AI Article Synopsis
- The study developed two types of magnetic biocatalysts using pectinase and cellulase: carrier-free magnetic CLEAs (CLEA-MP*) and magnetite-immobilized enzymes (Enz-Glu-MP*).
- Enz-Glu-MP* showed better magnetic properties, while CLEA-MP* had a larger surface area and pore volume, which affected their enzyme activity and stability.
- CLEA-MP* was found to be the most active and stable biocatalyst, retaining 33.4% cellulase activity after several cycles, suggesting magnetic enzyme immobilization could improve biocatalyst reuse in juice processing.
Article Abstract
In the present study, we prepared two different magnetic biocatalysts of pectinase and cellulase: carrier-free magnetic CLEAs (CLEA-MP*) and immobilization on glutaraldehyde-activated magnetite (Enz-Glu-MP*). The biocatalysts were compared to their magnetic properties, immobilization parameters, stability and grape juice clarification. Enz-Glu-MP* presented higher magnetic properties than CLEA-MP*, whereas this presented higher surface area and pore volume. The K of the enzyme immobilized on Enz-Glu-MP* was 25.65mM, lower in comparison to the CLEA-MP* (33.83mM). On the other hand, CLEA-MP* was the most active and stable biocatalyst, presenting higher recovered activity (33.4% of cellulase), higher thermal stability (2.39 stabilization factor) and improved reusability (8cycles). The integration of magnetic technology with enzymatic immobilization emerges as a possibility to increase the recover and reuse of biocatalysts for application in juice technology.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.ijbiomac.2018.04.028 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!