Catechol Removal from Aqueous Media Using Laccase Immobilized in Different Macro- and Microreactor Systems

• Published in: Applied biochemistry and biotechnology Vol. 182; no. 4; pp. 1575 - 1590
• Main Authors: Tusek, Ana Jurinjak, Salic, Anita, Zelic, Bruno
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.08.2017; Springer Nature B.V
• Subjects: Aqueous chemistry; Bacteria; Biocatalysis; Biocatalysts; Biochemistry; Bioreactors - microbiology; Biotechnology; Catechol; Catechols - isolation & purification; Catechols - metabolism; Chemistry; Chemistry and Materials Science; Covalence; Enzymes; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; Immobilization; Laccase; Laccase - chemistry; Laccase - metabolism; Microreactors; Oxidation; Oxidation process; Oxidation-Reduction; Phenols; Reactors; Trametes - enzymology; Water - chemistry; Water Pollutants, Chemical - isolation & purification; Water Pollutants, Chemical - metabolism; Immobilization; Oxidation of catechol; Microreactor; Laccase
• ISSN: 0273-2289; 1559-0291
• DOI: 10.1007/s12010-017-2419-2

Laccase belongs to the group of enzymes that are capable to catalyze the oxidation of phenols. Since the water is only by-product in laccase-catalyzed phenol oxidations, it is ideally “green” enzyme with many possible applications in different industrial processes. To make the oxidation process more sustainable in terms of biocatalyst consumption, immobilization of the enzyme is implemented in to the processes. Additionally, when developing a process, choice of a reactor type plays a significant role in the total outcome. In this study, the use of immobilized laccase from Trametes versicolor for biocatalytic catechol oxidation was explored. Two different methods of immobilization were performed and compared using five different reactor types. In order to compare different systems used for catechol oxidation, biocatalyst turnover number and turnover frequency were calculated. With low consumption of the enzyme and good efficiency, obtained results go in favor of microreactors with enzyme covalently immobilized on the microchannel surface.