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Title: High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production
Authors: Guzik, Urszula
Hupert-Kocurek, Katarzyna
Sitnik, Małgorzata
Wojcieszyńska, Danuta
Keywords: cis,cis-muconic acid production; Stenotrophomonas; Catechol 1,2-dioxygenase; Substrate specificity; Kinetic
Issue Date: 2013
Citation: Antonie van Leeuwenhoek, Vol. 103, iss. 6 (2013), s. 1297-1307
Abstract: This is the first report of a catechol 1,2- dioxygenase from Stenotrophomonas maltophilia strain KB2 with high activity against catechol and its methyl derivatives. This enzyme was maximally active at pH 8.0 and 40 C and the half-life of the enzyme at this temperature was 3 h. Kinetic studies showed that the value of Km and Vmax was 12.8 lM and 1,218.8 U/mg of protein, respectively. During our studies on kinetic properties of the catechol 1,2- dioxygenase we observed substrate inhibition at [80 lM. The nucleotide sequence of the gene encoding the S. maltophilia strain KB2 catechol 1,2- dioxygenase has high identity with other catA genes from members of the genus Pseudomonas. The deduced 314-residue sequence of the enzyme corresponds to a protein of molecular mass 34.5 kDa. This enzyme was inhibited by competitive inhibitors (phenol derivatives) only by ca. 30 %. High tolerance against condition changes is desirable in industrial processes. Our data suggest that this enzyme could be of use as a tool in production of cis,cis-muconic acid and its derivatives.
DOI: 10.1007/s10482-013-9910-8
ISSN: 0003-6072
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