Abstract
The combined analysis of peptide mass fingerprinting and 2-DE/MS using the induced and selected protein spots following growth of Pseudomonas sp. DU102 on benzoate or p-hydroxybenzoate revealed not only α- and β-subunits of protocatechuate 3,4-dioxygenase but also catechol 1,2-dioxygenase responsible for ortho-pathway through ring-cleavage of aromatic compounds. Toluate 1,2-dioxygenase and p-hydroxybenzoate hydroxylase were also identified. Purification of intradiol dioxygenases such as catechol 1,2-dioxygenase and protocatechuate 3,4-dioxygenase from the benzoate or p-hydroxybenzoate culture makes it possible to trace the biodegradation pathway of strain DU102 for monocyclic aromatic hydrocarbons. Interestingly, vanillin-induced protocatechuate 3,4-dioxygenase was identical in amino acid sequences with protocatechuate 3,4-dioxygenase from p-hydroxybenzoate.
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Acknowledgement
This work was supported by Basic Research Program funded by the Korean Basic Science Institute (N26047) and Korea Research Foundation Grant (KRF-2004-041-D00375). We thank Dr. Young Hwan Kim (Korea Basic Science Institute) for technical support of MS analysis.
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Kim, S.I., Park, SH., Kim, JW. et al. Peptide mass fingerprinting- and 2-DE/MS-based analysis of the biodegradation potential for monocyclic aromatic hydrocarbons in Pseudomonas sp.. Biotechnol Lett 29, 1475–1481 (2007). https://doi.org/10.1007/s10529-007-9443-1
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DOI: https://doi.org/10.1007/s10529-007-9443-1