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1.
Braz. arch. biol. technol ; Braz. arch. biol. technol;62: e19180360, 2019. tab, graf
Artigo em Inglês | LILACS | ID: biblio-1055421

RESUMO

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.


Assuntos
Oxirredutases , Catecóis , Polifenóis , Pseudomonas , Biodegradação Ambiental
2.
Bioprocess Biosyst Eng ; 39(11): 1759-73, 2016 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-27450069

RESUMO

A newly isolated microbial strain of thermophilic genus Geobacillus has been described with emphasis on polyphasic characterization and its application for degradation of hydrogen peroxide. The validation of this thermophilic strain of genus Geobacillus designated as BSS-7 has been demonstrated by polyphasic taxonomy approaches through its morphological, biochemical, fatty acid methyl ester profile and 16S rDNA sequencing. This thermophilic species of Geobacillus exhibited growth at broad pH and temperature ranges coupled with production of extraordinarily high quantities of intracellular catalase, the latter of which as yet not been reported in any member of this genus. The isolated thermophilic bacterial culture BSS-7 exhibited resistance against a variety of organic solvents. The immobilized whole cells of the bacterium successfully demonstrated the degradation of hydrogen peroxide (H2O2) in a packed bed reactor. This strain has potential application in various analytical and diagnostic methods in the form of biosensors and biomarkers in addition to applications in the textile, paper, food and pharmaceutical industries.


Assuntos
Proteínas de Bactérias , Catalase , Geobacillus/enzimologia , Peróxido de Hidrogênio/química , Proteínas de Bactérias/biossíntese , Proteínas de Bactérias/química , Proteínas de Bactérias/isolamento & purificação , Catalase/biossíntese , Catalase/química , Catalase/isolamento & purificação , Geobacillus/genética , Concentração de Íons de Hidrogênio , RNA Bacteriano/genética , RNA Ribossômico 16S/genética
3.
Braz. arch. biol. technol ; Braz. arch. biol. technol;56(5): 711-721, Sept.-Oct. 2013. graf, tab
Artigo em Inglês | LILACS | ID: lil-689798

RESUMO

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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