Functional characterization of a yellow laccase fr... - BV FAPESP
Advanced search
Start date
Betweenand
Related content
(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

Full text
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 Opportunities: Regular Research Grants