Previous Issue
Volume 15, January
 
 

Catalysts, Volume 15, Issue 2 (February 2025) – 1 article

  • Issues are regarded as officially published after their release is announced to the table of contents alert mailing list.
  • You may sign up for e-mail alerts to receive table of contents of newly released issues.
  • PDF is the official format for papers published in both, html and pdf forms. To view the papers in pdf format, click on the "PDF Full-text" link, and use the free Adobe Reader to open them.
Order results
Result details
Section
Select all
Export citation of selected articles as:
24 pages, 5668 KiB  
Article
A New Multi-Active Heterogeneous Biocatalyst Prepared Through a Layer-by-Layer Co-Immobilization Strategy of Lipase and Laccase on Nanocellulose-Based Materials
by Kimberle Paiva dos Santos, Maíra Saldanha Duarte, Nathália Saraiva Rios, Ana Iraidy Santa Brígida and Luciana Rocha Barros Gonçalves
Catalysts 2025, 15(2), 99; https://doi.org/10.3390/catal15020099 (registering DOI) - 21 Jan 2025
Abstract
Lipase from Pseudomonas fluorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde [...] Read more.
Lipase from Pseudomonas fluorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde groups through periodate oxidation (NCox) or glutaraldehyde activation (NC-GA). FTIR analysis confirmed these chemical modifications. Among the functionalized NCs, NCox showed the best capacity to retain higher amounts of PFL (maximum load: 20 mg/g), and this support was selected to proceed with the co-immobilization experiments. In this process, NCox-250-PFL (NCox activated with 250 µmol/g of aldehyde groups) was covered with polyethyleneimine (PEI), laccase was co-immobilized, and a crosslinking step using glutaraldehyde was used to covalently attach the enzymes to the support, producing the biocatalyst NCox-250-PFL-PEI-Lac-GA. Co-immobilized enzymes presented higher thermal stability (50 °C) than soluble enzymes; co-immobilized laccase retained 61.1% of its activity after 24 h, and PFL retained about 90% after 48 h of deactivation at 50 °C. In operational stability assays, the heterogeneous biocatalysts maintained more than 45% of their activity after five cycles of pNPB hydrolysis and ABTS oxidation. This co-immobilized biocatalyst, with its high stability and activity retention, is a promising multi-active heterogeneous biocatalyst for use in cascade reactions of industrial interest. Full article
(This article belongs to the Special Issue Immobilized Biocatalysts, 3rd Edition)
Show Figures

Figure 1

Previous Issue
Back to TopTop