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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Functional characterization of a yellow laccase from Leucoagaricus gongylophorus

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Autor(es):
Leme Ike, Priscila Tomie [1] ; Moreira, Ariele C. [1] ; de Almeida, Fernando G. [1] ; Ferreira, Douglas [1] ; Birolli, Willian Garcia [2] ; Meleiro Porto, Andre Luiz [2] ; Souza, Dulce Helena F. [1]
Número total de Autores: 7
Afiliação do(s) autor(es):
[1] Univ Fed Sao Carlos, Dept Quim, BR-13560 Sao Carlos, SP - Brazil
[2] Univ Sao Paulo, Inst Quim Sao Carlos, Sao Carlos, SP - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: SPRINGERPLUS; v. 4, OCT 30 2015.
Citações Web of Science: 5
Resumo

In this work we have identified, using mass spectrometry, two laccases produced by Leucoagaricus gongylophorus. One of them, Lac1Lg, was isolated, purified and characterized. Lac1Lg, a monomeric enzyme, was studied using ABTS and syringaldazine substrates. Lac1Lg presented kcat/Km almost threefold higher for syringaldazine than for ABTS, showing a higher catalytic efficiency of Lac1Lg for syringaldazine. The interference of several metal ions and substances in the laccase activity were evaluated. Lac1Lg did not absorb at 600 nm, which is a characteristic of so-called yellow laccases. Lac1Lg also was able to oxidize non-phenolic substrate (anthracene) in the absence of an exogenous mediator, showing that the enzyme has potential to explore in biotechnological processes. Our Lac1Lg three-dimensional molecular model, constructed using homology modeling, showed that the Lac1Lg catalytic site is very closed to blue laccases. (AU)

Processo FAPESP: 11/21955-3 - Enzimas lignocelulolíticas produzidas por fungos: estudos funcional e estrutural
Beneficiário:Dulce Helena Ferreira de Souza
Linha de fomento: Auxílio à Pesquisa - Regular