Photopolymerization of L-DOPA-Alginate Immobilized Cell Wall Laccase for Textile Dye Decolorization

Author:

Kokar Nikolina Popović1ORCID,Nikoletić Anamarija12ORCID,Stanišić Marija1ORCID,Crnoglavac Popović Milica1ORCID,Prodanović Radivoje1ORCID

Affiliation:

1. Faculty of Chemistry, University of Belgrade, Studentski trg 12–16, 11000 Belgrade, Serbia

2. Institute of Chemistry and Bioanalytics, School of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Hofackerstrasse 30, 4132 Muttenz, Switzerland

Abstract

Alginate is a naturally occurring polymer derived from brown algae biomass, which has numerous applications in various fields. Chemical modification of alginate is widely used to improve alginate’s physicochemical properties and provide new potential for multiple applications. In this article, we modified alginate with L-DOPA, using periodate oxidation and reductive amination, to obtain more suitable biopolymer for biocatalyst immobilization and hydrogel formation. Obtained modified alginate was used for the immobilization of laccase on cell walls. For this purpose, laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The obtained cell wall laccase was immobilized within L-DOPA-alginate beads by crosslinking the L-DOPA-alginate with calcium ions and laccase. The effect of additional crosslinking of beads by green light-induced photopolymerization with eosin Y was investigated. The immobilized laccase systems were used for dye decolorization and investigated in multiple treatment processes. Beads with L-DOPA-alginate with a higher degree of modification (5.0 mol%) showed higher enzymatic activity and better decolorization efficiency than those with a lower degree of modification (2.5 mol%). Obtained immobilized biocatalysts are suitable for decolorizing dye Evans Blue due to their high efficiency and reusability.

Funder

Ministry of Science, Technological Development, and Innovation of the Republic of Serbia

Publisher

MDPI AG

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