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Poly-/3-hydroxybutyrate depolymerase

PhaZ Poly(3-hydroxybutyrate) depolymerase PhaZc Hydroxybutyrate-dimer hydrolase... [Pg.51]

Biodegradable, aliphatic polyesters can be synthesized or produced by bacteria and cyanobacteria. These organisms accumulate poly(3-hydroxy butyrate) (PHB) up to 80 wt% of the dry cellular material. Long branching has been produced by modifying the culture medium [Ramsay et ah, 1991]. PHB is degraded by the enzyme poly(3-hydroxybutyrate depolymerase). [Pg.1155]

Kumar A, Gross RA, Jendrossek D (2000) Poly(3-hydroxybutyrate)-depolymerase from Pseudomonas lemoignei catalysis of esterifications in organic media. J Org Chem 65 7800-7806... [Pg.115]

Abe T, Kobayashi T, Seiito T (2005) Properties of a novel intracellular poly(3-hydroxybutyrate) depolymerase with high specific activity (PhaZd) in Wautersia eutiopha H16. J Bacteriol 187 6982-6990... [Pg.314]

Brucato CL, Wong SS (1991) Extracellular poly(3-hydroxybutyrate) depolymerase from PeniciUium funiculosum general characteristics and active site studies. Arch Biochem Biophys 290 497-502... [Pg.314]

Fukui T, Narikawa T, Miwa T, Shirakawa Y, Saito T, Tomita K (1998) Effect of limited tijrptic modification of a bacterial poly(3-hydroxybutyrate) depolymerase on its catolytic activity. Biochem Biophys Acta 952 164—171... [Pg.315]

Hiraishi T, Ohura T, Ito S, Kasuya K, Doi Y (2000) Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri. Biomacromolecules 1 320-324... [Pg.315]

Kobayashi T, Saito T (2003) Catalytic triad of intracellular poly(3-hydroxybutyrate) depolymerase (PhaZl) in Ralstonia eutropha H16. J Biosci Bioeng 96 487-492 Kobayashi T, Shiraki M, Abe T, Sugiyama M, Saito T (2003) Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase. J Bacteriol 185 3485-3490... [Pg.317]

Miyazaki S, Takahashi K, Shiraki M, Saito T, Tezuka Y, Kasuya K (2000) Properties of a poly(3-hydroxybutyrate) depolymerase from Penicillium funiculosum. J Polym Environ 8 175-182 Mukai K, Yamada K, Doi Y (1992) Extracellular polyhydroxyalkanoate depolymerases and their inhibitor from Pseudomonas lemoignei. Int 1 Biol Macromol 14 235-239 MiiUer B, Jendrossek D (1993) Purification and properties of poly(3-hydroxyvaleric acid) depolymerase from Pseudomonas lemoignei. Appl Microbiol Biotechnol 38 487-492 Murase T, Iwata T, Doi T (2001a) Direct observation of enzymatic degradation behavior of poly[(R)-3-hydroxybutyrate] lamellar single crystals by atomic force microscopy. Macromolecules 34 5848-5853... [Pg.318]

Tanio T, Fukui T, Shirakura Y, Saito T, Tomita K, Kaiho T, Masamune S (1982) An extracellular poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. Eur J Biochem 124 71-77 Tesema Y, Raghavan D, Stubbs J (2(X)5) Bone cell viabUity on methacrylic add grafted and collagen immobilized porous poly(3-hydroxybutyrate-co-3-hydroxyvalerate). J Appl Polym Sd 98(5) 1916-1921... [Pg.320]

Tseng CL, Chen HJ, Shaw GC (2006) Identification and characterization of the Bacillus thuringi-ensis phaZ gene, encoding new intracellular poly-3-hydroxybutyrate depolymerase. J Bacteriol 188 7592-7599... [Pg.320]

Sugiyama A, Kobayashi T, Shiraki M, Saito T. Roles of poly(3-hydroxybutyrate) depolymerase and 3HB-oUgomer hydrolase in bacterial PHB metabolism. Curr Microbiol 2004 48 424-427. [Pg.168]

Shirakura, Y, Fukui, T., Saito, T., Okamoto, Y, Narikawa, T, Koide, K., Tomita, K., Takemasa, T. and Masamune, S. (1986), Degradation of poly(3-hydroxybutyrate) by poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis Tj , Biochim. Biophys. Acta. 880 (1), 46-53. [Pg.35]

Klingbeil B, Kroppenstedt RM, Jendrossek D (1996), Taxonomic identification of Streptomyces exfoliatus KIO and characterization of its poly(3-hydroxybutyrate) depolymerase gene , FEMS Microbiol Lett, 142, 215-221. [Pg.400]

Nakayama K, Saito T, Fukui T, Shirakura Y, Tomita K (1985), Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerases from pseudomonas-lemoigneV, Biochem Biophys Acta, 827, 63-72. [Pg.403]

Yamashita K, Funato T, Suzuki Y, Teramachi S, Doi Y (2003) Characteristic interactions between poly(hydroxybutyrate) depolymerase and poly [(R)-3-hydroxybutyrate] film studied by a quartz crystal microbalance. Macromol Biosci 3 694—702 Yang L, Setyowati K, Li A, Gong S, Chen J (2008) Reversible infrared actuation of carbon nanotube-liquid crystalline elastomer nanocomposites. Adv Mater 20 2271-2275 Yu C, Shi L, Yao Z, Li D, Majumdar A (2005) Thermal conductance and thermopower of an individual single-wall carbon nanotube. Nano Lett 5 1842-1846 Yu H, Qin Z, Zhou Z (2011) Cellulose nanocrystals as green fillers to improve crystallization and hydrophilic property of poly(3-hydroxybut3uate-co-3-hydroxyvalerate). Prog Nat Sci Mater Int 21 478 84... [Pg.108]

Polyesters, such as microbially produced poly[(P)-3-hydroxybutyric acid] [poly(3HB)], other poly[(P)-hydroxyalkanoic acids] [poly(HA)] and related biosynthetic or chemosynthetic polyesters are a class of polymers that have potential applications as thermoplastic elastomers. In contrast to poly(ethylene) and similar polymers with saturated, non-functionalized carbon backbones, poly(HA) can be biodegraded to water, methane, and/or carbon dioxide. This review provides an overview of the microbiology, biochemistry and molecular biology of poly(HA) biodegradation. In particular, the properties of extracellular and intracellular poly(HA) hydrolyzing enzymes [poly(HA) depolymerases] are described. [Pg.289]

All purified poly(HA) depolymerases are specific for either poly(HASCL) or poly(HAMCL). Even a poly(3HB) depolymerase of S. exfoliatus K10, a strain that degrades both poly(3HB) and poly(3HO), is specific for poly(HASCL) [49]) indicating at least one additional depolymerase with specificity for poly(HAMCL) in S. exfoliatus. Experiments with copolymers consisting of 3-hydroxybutyrate and 3-hydroxyhexanoate and A.faecalis T1 poly(3HB) depolymerase are in agreement with the results obtained with poly(HASCL) and poly(HAMCL) the depolymerase was not able to hydrolyze ester bonds between two 3HAMCL monomers and between 3-hydroxybutyrate and 3-hydroxyhexanoate [50]. [Pg.298]

Hydrolysis of end-labeled 3-hydroxybutyrate oligomers by purified A. faecalis T poly(3HB) depolymerase showed that the enzyme mainly cleaved the second and third ester linkage from the hydroxyl terminus [69]. However, since the enzyme also hydrolyzes cyclic oligomers, the A. faecalis depolymerase has endo-hydrolase activity in addition to exo-hydrolase activity [18, 70]. Results of... [Pg.306]

The first products of enzymatic hydrolysis of poly(3HB) by purified poly(3HB) depolymerases are a mixture of monomeric and/or oligomeric 3-hydroxybuty-rate esters. Some enzymes are able to hydrolyze oligomers and dimers to monomeric 3-hydroxybutyrate after prolonged time of hydrolysis in the presence of an excess of the appropriate depolymerase. These poly(3HB) depolymerases have high endogenous dimer-hydrolase activities (e.g., the poly(3HB) depolymerases of Comamonas strains, P. stutzeri, S. exfoliatus, and the depolymerases... [Pg.308]

The i-poly(3HB) depolymerase of R. rubrum is the only i-poly(3HB) depolymerase that has been purified [174]. The enzyme consists of one polypeptide of 30-32 kDa and has a pH and temperature optimum of pH 9 and 55 °C, respectively. A specific activity of 4 mmol released 3-hydroxybutyrate/min x mg protein was determined (at 45 °C). The purified enzyme was inactive with denatured poly(3HB) and had no lipase-, protease-, or esterase activity with p-nitro-phenyl fatty acid esters (2-8 carbon atoms). Native poly(3HO) granules were not hydrolyzed by i-poly(3HB) depolymerase, indicating a high substrate specificity similar to extracellular poly(3HB) depolymerases. Recently, the DNA sequence of the i-poly(3HB) depolymerase of R. eutropha was published (AB07612). Surprisingly, the DNA-deduced amino acid sequence (47.3 kDa) did not contain a lipase box fingerprint. A more detailed investigation of the structure and function of bacterial i-poly(HA) depolymerases will be necessary in future. [Pg.316]

Numata K, Sato S, Fujita M, Tsuge T, Iwata T, Doi Y (2007) Adsorption effects of poly(hydroxybutyric add) depolymerase on chain-folding surface of polyester single crystals revealed by mutant enzyme and frictional force microscopy. Polym Degrad Stab 92 176-183 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 65 189-197... [Pg.319]

York GM, Lupberger 1, Han 1, Lawrence AG, Stubbe 1, Sinskey AJ (2003) Ralstonia eutrvpha H16 encodes two and possibly three intracellular poly[D-(-)-3-hydroxybutyrate] depolymerase genes. J Bacteriol 185 3788-3794... [Pg.322]

Tanio T, Fukui T, Saito T, Tomita K, Kaiho T, Masamune S (1982) An extracellular poly(P-hydroxybutyrate) depolymerase from Alcaligenes faecalis. Eur J Biochem 124 71-77... [Pg.340]


See other pages where Poly-/3-hydroxybutyrate depolymerase is mentioned: [Pg.15]    [Pg.62]    [Pg.318]    [Pg.319]    [Pg.116]    [Pg.337]    [Pg.339]    [Pg.292]    [Pg.309]    [Pg.311]    [Pg.315]    [Pg.32]    [Pg.15]    [Pg.58]    [Pg.62]    [Pg.318]    [Pg.319]    [Pg.174]    [Pg.296]    [Pg.302]    [Pg.313]    [Pg.315]    [Pg.319]    [Pg.116]    [Pg.336]    [Pg.337]    [Pg.339]   
See also in sourсe #XX -- [ Pg.85 ]




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