Use este identificador para citar ou linkar para este item: http://repositorio.ufla.br/jspui/handle/1/12542
Registro completo de metadados
Campo DCValorIdioma
dc.creatorChagas, Pricila Maria Batista-
dc.creatorTorres, Juliana Arriel-
dc.creatorSilva, Maria Cristina-
dc.creatorNogueira, Francisco Guilherme Esteves-
dc.creatorSantos, Custódio Donizete dos-
dc.creatorCorrêa, Angelita Duarte-
dc.date.accessioned2017-03-23T18:39:20Z-
dc.date.available2017-03-23T18:39:20Z-
dc.date.issued2014-11-
dc.identifier.citationCHAGAS, P. M. B. et al. Catalytic stability of turnip peroxidase in free and immobilized form on chitosan beads. International Journal of Current Microbiology and Applied Sciences, Tamilnadu, v. 3, n. 11, p. 576-595, Nov. 2014.pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/12542-
dc.description.abstractChitosan beads were prepared, using glutaraldehyde as a cross linking agent for the immobilization of turnip peroxidase (TP). The morphology and structure of materials were examined by X-ray diffraction and scanning electron microscopy. The activity of free and immobilized TP was studied. The optimum pH was 7.0 for both free and immobilized enzyme and both were active in the temperature range between 30 oC and 50 oC. It was found that storage stability of the immobilized enzyme was better than that of the free enzyme. Both free and immobilized enzymes were used in the color removal of the dye Remazol Brilliant Blue R (RBBR). In discoloration experiments with immobilized TP, two phenomena were observed: discoloration, due to adsorption on the support (60.45%) and dye degradation, due to the enzyme action (27.50%). The free enzyme removed 62.86% of the color. The immobilized enzyme showed a potential of 61.17% for the removal of the dye color after 6 consecutive cycles.pt_BR
dc.languageen_USpt_BR
dc.publisherIJCMASpt_BR
dc.rightsacesso abertopt_BR
dc.sourceInternational Journal of Current Microbiology and Applied Sciencespt_BR
dc.subjectTurnip peroxidasept_BR
dc.subjectDiscolorationpt_BR
dc.subjectGlutaraldehydept_BR
dc.subjectRemazolpt_BR
dc.titleCatalytic stability of turnip peroxidase in free and immobilized form on chitosan beadspt_BR
dc.typeArtigopt_BR
Aparece nas coleções:DQI - Artigos publicados em periódicos

Arquivos associados a este item:
Arquivo Descrição TamanhoFormato 
ARTIGO_Catalytic stability of turnip peroxidase in free and immobilized form on chitosan beads.pdf2,05 MBAdobe PDFVisualizar/Abrir


Este item está licenciada sob uma Licença Creative Commons Creative Commons