Merrick JM, Doudoroff M. 1964. Depolymerisation of poly-β-hydroxybutyrate by an intracellular enzyme system. J. Bacteriol. 88:60-71
    • (1964) J. Bacteriol. , vol.88 , pp. 60-71
    • Merrick, J.M.1    Doudoroff, M.2
  • 71
    • 0033045521 scopus 로고    scopus 로고
    • Hydrolysis of native poly(hydroxybutyrate) granules (PHB), crystalline PHB, and artificial amorphous PHB granules by intracellular and extracellular depolymerases
    • Merrick JM, Steger R, Dombroski D. 1999. Hydrolysis of native poly(hydroxybutyrate) granules (PHB), crystalline PHB, and artificial amorphous PHB granules by intracellular and extracellular depolymerases. Int. J. Biol. Macromol. 25:129-34
    • (1999) Int. J. Biol. Macromol. , vol.25 , pp. 129-134
    • Merrick, J.M.1    Steger, R.2    Dombroski, D.3
  • 73
    • 0027404438 scopus 로고
    • Purification and properties of a poly(3-hydroxyvalerate) depolymerase from Pseudomonas lemoignei
    • Müller B, Jendrossek D. 1993. Purification and properties of a poly(3-hydroxyvalerate) depolymerase from Pseudomonas lemoignei. Appl. Microbiol. Biotechnol. 38:487-92
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 487-492
    • Müller, B.1    Jendrossek, D.2
  • 74
    • 33748242975 scopus 로고
    • Poly(hydroxyalkanoates): A fifth class of physiologically important organic biopolymers?
    • Müller HM, Seebach D. 1993. Poly(hydroxyalkanoates): A fifth class of physiologically important organic biopolymers? Angew. Chem. Int. Ed. Engl. 32:477-502
    • (1993) Angew. Chem. Int. Ed. Engl. , vol.32 , pp. 477-502
    • Müller, H.M.1    Seebach, D.2
  • 75
    • 0022429859 scopus 로고
    • Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerases from Pseudomonas lemoignei
    • Nakayama K, Saito T, Fukui T, Shirakura Y, Tomita K. 1985. Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerases from Pseudomonas lemoignei. Biochim. Biophys. Acta 827:63-72
    • (1985) Biochim. Biophys. Acta. , vol.827 , pp. 63-72
    • Nakayama, K.1    Saito, T.2    Fukui, T.3    Shirakura, Y.4    Tomita, K.5
  • 77
    • 0030422094 scopus 로고    scopus 로고
    • Splintering of poly(3-hydroxybutyrate) single crystals by PHB-depolymerase A from Pseudomonas lemoignei
    • Nobes GAR, Marchessault RH, Chanzy H, Briese BH, Jendrossek D. 1996. Splintering of poly(3-hydroxybutyrate) single crystals by PHB-depolymerase A from Pseudomonas lemoignei. Macromolecules 29:8330-33
    • (1996) Macromolecules , vol.29 , pp. 8330-8333
    • Nobes, G.A.R.1    Marchessault, R.H.2    Chanzy, H.3    Briese, B.H.4    Jendrossek, D.5
  • 78
    • 0030730849 scopus 로고    scopus 로고
    • Structure and function of poly(3-hydroxybutyrate) depolymerases from Alcaligenes faecalis T1
    • Nojiri M, Saito T. 1997. Structure and function of poly(3-hydroxybutyrate) depolymerases from Alcaligenes faecalis T1. J. Bacteriol. 179:6965-70
    • (1997) J. Bacteriol. , vol.179 , pp. 6965-6970
    • Nojiri, M.1    Saito, T.2
  • 79
    • 0015839148 scopus 로고
    • β-Ketothiolase from Hydrogenomonas eutropha H16 and its significance in the regulation of poly-β-hydroxybutyrate metabolism
    • Oeding V, Schlegel HG. 1973. β-Ketothiolase from Hydrogenomonas eutropha H16 and its significance in the regulation of poly-β-hydroxybutyrate metabolism. Biochem. J. 134:239-48
    • (1973) Biochem. J. , vol.134 , pp. 239-248
    • Oeding, V.1    Schlegel, H.G.2
  • 80
    • 0032740674 scopus 로고    scopus 로고
    • Biodegradation of poly(3-hydroxyalkanoic acids) fibers and isolation of poly(3-hydroxybutyric acid)degrading microorganisms under aquatic environments
    • Ohura T, Aoyagi Y, Takagi K, Yoshida Y, Kasuya K, Doi Y. 1999. Biodegradation of poly(3-hydroxyalkanoic acids) fibers and isolation of poly(3-hydroxybutyric acid)degrading microorganisms under aquatic environments. Polym. Degrad. Stab. 63:23-29
    • (1999) Polym. Degrad. Stab. , vol.63 , pp. 23-29
    • Ohura, T.1    Aoyagi, Y.2    Takagi, K.3    Yoshida, Y.4    Kasuya, K.5    Doi, Y.6
  • 81
    • 0032963796 scopus 로고    scopus 로고
    • Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains
    • Ohura T, Kasuya K, Doi Y. 1999. Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains. Appl. Environ. Microbiol. 65:189-97
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 189-197
    • Ohura, T.1    Kasuya, K.2    Doi, Y.3
  • 83
    • 0033045322 scopus 로고    scopus 로고
    • Extracellular degradation of medium chain length poly(beta-hydroxyalkanoates) by Comamonas sp.
    • Quinteros R, Goodwin S, Lenz RW, Park WH. 1999. Extracellular degradation of medium chain length poly(beta-hydroxyalkanoates) by Comamonas sp. Int. J. Biol. Macromol. 25:135-43
    • (1999) Int. J. Biol. Macromol. , vol.25 , pp. 135-143
    • Quinteros, R.1    Goodwin, S.2    Lenz, R.W.3    Park, W.H.4
  • 84
    • 0028322878 scopus 로고
    • A method for the isolation of microorganisms producing extracellular long-side-chain poly(β-hydroxyalkanoate) depolymerase
    • Ramsay BA, Saracovan I, Ramsay JA, Marchessault RH. 1994. A method for the isolation of microorganisms producing extracellular long-side-chain poly(β-hydroxyalkanoate) depolymerase. J. Environ. Polym. Degrad. 2:1-7
    • (1994) J. Environ. Polym. Degrad. , vol.2 , pp. 1-7
    • Ramsay, B.A.1    Saracovan, I.2    Ramsay, J.A.3    Marchessault, R.H.4
  • 85
    • 0035167677 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate degradation is associated with nucleotide accumulation and enhances stress resistance and survival of Pseudomonas oleovorans in natural water microcosms
    • Ruiz JA, Lopez NI, Fernandez RO, Mendez BS. 2001. Polyhydroxyalkanoate degradation is associated with nucleotide accumulation and enhances stress resistance and survival of Pseudomonas oleovorans in natural water microcosms. Appl. Environ. Microbiol. 67:225-30
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 225-230
    • Ruiz, J.A.1    Lopez, N.I.2    Fernandez, R.O.3    Mendez, B.S.4
  • 86
    • 0035190694 scopus 로고    scopus 로고
    • Cloning of an intracellular poly [D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product
    • Saegusa H, Shiraki M, Kanai C, Saito T. 2001. Cloning of an intracellular poly [D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product. J. Bacteriol. 183:94-100
    • (2001) J. Bacteriol. , vol.183 , pp. 94-100
    • Saegusa, H.1    Shiraki, M.2    Kanai, C.3    Saito, T.4
  • 88
    • 0027018085 scopus 로고
    • Intracellular degradation of poly(3-hydroxybutyrate) granules of Zoogloea ramigera I-16-M
    • Saito T, Saegusa H, Miyata Y, Fukui T. 1992. Intracellular degradation of poly(3-hydroxybutyrate) granules of Zoogloea ramigera I-16-M. FEMS Microbiol. Rev. 103:333-38
    • (1992) FEMS Microbiol. Rev. , vol.103 , pp. 333-338
    • Saito, T.1    Saegusa, H.2    Miyata, Y.3    Fukui, T.4
  • 89
    • 0024526245 scopus 로고
    • Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis
    • Saito T, Suzuki K, Yamamoto J, Fukui T, Miwa K, et al. 1989. Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. J. Bacteriol. 171:184-89
    • (1989) J. Bacteriol. , vol.171 , pp. 184-189
    • Saito, T.1    Suzuki, K.2    Yamamoto, J.3    Fukui, T.4    Miwa, K.5
  • 90
    • 0029125404 scopus 로고
    • Intracellular poly (3-hydroxybutyrate) depolymerase in Alcaligenes eutrophus
    • Saito T, Takizawa K, Saegusa H. 1995. Intracellular poly (3-hydroxybutyrate) depolymerase in Alcaligenes eutrophus. Can. J. Microbiol. 41(Suppl. 1):187-91
    • (1995) Can. J. Microbiol. , vol.41 , Issue.SUPPL. 1 , pp. 187-191
    • Saito, T.1    Takizawa, K.2    Saegusa, H.3
  • 92
    • 0034570978 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of oligomeric models of poly-3-hydroxybutyrate
    • Scherer TM, Fuller C, Goodwin S, Lenz RW. 2000. Enzymatic hydrolysis of oligomeric models of poly-3-hydroxybutyrate. Biomacromolecules 1:577-83
    • (2000) Biomacromolecules , vol.1 , pp. 577-583
    • Scherer, T.M.1    Fuller, C.2    Goodwin, S.3    Lenz, R.W.4
  • 93
    • 0028020870 scopus 로고
    • Molecular characterization of the extracellular poly(3-hydroxyoktanoic acid) [P(3HO)] depolymerase gene of Pseudomonas fluorescens GK13 and of its gene product
    • Schirmer A, Jendrossek D. 1994. Molecular characterization of the extracellular poly(3-hydroxyoktanoic acid) [P(3HO)] depolymerase gene of Pseudomonas fluorescens GK13 and of its gene product. J. Bacteriol. 176:7065-73
    • (1994) J. Bacteriol. , vol.176 , pp. 7065-7073
    • Schirmer, A.1    Jendrossek, D.2
  • 94
    • 0027462754 scopus 로고
    • Degradation of poly(3-hydroxyoctanoic acid), [P(3HO)], by bacteria. Purification and properties of a P(3HO) depolymerase of Pseudomonas fluorescens GK13 biovarV
    • Schirmer A, Jendrossek D, Schlegel HG. 1993. Degradation of poly(3-hydroxyoctanoic acid), [P(3HO)], by bacteria. Purification and properties of a P(3HO) depolymerase of Pseudomonas fluorescens GK13 biovarV. Appl. Environ. Microbiol. 59:1220-27
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1220-1227
    • Schirmer, A.1    Jendrossek, D.2    Schlegel, H.G.3
  • 95
    • 0029123499 scopus 로고
    • Substrate specificities of PHA-degrading bacteria and active site studies on the extracellular poly(3-hydroxyoctanoic acid) [P(3HO)] depolymerase of Pseudomonas fluorescens GK13
    • Schirmer A, Matz C, Jendrossek D. 1995. Substrate specificities of PHA-degrading bacteria and active site studies on the extracellular poly(3-hydroxyoctanoic acid) [P(3HO)] depolymerase of Pseudomonas fluorescens GK13. Can. J. Microbiol. 41(Suppl. 1):170-79
    • (1995) Can. J. Microbiol. , vol.41 , Issue.SUPPL. 1 , pp. 170-179
    • Schirmer, A.1    Matz, C.2    Jendrossek, D.3
  • 96
    • 0343674510 scopus 로고    scopus 로고
    • Poly (3-hydroxyvalerate) depolymerase of Pseudomonas lemoignei
    • Schöber U, Thiel C, Jendrossek D. 2000. Poly (3-hydroxyvalerate) depolymerase of Pseudomonas lemoignei. Appl. Environ. Microbiol. 66:1385-92
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1385-1392
    • Schöber, U.1    Thiel, C.2    Jendrossek, D.3
  • 97
    • 0015887907 scopus 로고
    • The regulation of poly-β-hydroxybutyrate metabolism in Azotobacter beijerinkii
    • Senior PJ, Dawes EA. 1973. The regulation of poly-β-hydroxybutyrate metabolism in Azotobacter beijerinkii. Biochem. J. 134:225-38
    • (1973) Biochem. J. , vol.134 , pp. 225-238
    • Senior, P.J.1    Dawes, E.A.2
  • 98
    • 0030585818 scopus 로고    scopus 로고
    • Determination of the active sites serine of the poly(3-hydroxybutyrate) depolymerases of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis
    • Shinohe T, Nojiri M, Saito T, Stanislawski T, Jendrossek D. 1996. Determination of the active sites serine of the poly(3-hydroxybutyrate) depolymerases of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis. FEMS Microbiol. Lett. 141:103-9
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 103-109
    • Shinohe, T.1    Nojiri, M.2    Saito, T.3    Stanislawski, T.4    Jendrossek, D.5
  • 99
    • 0030921217 scopus 로고    scopus 로고
    • Cloning of the gene for poly(3-hydroxybutyric acid) depolymerase of Comamonas testosteroni and functional analysis of its substrate-binding domain
    • Shinomiya M, Iwata T, Kasuya K, Doi Y. 1997. Cloning of the gene for poly(3-hydroxybutyric acid) depolymerase of Comamonas testosteroni and functional analysis of its substrate-binding domain. FEMS Microbiol. Lett. 154:89-94
    • (1997) FEMS Microbiol. Lett. , vol.154 , pp. 89-94
    • Shinomiya, M.1    Iwata, T.2    Kasuya, K.3    Doi, Y.4
  • 101
    • 0029090067 scopus 로고
    • Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acids inclusions
    • Steinbüchel A, Aerts K, Babel W, Föllner C, Liebergesell M, et al. 1995. Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acids inclusions. Can. J. Microbiol. 41(Suppl. 1):94-105
    • (1995) Can. J. Microbiol. , vol.41 , Issue.SUPPL. 1 , pp. 94-105
    • Steinbüchel, A.1    Aerts, K.2    Babel, W.3    Föllner, C.4    Liebergesell, M.5
  • 104
    • 0029018968 scopus 로고
    • Diversity of bacterial polyhydroxyalkanoic acids
    • Steinbiichel A, Valentin HE. 1995. Diversity of bacterial polyhydroxyalkanoic acids. FEMS Microbiol. Lett. 128:219-28
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 219-228
    • Steinbiichel, A.1    Valentin, H.E.2
  • 105
    • 0016233256 scopus 로고
    • Extracellular enzyme secretion by Pseudomonas lemoignei
    • Stinson MW, Merrick JM. 1974. Extracellular enzyme secretion by Pseudomonas lemoignei. J. Bacteriol. 119:152-61
    • (1974) J. Bacteriol. , vol.119 , pp. 152-161
    • Stinson, M.W.1    Merrick, J.M.2
  • 106
    • 0042097966 scopus 로고    scopus 로고
    • Intracellular depolymerase functionality and location in Pseudomonas oleovorans inclusions containing polyhydroxyalkanoate
    • Stuart ES, Foster LJR, Lenz RW, Fuller RC. 1996. Intracellular depolymerase functionality and location in Pseudomonas oleovorans inclusions containing polyhydroxyalkanoate. Int. J. Biol. Macromol. 19:171-76
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 171-176
    • Stuart, E.S.1    Foster, L.J.R.2    Lenz, R.W.3    Fuller, R.C.4
  • 107
    • 0034885218 scopus 로고    scopus 로고
    • Involvement of catalytic amino acid residues in enzyme-catalyzed polymerization for the synthesis of polyesters
    • Suzuki Y, Taguchi S, Saito S, Toshima K, Matsumura S, Doi Y. 2001. Involvement of catalytic amino acid residues in enzyme-catalyzed polymerization for the synthesis of polyesters. Biomacromolecules 2:541-44
    • (2001) Biomacromolecules , vol.2 , pp. 541-544
    • Suzuki, Y.1    Taguchi, S.2    Saito, S.3    Toshima, K.4    Matsumura, S.5    Doi, Y.6
  • 108
    • 0029006910 scopus 로고
    • Turnover of poly(3-hydroxybutyrate) (PHB) and its influence on the molecular mass of the polymer accumulated by Alcaligenes eutrophus during batch culture
    • Taidi B, Mansfield DA, Anderson AJ. 1995. Turnover of poly(3-hydroxybutyrate) (PHB) and its influence on the molecular mass of the polymer accumulated by Alcaligenes eutrophus during batch culture. FEMS Microbiol. Lett. 129:201-6
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 201-206
    • Taidi, B.1    Mansfield, D.A.2    Anderson, A.J.3
  • 109
    • 0034302593 scopus 로고    scopus 로고
    • Cloning and expression of the gene encoding thermostable poly(3-hydroxybutyrate) depolymerase
    • Takeda M, Kitashima K, Adachi K, Hanaoka Y, Suzuki I, Koizumi J. 2000. Cloning and expression of the gene encoding thermostable poly(3-hydroxybutyrate) depolymerase. J. Biosci. Bioeng. 90:416-21
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 416-421
    • Takeda, M.1    Kitashima, K.2    Adachi, K.3    Hanaoka, Y.4    Suzuki, I.5    Koizumi, J.6
  • 112
    • 0032912648 scopus 로고    scopus 로고
    • Relationship between succinate transport and production of extracellular poly(3-hydroxybutyrate) depolymerase in Pseudomonas lemoignei
    • Terpe K, Kerkhoff K, Pluta E, Jendrossek D. 1999. Relationship between succinate transport and production of extracellular poly(3-hydroxybutyrate) depolymerase in Pseudomonas lemoignei. Appl. Environ. Microbiol. 65:1703-9
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1703-1709
    • Terpe, K.1    Kerkhoff, K.2    Pluta, E.3    Jendrossek, D.4
  • 113
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinases A1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe T, Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H. 1994. The roles of the C-terminal domain and type III domains of chitinases A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176:4465-72
    • (1994) J. Bacteriol. , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 114
    • 0034643859 scopus 로고    scopus 로고
    • The FK520 gene cluster of Streptomyces hygroscopicus var. ascomyceticus (ATCC 14891) contains genes for biosynthesis of unusual polyketide extender units
    • Wu K, Chung L, Revill WP, Katz L, Reeves CD. 2000. The FK520 gene cluster of Streptomyces hygroscopicus var. ascomyceticus (ATCC 14891) contains genes for biosynthesis of unusual polyketide extender units. Gene 251:81-90
    • (2000) Gene , vol.251 , pp. 81-90
    • Wu, K.1    Chung, L.2    Revill, W.P.3    Katz, L.4    Reeves, C.D.5
  • 115
    • 0034894206 scopus 로고    scopus 로고
    • Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes facalis T1 by using a quartz crystal microbalance
    • Yamashita K, Aoyagi Y, Abe H, Doi Y. 2001. Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes facalis T1 by using a quartz crystal microbalance. Biomacromolecules 2:25-28
    • (2001) Biomacromolecules , vol.2 , pp. 25-28
    • Yamashita, K.1    Aoyagi, Y.2    Abe, H.3    Doi, Y.4
  • 116
    • 0034977798 scopus 로고    scopus 로고
    • Accumulation of the PhaP phasin of Ralstonia eutropha is dependent on production of polyhydroxybutyrate in cells
    • York GM, Junker BH, Stubbe JA, Sinskey AJ. 2001. Accumulation of the PhaP phasin of Ralstonia eutropha is dependent on production of polyhydroxybutyrate in cells. J. Bacteriol. 183:4217-26
    • (2001) J. Bacteriol. , vol.183 , pp. 4217-4226
    • York, G.M.1    Junker, B.H.2    Stubbe, J.A.3    Sinskey, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.