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Amino-modified kraft lignin microspheres as a support for enzyme immobilization

In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing β-galactosidase from A. o...

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Autores principales: Bebić, Jelena, Banjanac, Katarina, Rusmirović, Jelena, Ćorović, Marija, Milivojević, Ana, Simović, Milica, Marinković, Aleksandar, Bezbradica, Dejan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9054402/
https://www.ncbi.nlm.nih.gov/pubmed/35518748
http://dx.doi.org/10.1039/d0ra03439h
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author Bebić, Jelena
Banjanac, Katarina
Rusmirović, Jelena
Ćorović, Marija
Milivojević, Ana
Simović, Milica
Marinković, Aleksandar
Bezbradica, Dejan
author_facet Bebić, Jelena
Banjanac, Katarina
Rusmirović, Jelena
Ćorović, Marija
Milivojević, Ana
Simović, Milica
Marinković, Aleksandar
Bezbradica, Dejan
author_sort Bebić, Jelena
collection PubMed
description In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing β-galactosidase from A. oryzae and laccase from M. thermophila expressed in A. oryzae (Novozym® 51003) onto A-LMS. Two types of A-LMS were investigated, with different emulsifier concentrations (5 wt% and 10 wt%), and microspheres produced using 5 wt% of emulsifier (A-LMS_5) showed adequate pore shape, size and distribution for enzyme attachment. The type of interactions formed between enzymes (β-galactosidase and laccase) and A-LMS_5 microspheres demonstrated that β-galactosidase is predominantly attached via electrostatic interactions while attachment of laccase is equally governed by electrostatic and hydrophobic interactions. Furthermore, the A-LMS_5-β-galactosidase exhibited specificity towards recognized prebiotics (galacto-oligosaccharides (GOS)) synthesis with 1.5-times higher GOS production than glucose production, while for environmental pollutant lindane degradation, the immobilized laccase preparation exhibited high activity with a minimum remaining lindane concentration of 22.4% after 6 days. Thus, this novel enzyme immobilization support A-LMS_5 has potential for use in green biotechnologies.
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spelling pubmed-90544022022-05-04 Amino-modified kraft lignin microspheres as a support for enzyme immobilization Bebić, Jelena Banjanac, Katarina Rusmirović, Jelena Ćorović, Marija Milivojević, Ana Simović, Milica Marinković, Aleksandar Bezbradica, Dejan RSC Adv Chemistry In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing β-galactosidase from A. oryzae and laccase from M. thermophila expressed in A. oryzae (Novozym® 51003) onto A-LMS. Two types of A-LMS were investigated, with different emulsifier concentrations (5 wt% and 10 wt%), and microspheres produced using 5 wt% of emulsifier (A-LMS_5) showed adequate pore shape, size and distribution for enzyme attachment. The type of interactions formed between enzymes (β-galactosidase and laccase) and A-LMS_5 microspheres demonstrated that β-galactosidase is predominantly attached via electrostatic interactions while attachment of laccase is equally governed by electrostatic and hydrophobic interactions. Furthermore, the A-LMS_5-β-galactosidase exhibited specificity towards recognized prebiotics (galacto-oligosaccharides (GOS)) synthesis with 1.5-times higher GOS production than glucose production, while for environmental pollutant lindane degradation, the immobilized laccase preparation exhibited high activity with a minimum remaining lindane concentration of 22.4% after 6 days. Thus, this novel enzyme immobilization support A-LMS_5 has potential for use in green biotechnologies. The Royal Society of Chemistry 2020-06-04 /pmc/articles/PMC9054402/ /pubmed/35518748 http://dx.doi.org/10.1039/d0ra03439h Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Bebić, Jelena
Banjanac, Katarina
Rusmirović, Jelena
Ćorović, Marija
Milivojević, Ana
Simović, Milica
Marinković, Aleksandar
Bezbradica, Dejan
Amino-modified kraft lignin microspheres as a support for enzyme immobilization
title Amino-modified kraft lignin microspheres as a support for enzyme immobilization
title_full Amino-modified kraft lignin microspheres as a support for enzyme immobilization
title_fullStr Amino-modified kraft lignin microspheres as a support for enzyme immobilization
title_full_unstemmed Amino-modified kraft lignin microspheres as a support for enzyme immobilization
title_short Amino-modified kraft lignin microspheres as a support for enzyme immobilization
title_sort amino-modified kraft lignin microspheres as a support for enzyme immobilization
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9054402/
https://www.ncbi.nlm.nih.gov/pubmed/35518748
http://dx.doi.org/10.1039/d0ra03439h
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