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Registro Completo |
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Biblioteca(s): |
Embrapa Florestas. |
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Data corrente: |
30/08/2007 |
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Data da última atualização: |
13/02/2015 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
FARIA, R. O. de; MOURE, V. R.; BALTMANT, W.; AMAZONAS, M. A. L. de; KRIEGER, W.; MITCHELL, D. A. |
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Afiliação: |
Rodrigo Otávio de Faria, UFPR; Vivian Rotuno Moure, UFPR; Wellington Balmant, UFPR; Maria Angela Lopes de Almeida Amazonas, Embrapa Florestas; Nadia Krieger, UFPR; David Alexander Mitchell, UFPR. |
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Título: |
The tyrosinase produced by Lentinula boryana (Berk. & Mont.) pegler suffers substrate inhibition by L-DOPA. |
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Ano de publicação: |
2007 |
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Fonte/Imprenta: |
Food Technology and Biotechnology, v. 45, n. 3, p. 334-340, 2007. |
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Idioma: |
Inglês |
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Conteúdo: |
We undertook a preliminary characterization of the tyrosinase produced by a strain of Lentinula boryana from Brazil, with a view to evaluate its potential for biotechnological applications. The enzyme was similar to other fungal tyrosinases in many respects. When the crude extract was characterized, the tyrosinase activity was optimal at pH=6 and was not particularly thermostable, with half-lives of about 10 min and 1 min at 50 and 60 °C, respectively. We purified the enzyme with ammonium sulfate precipitation followed by ion exchange chromatography on a DEAE Sepharose column, obtaining a yield of 33 % and a 5.3-fold enrichment. The purified preparation gave three bands on SDS-PAGE, with molecular masses of 20, 27 and 47 kDa. This preparation showed substrate inhibition kinetics with L-DOPA (3,4-dihydroxy-L-phenylalanine), with a KM of 1.9 mM and a KI of 72 mM. Under the same reaction conditions, a commercial mushroom tyrosinase followed Michaelis- Menten kinetics, with a KM of 0.51 mM. Although the present study did not identify properties that would make the tyrosinase of L. boryana more suitable in biotechnological applications than tyrosinases from other mushrooms, it has made a contribution by showing that the enzyme suffers substrate inhibition by L-DOPA, something that has not previously been reported for mushroom tyrosinases. |
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Palavras-Chave: |
Inibição; Lentinula boryna; Substrato; Tirosinase. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02046naa a2200229 a 4500
001 1312078
005 2015-02-13
008 2007 bl uuuu u00u1 u #d
100 1 $aFARIA, R. O. de
245 $aThe tyrosinase produced by Lentinula boryana (Berk. & Mont.) pegler suffers substrate inhibition by L-DOPA.$h[electronic resource]
260 $c2007
520 $aWe undertook a preliminary characterization of the tyrosinase produced by a strain of Lentinula boryana from Brazil, with a view to evaluate its potential for biotechnological applications. The enzyme was similar to other fungal tyrosinases in many respects. When the crude extract was characterized, the tyrosinase activity was optimal at pH=6 and was not particularly thermostable, with half-lives of about 10 min and 1 min at 50 and 60 °C, respectively. We purified the enzyme with ammonium sulfate precipitation followed by ion exchange chromatography on a DEAE Sepharose column, obtaining a yield of 33 % and a 5.3-fold enrichment. The purified preparation gave three bands on SDS-PAGE, with molecular masses of 20, 27 and 47 kDa. This preparation showed substrate inhibition kinetics with L-DOPA (3,4-dihydroxy-L-phenylalanine), with a KM of 1.9 mM and a KI of 72 mM. Under the same reaction conditions, a commercial mushroom tyrosinase followed Michaelis- Menten kinetics, with a KM of 0.51 mM. Although the present study did not identify properties that would make the tyrosinase of L. boryana more suitable in biotechnological applications than tyrosinases from other mushrooms, it has made a contribution by showing that the enzyme suffers substrate inhibition by L-DOPA, something that has not previously been reported for mushroom tyrosinases.
653 $aInibição
653 $aLentinula boryna
653 $aSubstrato
653 $aTirosinase
700 1 $aMOURE, V. R.
700 1 $aBALTMANT, W.
700 1 $aAMAZONAS, M. A. L. de
700 1 $aKRIEGER, W.
700 1 $aMITCHELL, D. A.
773 $tFood Technology and Biotechnology$gv. 45, n. 3, p. 334-340, 2007.
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