Starch-Based Lactoperoxidase Immobilization on Metal Oxide Nanofılm: A Novel Approach for the Synthesis, Characterization, and Antibacterial Potential
This study aims to develop a novel method for immobilizing lactoperoxidase (LPO) on starch-based metal oxide bionanofilms and evaluate its structural and antibacterial properties. LPO is an enzyme with broad-spectrum antimicrobial activity, and its stabilization is crucial for industrial applications. In this research, LPO was successfully immobilized onto starch and starch-based metal oxide films (starch@magnesium oxide (MgO), zinc oxide (ZnO), and copper oxide (CuO)) via surface adsorption and entrapment techniques. The immobilization was confirmed by Fourier transform infrared spectroscopy (FT-IR), x-ray diffraction (XRD), and field emission scanning electron microscopy (FE-SEM). The optimal pH for both free and immobilized LPO was determined to be 6. Although the free enzyme exhibited maximum activity at 40 degrees C, the immobilized enzyme demonstrated increased thermal stability, maintaining optimal activity at 60 degrees C. Furthermore, the initial activity of the immobilized LPO was 16.5%-19% after 60 min at 60 degrees C, whereas the free enzyme completely lost activity within 5 min. Storage stability tests revealed that immobilized LPO maintained 27.7%-39.6% of its initial activity for 21 days at 4 degrees C and 25 degrees C, whereas 95% of the free LPO was lost under the same conditions. The antibacterial properties of the prepared bionanofilms' were evaluated against gram-positive and gram-negative bacteria. The starch@ZnO/LPO film exhibited significant antibacterial activity among the tested films. These findings indicate that the immobilization of LPO onto starch-based metal oxide bionanofilms enhances its stability and antibacterial efficiency, making it a promising candidate for biomedical and industrial applications.
- Journal
- BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
- Year
- 2026
- Volume
- 73
- Issue
- 2
- Pages
- 435-454
- ISSN
- 0885-4513
- eISSN
- 1470-8744
- DOI
- 10.1002/bab.70032
- WoS UID
- WOS:001525578400001