Purification and characterization of a peroxidase present in xilopodium exsudates of umbu plants (Spondias tuberosa A.).

• Autor(a) principal: PINTO, M. dos S. T.
• Data de Publicação: 2015
• Outros Autores: RIBEIRO, J. M., ARAUJO, F. P. de, MELO, N. F. de, FERNANDES, K. V. S.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
• Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1019494
• topic: Spondia tuberosa; Guaiacol peroxidase; Root enzyme; Tssue brownig; Umbu; Caatinga; Peroxidase

Umbu plants are drought resistant trees which are able to store water and several other substances into its adapted root, named xylopodium. The exsudate from xilopodium is a natural solution rich in salts, sugars and a little concentration of proteins. In this work, we report the purification of a peroxidase (POX) from umbu xilopodium exsudate by direct extraction from polyacrylamide electrophoresis gels. Umbu POX showed optimum activity at pHs around 6.0 to 7.0 and high thermal resistance after incubation at 7 0°C for 6 min. POX activity present in crude extracts was more heat - resistant than in its purified form. When assayed with metal ions, umbu POX activity was shown to be inhibited by Mn 2+ and stimulated by Ca 2+ and Mg 2+ ; it was also inhibited by sodium azid e (concentrations higher then 1 mM) and not inhibited by either EDTA or tropolone. POX Km values for guaiacol and methylcatechol substrates were 6.83 and 22.25, respectively. The enzyme is proposed to be a guaiacol peroxidase and was seen to be located at higher concentrations in the outermost layers of xylopodium tissue, such as the endoderm.