Literature DB >> 15993161

Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds.

M Lorenzo1, D Moldes, S Rodríguez Couto, Maria A Sanromán.   

Abstract

Due to the numerous biotechnological applications of laccase enzyme, it is essential to know the influence of different agents usually present in the natural environment on its enzymatic action, especially for in situ treatment technologies. In the present work, a simple and rapid method to determine the inhibitory or inducer effect of different compounds on laccase activity was developed. The compounds tested were copper-chelating agents and heavy metals. It was found that using syringaldazine as a substrate, all copper-chelating agents (except EDTA) highly inhibited laccase activity (around 100%) at an inhibitor concentration lower than 20 mM. Moreover, 40% of inhibition, which was detected at a concentration of 20 mM for both Cd(2+) and Cu(2+) increased with concentration until nearly complete inhibition at 80 mM.

Entities:  

Mesh:

Substances:

Year:  2005        PMID: 15993161     DOI: 10.1016/j.chemosphere.2004.12.051

Source DB:  PubMed          Journal:  Chemosphere        ISSN: 0045-6535            Impact factor:   7.086


  11 in total

1.  Ptilomycalin A inhibits laccase and melanization in Cryptococcus neoformans.

Authors:  Doralyn S Dalisay; Jonel P Saludes; Tadeusz F Molinski
Journal:  Bioorg Med Chem       Date:  2011-05-27       Impact factor: 3.641

2.  A first report on competitive inhibition of laccase enzyme by lignin degradation intermediates.

Authors:  Sirisha Pamidipati; Asma Ahmed
Journal:  Folia Microbiol (Praha)       Date:  2019-12-20       Impact factor: 2.099

3.  Degradation of the disease-associated prion protein by a serine protease from lichens.

Authors:  Christopher J Johnson; James P Bennett; Steven M Biro; Juan Camilo Duque-Velasquez; Cynthia M Rodriguez; Richard A Bessen; Tonie E Rocke
Journal:  PLoS One       Date:  2011-05-11       Impact factor: 3.240

4.  Reduced toxicity of malachite green decolorized by laccase produced from Ganoderma sp. rckk-02 under solid-state fermentation.

Authors:  Abha Sharma; Bhuvnesh Shrivastava; Ramesh Chander Kuhad
Journal:  3 Biotech       Date:  2014-11-11       Impact factor: 2.406

5.  A novel homodimer laccase from Cerrena unicolor BBP6: Purification, characterization, and potential in dye decolorization and denim bleaching.

Authors:  Ji Zhang; Lei Sun; Hao Zhang; Shufang Wang; Xiaoyu Zhang; Anli Geng
Journal:  PLoS One       Date:  2018-08-23       Impact factor: 3.240

6.  A structural-chemical explanation of fungal laccase activity.

Authors:  Rukmankesh Mehra; Jan Muschiol; Anne S Meyer; Kasper P Kepp
Journal:  Sci Rep       Date:  2018-11-23       Impact factor: 4.379

7.  Poly(2-oxazoline)s with a 2,2'-Iminodiacetate End Group Inhibit and Stabilize Laccase.

Authors:  Montasser Hijazi; Esra Türkmen; Joerg C Tiller
Journal:  Chembiochem       Date:  2019-12-13       Impact factor: 3.164

8.  Discovery of two novel laccase-like multicopper oxidases from Pleurotus citrinopileatus and their application in phenolic oligomer synthesis.

Authors:  A Zerva; C Pentari; A Termentzi; A H P America; D Zouraris; S K Bhattacharya; A Karantonis; G I Zervakis; E Topakas
Journal:  Biotechnol Biofuels       Date:  2021-04-01       Impact factor: 6.040

9.  Functional characterization of a yellow laccase from Leucoagaricus gongylophorus.

Authors:  Priscila Tomie Leme Ike; Ariele C Moreira; Fernando G de Almeida; Douglas Ferreira; Willian Garcia Birolli; Andre Luiz Meleiro Porto; Dulce Helena F Souza
Journal:  Springerplus       Date:  2015-10-30

10.  Optimization of Laccase from Ganoderma lucidum Decolorizing Remazol Brilliant Blue R and Glac1 as Main Laccase-Contributing Gene.

Authors:  Peng Qin; Yuetong Wu; Bilal Adil; Jie Wang; Yunfu Gu; Xiumei Yu; Ke Zhao; Xiaoping Zhang; Menggen Ma; Qiang Chen; Xiaoqiong Chen; Zongjin Zhang; Quanju Xiang
Journal:  Molecules       Date:  2019-10-30       Impact factor: 4.411

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.