Researchers have successfully developed innovative carriers from egg protein and carrageenan to improve the performance of cellulase enzymes, which play a pivotal role in juice clarification processes. This groundbreaking study, published on February 1, 2025, highlights the efficiency and stability of from improved glutaraldehyde-treated egg protein (GA-EP) and carrageenan (Carr) beads when used with the Aspergillus niger MK981235 cellulase.
The motivation behind this research stems from the increasing industrial demand for sustainable enzymatic processes, particularly within the juice industry. Traditional free enzymes often face stability issues under harsh operating conditions, limiting their practical application and effectiveness. By focusing on enzyme immobilization—a technique known to encapsulate enzymes making them more resilient—researchers aimed to craft high-performance carriers.
Through the Box Behnken design (BBD), the researchers optimized parameters including the glutaraldehyde concentration, egg protein concentration, and pH levels at which the cellulase was to be immobilized. The optimal settings were identified as 11.21% (w/v) glutaraldehyde, 8% (w/w) egg protein, and pH 3, which demonstrated the best conditions for maximum binding of the enzyme.
When tested, the GA-EP-Carr encapsulated cellulase revealed impressive thermal stability, performing effectively across extended temperature ranges. Notably, the im-cellulase retained 100% activity over 20 successive cycles and maintained activity for 60 days at 4 °C, demonstrating its repeated usability which is advantageous for industrial applications.
The scope of this research extends to real-world applications, particularly juice clarification. GA-EP-Carr im-cellulase was effective across various fruit juices—specifically mango, peach, grape, and orange—showing significant improvements not only in clarity but also measurable increases in total soluble solids and reducing sugars.
"We observed significant efficiency improvements during the clarification of mango, peach, grape, and orange juices," the authors noted, underscoring the potential for this technology to benefit the juice industry where visual clarity and quality of the product are of utmost importance.
This study not only presents innovative solutions to improve enzyme functionality but also sheds light on environmentally sustainable practices within food processing industries. The insights gained here promise to pave the way for future research aimed at enhancing the robustness of enzymatic applications across various fields.
Overall, the covalent binding of A. niger MK981235 cellulase onto GA-EP-Carr beads improved its thermal stability, with activation energy values altering significantly, offering industrial viability for the newly developed carriers. The introduction of these egg protein and carrageenan-based immobilizers is poised to advance juice processing technologies, setting the stage for more sustainable practices within the sector.