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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Functional characterization of a yellow laccase from Leucoagaricus gongylophorus

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Author(s):
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]
Total Authors: 7
Affiliation:
[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
Total Affiliations: 2
Document type: Journal article
Source: SPRINGERPLUS; v. 4, OCT 30 2015.
Web of Science Citations: 5
Abstract

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)

FAPESP's process: 11/21955-3 - Lignocellulolytic enzymes from fungi: functional and structural studies
Grantee:Dulce Helena Ferreira de Souza
Support type: Regular Research Grants