Functional characterization of a yellow laccase from Leucoagaricus gongylophorus

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]

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

• 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
• Modalidade de apoio: Auxílio à Pesquisa - Regular