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1.
Braz. arch. biol. technol ; 62: e19180360, 2019. tab, graf
Article in English | LILACS | ID: biblio-1055421

ABSTRACT

Abstract Catecholase (EC 1.10.3.1), an oxidoreductase enzyme is a key member of polyphenol oxidase family which catalyze the degradation of catechol. This enzyme possesses vast applications in diverse areas and is found in bacteria, fungi, mushrooms, higher plants, arthropods, amphibians and mammals. Catechol, a phenolic compound, is used as a starting material in the synthesis of various industrial compounds such as inhibitors, antioxidants, pesticides etc. The release of this phenolic compound in the environment causes toxicity to both flora and fauna. In the present studies, emphasis has been laid on isolation, screening and characterization of catechol degrading bacterium coupled with synthesis of catecholase enzyme. Further, the selected isolated strain was phenotypically characterized and was found to be member of genus Pseudomonas. Among all the isolates, BSC-6 was found as best isolate with maximum extracellular catecholase activity of 152.32 IU/L obtained after scale up studies. The herein synthesized bacterial catecholase may be employed for wide applications particularly in bioremediation of phenol enriched polluted sites.


Subject(s)
Oxidoreductases , Catechols , Polyphenols , Pseudomonas , Biodegradation, Environmental
2.
Braz. arch. biol. technol ; 56(5): 711-721, Sept.-Oct. 2013. graf, tab
Article in English | LILACS | ID: lil-689798

ABSTRACT

The aim of the present work was to study the influence of multiple bioprocess parameters for the maximum production of lipase from Pseudomonas sp. BWS-5. The culture reached the stationary phase of growth after 36h of incubation when the maximum lipase production was obtained at flask level. The different media components such as carbon sources, nitrogen sources, trace elements and process parameters such as the pH of the medium, temperature and time of incubation, agitation/stationary conditions, etc. were optimized at flask level and at bioreactor level. The maximum enzyme production of 298 IU/mL was obtained with the use of simple medium with pH 6.5 containing glucose (1 %, w/v), peptone (3 %, w/v) and KCl (0.05 %, w/v) after 30h of incubation at 37°C under agitation (200 rpm) conditions with 0.75 vvm of air supply.

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