Enhancing the Catalytic Performance of β-Mannanase via Polyvinyl Alcohol Immobilization and Genipin Modification

Nazli Ece Varan Faki ¹, Ali Toprak ², Guzide Yucebilgic ¹

⁰Chemistry Department, Sciences & Letters Faculty, Cukurova University, Adana 01330, Turkey.

Molecules (basel, Switzerland) +

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December 11, 2025

View abstract on PubMed

Summary

Immobilizing genipin-modified beta-mannanase in polyvinyl alcohol hydrogels enhances enzyme stability and catalytic efficiency. This method efficiently produces mannooligosaccharides with potential antitumoral activity.

Area Of Science

Biotechnology
Enzyme Engineering
Biochemistry

Background

Mannooligosaccharides (MOSs) are valuable prebiotics.
Beta-mannanase is key for MOS production.
Enzyme immobilization can improve enzyme stability and reusability.

Purpose Of The Study

To immobilize beta-mannanase from Aspergillus niger within polyvinyl alcohol hydrogels.
To enhance enzyme stability, catalytic efficiency, and reusability.
To produce MOSs and evaluate their antitumoral potential.

Main Methods

Immobilization of unmodified and genipin-modified beta-mannanase in PVA hydrogels.
Characterization of enzyme properties (optimal pH, temperature, stability).
Evaluation of MOS production and antitumoral activity against cancer cell lines.

Main Results

Immobilized enzymes showed optimal pH 5.0 and optimal temperature 55 °C.
Genipin modification significantly increased enzyme half-life (429.2 h) and catalytic efficiency (2.3-fold).
Immobilized enzymes retained >75% activity after five reuse cycles.
MOS production yielded mannotetraose as the main product.
Generated MOSs exhibited moderate inhibition of MCF-7 and HCT-116 cancer cells.

Conclusions

Enzyme immobilization, especially with genipin modification, enhances beta-mannanase performance.
The developed system efficiently produces MOSs.
The produced MOSs show potential as antitumoral agents.

Keywords:

MOS anticancer effect enzyme stability genipin immobilization mannanase