Amino-modified kraft lignin microspheres as a support for enzyme immobilization. Issue 36 (4th June 2020)
- Record Type:
- Journal Article
- Title:
- Amino-modified kraft lignin microspheres as a support for enzyme immobilization. Issue 36 (4th June 2020)
- Main Title:
- Amino-modified kraft lignin microspheres as a support for enzyme immobilization
- Authors:
- Bebić, Jelena
Banjanac, Katarina
Rusmirović, Jelena
Ćorović, Marija
Milivojević, Ana
Simović, Milica
Marinković, Aleksandar
Bezbradica, Dejan - Abstract:
- Abstract : The active biocatalyst systems were developed by immobilizing β-galactosidase from A. oryzae and laccase from M. thermophila expressed in A. oryzae (Novozym®51003) onto amino-modified microspheres based on bio-waste derived material, such as kraft lignin. Abstract : 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 highAbstract : The active biocatalyst systems were developed by immobilizing β-galactosidase from A. oryzae and laccase from M. thermophila expressed in A. oryzae (Novozym®51003) onto amino-modified microspheres based on bio-waste derived material, such as kraft lignin. Abstract : 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. … (more)
- Is Part Of:
- RSC advances. Volume 10:Issue 36(2020)
- Journal:
- RSC advances
- Issue:
- Volume 10:Issue 36(2020)
- Issue Display:
- Volume 10, Issue 36 (2020)
- Year:
- 2020
- Volume:
- 10
- Issue:
- 36
- Issue Sort Value:
- 2020-0010-0036-0000
- Page Start:
- 21495
- Page End:
- 21508
- Publication Date:
- 2020-06-04
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0ra03439h ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13852.xml