Titre :

Corn Cob as a Green Support for Laccase Immobilization-Application on Decolorization of Remazol Brilliant Blue R

Auteur(s) :

Dos Santos, Priscila M. [Auteur]
Baruque, Julia R. [Auteur]
De Souza Lira, Regiane K. [Auteur]
Leite, Selma G. F. [Auteur]
Do Nascimento, Rodrigo P. [Auteur]
Borges, Cristiano P. [Auteur]
Wojcieszak, Robert [Auteur]
Unité de Catalyse et Chimie du Solide (UCCS) - UMR 8181
Itabaiana Junior, Ivaldo [Auteur]
Universidade Federal Rural do Rio de Janeiro [UFRRJ]
Unité de Catalyse et Chimie du Solide (UCCS) - UMR 8181

Titre de la revue :

International Journal of Molecular Sciences

Nom court de la revue :

Int J Mol Sci

Numéro :

23

Pagination :

9363

Éditeur :

MDPI

Date de publication :

2022-09-02

ISSN :

1422-0067

Mot(s)-clé(s) en anglais :

laccase
laccase immobilization
corn cob
lignocellulosic biomass
dye degradation

Discipline(s) HAL :

Chimie/Catalyse

Résumé en anglais : [en]

The high demand for food and energy imposed by the increased life expectancy of the population has driven agricultural activity, which is reflected in the larger quantities of agro-industrial waste generated, and requires ...
Lire la suite >The high demand for food and energy imposed by the increased life expectancy of the population has driven agricultural activity, which is reflected in the larger quantities of agro-industrial waste generated, and requires new forms of use. Brazil has the greatest biodiversity in the world, where corn is one of the main agricultural genres, and where over 40% of the waste generated is from cobs without an efficient destination. With the aim of the valorization of these residues, we proposed to study the immobilization of laccase from Aspergillus spp. (LAsp) in residual corn cob and its application in the degradation of Remazol Brilliant Blue R (RBBR) dye. The highest yields in immobilized protein (75%) and residual activity (40%) were obtained at pH 7.0 and an enzyme concentration of 0.1 g.mL−1, whose expressed enzyme activity was 1854 U.kg−1. At a temperature of 60 °C, more than 90% of the initial activity present in the immobilized biocatalyst was maintained. The immobilized enzyme showed higher efficiency in the degradation (64%) of RBBR dye in 48 h, with improvement in the process in 72 h (75%). The new biocatalyst showed operational efficiency during three cycles, and a higher degradation rate than the free enzyme, making it a competitive biocatalyst and amenable to industrial applications.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Projet ANR :

ULNE

Établissement(s) :

Université de Lille
CNRS
Centrale Lille
ENSCL
Univ. Artois

Collections :

• Unité de Catalyse et Chimie du Solide (UCCS) - UMR 8181

Équipe(s) de recherche :

Valorisation des alcanes et de la biomasse (VAALBIO)

Date de dépôt :

2023-05-30T15:12:55Z
2023-06-20T10:39:42Z