Enhanced biocatalytic sustainability of laccase by immobilization on functionalized carbon nanotubes/polysulfone membranes

• Type: Article in International Scientific Journal
• Date: 2019

Authors

João B. Costa (Author) Other; Sampaio, M.J. (Author) FEUP; Maria J. Sampaio (Author) Other; Márcia C. Neves (Author) Other; Joaquim L. Faria (Author) FEUP; Sergio Morales-Torres (Author) Other; Ana P. M. Tavares (Author) Other; Cláudia G. Silva (Author) FEUP

Journal

Title: Chemical Engineering Journal

Vol. 355

Pages: 974-985

ISSN: 1385-8947

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 11 Citations

Scopus - 62 Citations

INSPEC

Associated Projects

IF/00514/2014/CP1249/CT0004 - Desafiando a síntese em química fina: uma nova abordagem utilizando fotocatalisadores isentos de metais

NanoPurAsp - Desenvolvimento de nanomateriais sustentáveis para a purificação de fármacos antileucémicos

Other information

Authenticus ID: P-00P-KV7

DOI: 10.1016/j.cej.2018.08.178

Abstract (EN): Chemically functionalized multi-walled carbon nanotubes (CNTs) are used as carriers for laccase immobilization. In this work, CNTs were modified using different approaches with a combination of methods involving hydrothermal oxidation with nitric acid, treatment with 3-aminopropyltriethoxysilane, glutaraldehyde, N-ethyl-N-(3-(dimethyl-amino)- propyl) carbodiimide hydrochloride and N-hydroxysuccinimide. The enzyme immobilization efficiency and recovered activity were evaluated towards 2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonic acid) biocatalytic oxidation. The best compromise between immobilization efficiency and recovered activity was obtained using the CNTs functionalized with 0.3M HNO3, treated with N-ethyl-N-(3-(dimethylamino) propyl) carbodiimide hydrochloride and N-hydroxysuccinimide. This catalyst also showed the best thermal stability (at 50 and 60 degrees C). The bioconjugate based on this material was characterized by vibrational spectroscopies (FTIR and Raman) and by N-2 adsorption. The results from reutilization tests showed that laccase activity was kept above 65% of its initial value after five consecutive cycles of reuse. The biocatalytic performance of the immobilized enzyme was evaluated for the degradation of a mixture of phenolic compounds in water containing phenol, resorcinol, 4-methoxyphenol and 4-chlorophenol. As means of cost efficient to enzyme reutilization, laccase was immobilized over polysulfone membranes blended with the functionalized CNTs and studied in the degradation of 4-methoxyphenol.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12