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Registro Completo |
Biblioteca(s): |
Embrapa Semiárido. |
Data corrente: |
08/07/2015 |
Data da última atualização: |
03/05/2017 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
PINTO, M. dos S. T.; RIBEIRO, J. M.; ARAUJO, F. P. de; MELO, N. F. de; FERNANDES, K. V. S. |
Afiliação: |
MARCIO DOS SANTOS TEIXEIRA PINTO, Universidade Federal do Tocantins - UFT; JULIANA MARTINS RIBEIRO, CPATSA; FRANCISCO PINHEIRO DE ARAUJO, CPATSA; NATONIEL FRANKLIN DE MELO, CPATSA; KÁTIA VALEVSKI SALES FERNANDES, Universidade Estadual do Norte Fluminense Darcy Ribeiro - UENF. |
Título: |
Purification and characterization of a peroxidase present in xilopodium exsudates of umbu plants (Spondias tuberosa A.). |
Ano de publicação: |
2015 |
Fonte/Imprenta: |
African Journal of Biotechnology, v. 14, n. 21, p. 1838-1845, 2015. |
DOI: |
10.5897/AJB2015.14521 |
Idioma: |
Inglês |
Conteúdo: |
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. |
Palavras-Chave: |
Guaiacol peroxidase; Root enzyme; Spondia tuberosa; Tssue brownig. |
Thesagro: |
Caatinga; Peroxidase; Umbu. |
Categoria do assunto: |
F Plantas e Produtos de Origem Vegetal |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/126327/1/Juliana-2015.pdf
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Marc: |
LEADER 01940naa a2200265 a 4500 001 2019494 005 2017-05-03 008 2015 bl uuuu u00u1 u #d 024 7 $a10.5897/AJB2015.14521$2DOI 100 1 $aPINTO, M. dos S. T. 245 $aPurification and characterization of a peroxidase present in xilopodium exsudates of umbu plants (Spondias tuberosa A.).$h[electronic resource] 260 $c2015 520 $aUmbu 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. 650 $aCaatinga 650 $aPeroxidase 650 $aUmbu 653 $aGuaiacol peroxidase 653 $aRoot enzyme 653 $aSpondia tuberosa 653 $aTssue brownig 700 1 $aRIBEIRO, J. M. 700 1 $aARAUJO, F. P. de 700 1 $aMELO, N. F. de 700 1 $aFERNANDES, K. V. S. 773 $tAfrican Journal of Biotechnology$gv. 14, n. 21, p. 1838-1845, 2015.
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Embrapa Semiárido (CPATSA) |
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Registro Completo
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
Data corrente: |
17/03/2008 |
Data da última atualização: |
18/03/2008 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
LIMA, F. L.; CARVALHO, M. A. R.; SANTORO, M. M.; BEMQUERER, M. P.; OLIVEIRA, J. S.; APOLÔNIO, A. C. M.; ALVIANO, C. S.; FARIAS, L. M. |
Afiliação: |
F. L. Lima, UFRJ; M. A. R. Carvalho, ICB/UFMG; M. M. Santoro, ICB/UFMG; Marcelo Porto Bemquerer, Embrapa Recursos Genéticos e Biotecnologia; J. S. Oliveira, ICB/UFMG; A. C. M. Apolônio, ICB/UFMG; C. S. Alviano, UFRJ; L. M. Farias, ICB/UFMG. |
Título: |
Actinomycetemcomitin: a new bacteriocin produced by Aggregatibacter (Actinobacillus) Actinomycetemcomitans. |
Ano de publicação: |
2007 |
Fonte/Imprenta: |
In: ANNUAL MEETING OF THE SBBq, 36.; IUBMB CONFERENCE, 10., 2007, Salvador, BA. Infectious diseases: biochemistry of parasites, vectors and hosts: program and abstracts. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2007. |
Idioma: |
Inglês |
Palavras-Chave: |
Actinomyctemcomitin; Aggregatibacter actinomycetemcomitans; Bacteriocin. |
Categoria do assunto: |
-- |
Marc: |
LEADER 00885nam a2200217 a 4500 001 1188721 005 2008-03-18 008 2007 bl uuuu u01u1 u #d 100 1 $aLIMA, F. L. 245 $aActinomycetemcomitin$ba new bacteriocin produced by Aggregatibacter (Actinobacillus) Actinomycetemcomitans. 260 $aIn: ANNUAL MEETING OF THE SBBq, 36.; IUBMB CONFERENCE, 10., 2007, Salvador, BA. Infectious diseases: biochemistry of parasites, vectors and hosts: program and abstracts. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology$c2007 653 $aActinomyctemcomitin 653 $aAggregatibacter actinomycetemcomitans 653 $aBacteriocin 700 1 $aCARVALHO, M. A. R. 700 1 $aSANTORO, M. M. 700 1 $aBEMQUERER, M. P. 700 1 $aOLIVEIRA, J. S. 700 1 $aAPOLÔNIO, A. C. M. 700 1 $aALVIANO, C. S. 700 1 $aFARIAS, L. M.
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