Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Mais filtros

Base de dados
Ano de publicação
Tipo de documento
País de afiliação
Intervalo de ano de publicação
1.
Chemosphere ; 312(Pt 1): 137218, 2023 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-36370757

RESUMO

Enzyme-based biocatalytic treatment has been known as an effective measure to biologically degrade organic pollutants. Advantageously, enzymes could be immobilized on solid supports, and such fact enables reuse/prolong the enzymatic capability. It could be of great importance to functionalize a support material for enhancing the immobilization efficiency/stability of enzymes. As such, this study laid great emphasis on covalent bonding to immobilize horseradish peroxidase (HRP) on a functionalized rice straw biochar with glutaraldehyde (GA) as a crosslinker. Biochar was pretreated by the electrochemical method and the acid treatment respectively to enrich the oxygen-containing functional groups. These led to the enhanced immobilizing ability of biochar. The HRP immobilized on the electrochemically-functionalized biochar (HRP-EBC) showed three times as much enzyme activity as the HRP directly adsorbed onto biochar. The HRP immobilized on the acid-functionalized biochar (HRP-ABC) showed activity similar to that of HRP-EBC. It was concluded that both the (acid/electrochemical) pretreatments are effective to enhance enzyme immobilization. Nevertheless, the electrochemical functionalized method of biochar is chemical oxidant-free, and one important lesson from a series of tests was that the pretreatment of biochar through the electrochemical method could be more environmentally benign. Moreover, employing HRP-EBC could be beneficial from a perspective of a real environmental practice considering its higher pH, thermal stability, and good reusability. 80% of phenol was degraded in 1 h in the presence of HRP-EBC when pH was 7.0 and a ratio of H2O2 to phenol was 1:1.5.


Assuntos
Peróxido de Hidrogênio , Fenol , Peroxidase do Rábano Silvestre/metabolismo , Estabilidade Enzimática , Temperatura , Enzimas Imobilizadas/metabolismo , Fenóis
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA