Improved L-Asparaginase Properties and Reusability by Immobilization onto Functionalized Carbon Xerogels

• Type: Article in International Scientific Journal
• Date: 2024

Authors

Barros, RAM (Author) Other; Raquel O. Cristóvão (Author) FEUP; Carneiro, IG (Author) Other; Barros, MA (Author) Other; Pereira, MM (Author) Other; Carabineiro, SAC (Author) Other; Freire, MG (Author) Other; Faria, JL (Author) Other; Santos Ebinuma, VC (Author) Other; Tavares, APM (Author) Other; Claudia G Silva (Author) FEUP

Journal

Title: ChemPlusChem

Vol. 89 No. e202400025

ISSN: 2192-6506

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 1 Citation

Scopus - 0 Citations

Associated Projects

LA LSRE-LCM - Financiamento Plurianual 2020-2023 para a Unidade LA LSRE-LCM Laboratório de Processos de Separação e Reacção - Laboratório de Catálise e Materiais

Other information

Authenticus ID: P-010-4ET

DOI: 10.1002/cplu.202400025

Abstract (EN): Enzyme immobilization can offer a range of significant advantages, including reusability, and increased selectivity, stability, and activity. In this work, a central composite design (CCD) of experiments and response surface methodology (RSM) were used to study, for the first time, the L-asparaginase (ASNase) immobilization onto functionalized carbon xerogels (CXs). The best results were achieved using CXs obtained by hydrothermal oxidation with nitric acid and subsequent heat treatment in a nitrogen flow at 600 degrees C (CX-OX-600). Under the optimal conditions (81 min of contact time, pH 6.2 and 0.36 g/L of ASNase), an immobilization yield (IY) of 100 % and relative recovered activity (RRA) of 103 % were achieved. The kinetic parameters obtained also indicate a 1.25-fold increase in the affinity of ASNase towards the substrate after immobilization. Moreover, the immobilized enzyme retained 97 % of its initial activity after 6 consecutive reaction cycles. All these outcomes confirm the promising properties of functionalized CXs as support for ASNase, bringing new insights into the development of an efficient and stable immobilization platform for use in the pharmaceutical industry, food industry, and biosensors. The development of an efficient strategy for immobilizing L-asparaginase enzyme onto functionalized carbon xerogels is the focus of this work. The results reveal the importance of tuning the surface chemistry of the materials and prove the enhanced activity, higher affinity with the substrate, and reusability of L-asparaginase achieved through immobilization.+ image

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 13