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  • 11
    Electronic Resource
    Electronic Resource
    Identification of Ca2+/calmodulin-dependent protein kinase and endogenous substrate of Fusarium oxysporum (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 94 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Ca2+/calmodulin-dependent phosphorylation and cross-reactivity between anti-rat brain Ca2+/calmodulin-dependent protein kinase II (CaMK) antibody and partially purified CaMK from Fusarium oxysporum were detected in the component of high-molecular mass (Mr 〉 100 000). In vitro, Ca2+/CaM-dependent phosphorylation of only a 16-kDa protein was detected. The 16-kDa protein was localized in the membrane fraction. Amino acid sequence of one of the peptides derived from partial hydrolysis of the 16-kDa protein had a high homology (65.5%) with the bovine transducin β chain. It is assumed that the 16-kDa protein is an endogenous substrate of F. oxysporum CaMK.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05283.x
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  • 12
    Electronic Resource
    Electronic Resource
    Identification of the intracellular polyhydroxyalkanoate depolymerase gene of Paracoccus denitrificans and some properties of the gene product (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 196 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Paracoccus denitrificans degraded poly(3-hydroxybutyrate) (PHB) in the cells under carbon source starvation. Intracellular poly(3-hydroxyalkanoate) (PHA) depolymerase gene (phaZ) was identified near the PHA synthase gene (phaC) of P. denitrificans. Cell extract of Escherichia coli carrying lacZ–phaZ fusion gene degraded protease-treated PHB granules. Reaction products were thought to be mainly d(−)-3-hydroxybutyrate (3HB) dimer and 3HB oligomer. Diisopropylfluorophosphonate and Triton X-100 exhibited an inhibitory effect on the degradation of PHB granules. When cell extract of the recombinant E. coli was used, Mg2+ ion inhibited PHB degradation. However, the inhibitory effect by Mg2+ ion was not observed using the cell extract of P. denitrificans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10558.x
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  • 13
    Electronic Resource
    Electronic Resource
    PhaR, a protein of unknown function conserved among short-chain-length polyhydroxyalkanoic acids producing bacteria, is a DNA-binding protein and represses Paracoccus denitrificans phaP expression in vitro (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 200 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A putative regulatory protein, PhaR, which was identified in the polyhydroxyalkanoic acid synthetic locus (phaZCPR) in Paracoccus denitrificans, was investigated. The PhaR protein purified from a recombinant Escherichia coli was estimated to be 22 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, being consistent with the mass calculated from the nucleotide sequence. The molecular mass was determined to be 93 kDa by size-exclusion chromatography, suggesting that the protein formed a tetramer. A gel mobility shift assay showed that PhaR specifically bound to the intergenic region of phaC–phaP. In a cell-free protein synthesis system using E. coli S30 extract, the expression of the phaP gene was repressed by the addition of purified PhaR. These results suggest that PhaR is a DNA-binding protein and may play a role in the regulation of phaP gene expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10685.x
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  • 14
    Electronic Resource
    Electronic Resource
    Purification and properties of d-(−)-3-hydroxybutyrate oligomer hydrolase of Paracoccus denitrificans (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 206 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: d-(−)-3-Hydroxybutyrate (3HB) oligomer hydrolase was purified from Paracoccus denitrificans. The enzyme was a monomeric protein with an approximate molecular mass of 31 kDa. The isoelectric point of the enzyme was 5.2. Optimum temperature and pH were 35–40°C and 8.0, respectively. The enzyme activity was not affected by sulfhydryl reagents but strongly inhibited by serine proteinase inhibitors. Both 3HB trimer and 3HB dimer were hydrolyzed by the enzyme, indicating that the enzyme is not 3HB dimer hydrolase but 3HB oligomer hydrolase. para-Nitrophenyl esters of short-chain fatty acids were also hydrolyzed by the enzyme. 3HB dimer was hydrolyzed somewhat faster than 3HB trimer. The level of the enzyme activity was almost constant, irrespective of carbon sources for the bacterial growth and of the cultivation conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11006.x
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  • 15
    Electronic Resource
    Electronic Resource
    Continuous Hydrolysis of Olive Oil by Lipase in Microporous Hydrophobic Membrane Bioreactor (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 501 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb45713.x
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  • 16
    Electronic Resource
    Electronic Resource
    Continuous Synthesis of Glycerides by Lipase in a Microporous Membrane Bioreactor (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 434 (1984), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1984.tb29892.x
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  • 17
    Electronic Resource
    Electronic Resource
    Polyhydroxyalkanoate synthesis from alcohols during the growth of Paracoccus denitrificans (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 135 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Several alcohols were examined as substrates for the polyhydroxyalkanoate synthesis by Paracoccus denitrificans. The bacterium synthesized a homopolyester of poly(3-hydroxybutyrate) from ethanol. When n-pentanol was used as growth substrate, homopolyester poly(3-hydroxyvalerate) was synthesized, whereas copolyester poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulated during bacterial growth on n-propanol. When alcohols were automatically fed as growth substrates, ethanol, n-propanol, and n-pentanol gave higher polyester content. Although poly(3-hydroxybutyrate) was synthesized from methanol or n-butanol, its content was very low. Under nitrogen-deficient conditions, polyester;content in cells increased, especially with ethanol, n-propanol, and n-pentanol. Using a mixture of two alcohols P. denitrificans could synthesize polyesters with varying relative ratios of 3-hydroxybutyrate to 3-hydroxyvalerate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb07991.x
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  • 18
    Electronic Resource
    Electronic Resource
    Analysis of β-ketothiolase and acetoacetyl-CoA reductase genes of a methylotrophic bacterium, Paracoccus denitrifleans, and their expression in Escherichia coli (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 133 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The β-ketothiolase gene (phaA) and acetoacetyl-CoA reductase gene (phaB) were isolated from Paracoccus denitrificans. Nucleotide sequence analysis showed that they encoded proteins of 391 amino acids with a molecular mass of 40744 Da and of 242 amino acids with a molecular mass of 25614 Da, respectively. The predicted gene products exhibited high amino acid identities with those from other bacteria: 64.4–74.0% for the phaA gene product and 47.6–80.6% for the phaB gene product, respectively. Both genes were co-transcribed in a recombinant Escherichia coli. In addition, promoter activity was detected upstream of the phaA gene. Hence, the two genes are organized as an operon, phaA-phaB, in P. denitrificans. NADH was preferred to NADPH as a cofactor of acetoacetyl-CoA reductase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07865.x
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  • 19
    Electronic Resource
    Electronic Resource
    Cultivation engineering of microbial bioplastics production (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 103 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Theoretical yields of poly-d(−)-3-hydroxybutyrate (PHB) from several carbon sources have been estimated from biochemical pathways leading to PHB. In estimating the yields, a special emphasis is made on recycling (or regeneration) of NADP+ which is the co-substrate of acetoacetyl-CoA reductase, one of three key enzymes involved in the biosynthesis of PHB. As a NADP+-regenerating enzyme, glucose-6-phosphate dehydrogenase or isocitrate dehydrogenase is conceived. Theoretical and observed yields have been compared when polyhydroxyalkanoates (PHA) were synthesized from methanol and from n-amyl alcohol by a methylotroph, Paracoccus denitrificans.An equation, which predicts the overall yield of PHB when allowance is made for non-PHB biomass formation in actual bacterial PHB production, has been derived as a function of both theoretical yields and PHB content of the total dry cell mass. The ratio of the overall (yield) to be theoretical yield is roughly proportional to the PHB content. A novel specific PHB formation rate on the basis of the residual biomass (total biomass-PHB contained) was proposed. The specific PHB formation rate decreased according to a mono-molecular decay model whose decay constant depended solely on the C/N ratio of the feed solution. From this model, an equation has been derived to calculate the volumetric productivity of PHB on the assumption that the total amount of the residual biomass is unchanged in the nitrogen-deficient PHB formation phase. Also, a graphical procedure has been shown to calculate the volumetric productivity of PHB. A comparison has been made between several data of PHB productivities that have been calculated from the literature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05846.x
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  • 20
    Electronic Resource
    Electronic Resource
    Repeated batch and continuous operations for phosphatidylglycerol synthesis from phosphatidylcholine with immobilized phospholipase D (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 146-151 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The repeated batch and continuous operations for transphosphatidylation reaction were carried out for phosphatidylglycerol (PG) synthesis from phosphatidylcholine (PC) with the help of immobilized cabbage phospholipase D (PLD) in the presence of glycerol. The biphasic reaction system was used which included the aqueous phase containing immobilized PLD along with high concentrations of glycerol (30%–50%) and buffer, whereas the main part of substrate (PC) and products (mainly PG) formed were in the organic phase (diethyl ether). Octyl-Sepharose CL-4B having a hydrophobic octyl group was chosen for the PLD immobilization. Both immobilization yield and activity yield of immobilized enzyme were 100%. The effects of solvents, temperature and glycerol concentrations on the immobilized PLD were examined. Repeated batch conversion of PC (15 g/l) to PG was examined with the immobilized PLD in 30% glycerol. In all five batch cycles examined, 100% selectivity was obtained and there was no significant decrease in the fractional conversion of PC to PG (98%–99%) in the first three batch cycles. In the cases of a packed-bed reactor (PBR) and a continuous stirred-tank reactor (CSTR) used for continuous synthesis of PG with the immobilized PLD, the operational stabilities of the immobilized enzyme were almost the same (half life=14 h at 30°C) when purified PC was used, while in the case of partially purified PC in CSTR the half life increased more than five times.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00251937
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