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

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 cor...

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Detalles Bibliográficos
Autores principales: dos Santos, Priscila M., Baruque, Julia R., de Souza Lira, Regiane K., Leite, Selma G. F., do Nascimento, Rodrigo P., Borges, Cristiano P., Wojcieszak, Robert, Itabaiana, Ivaldo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9409158/
https://www.ncbi.nlm.nih.gov/pubmed/36012620
http://dx.doi.org/10.3390/ijms23169363
Descripción
Sumario: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. (L(Asp)) 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.