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    Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/18869

    Title: Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source
    Authors: Wang, Chuan-Lu;You, Su-Lin;Wang, San-Lang
    Contributors: 淡江大學生命科學研究所
    Keywords: Amino acids;Aromatic hydrocarbons;Bacteria;Bioconversion;Characterization;Enzymes;Monomers;pH;Benzoate-assimilating bacterium;Catechol 1,2-dioxygenase;Catechol production;Pyrogallol;Enzyme kinetics;Bacteria (microorganisms);Pseudomonas aeruginosa
    Date: 2006-07
    Issue Date: 2013-02-27 09:38:43 (UTC+8)
    Publisher: Camden: Elsevier Ltd
    Abstract: Pseudomonas aeruginosa TKU002, capable of growing significantly on acidic side pH 5.5 and benzoic acid as a sole carbon source, was isolated from enrichment culture accumulation of catechol. An intracellular catechol 1,2-dioxygenase (CD) produced by P. aeruginosa TKU002 was purified and characterized. The TKU002 CD was found to have unique characteristics different to other microbial CDs. The unique characteristics include the smallest molecular mass of 22 kDa, the most acidic pI value of lower than 4, and the highest cleavage activity to the substrate, pyrogallol. Different to other CD producing strains, P. aeruginosa TKU002 produced CD at a lower pH of 5.5 when benzoate was used as the sole carbon source. The TKU002 CD was a monomer with a Km of 5.9 μM. The TKU002 CD showed 36% and 14% sequence coverage rate with protocatechuate 3,4-dioxygenase β-subunit of P. aeruginosa UCBPP-COG3485 and catechol 1,2-dioxygenase of P. aeruginosa PA01, respectively, and possessed one matched peptide (YLWDDFAYATR). In conclusion, this is the first report of a microbial CD with the smallest molecular mass, the most acidic pI value, the highest specific activity to the substrate pyrogallol, and the most acidic medium for CD production.
    Relation: Process Biochemistry 41(7), pp.1594-1601
    DOI: 10.1016/j.procbio.2006.03.008
    Appears in Collections:[Graduate Institue of Life Sciences] Journal Article

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