Monatshefte fur Chemie, cilt.156, sa.12, ss.1373-1389, 2025 (SCI-Expanded, Scopus)
Enzymes are biocatalysts that catalyze a wide variety of reactions. Enzyme immobilization is a technique in which an enzyme is immobilized and bound to a support while retaining its catalytic activity. In this study, Aspergillus niger pectinase enzyme was immobilized on chitosan–boric acid beads. The composite surface was characterized by scanning electron microscopy before and after immobilization. The bonds in the molecular structure were determined using Fourier Transform Infrared. In the study, parameters such as pH, temperature, kinetic calculations, reusability, immobilization time, enzyme concentration, storage, and theoretical calculations were studied. The temperature (37 °C) and pH (5) values did not change after immobilization. It was determined that immobilized pectinase retained 65% of its activity for 20 days. The immobilized enzyme still maintained nearly 100% activity after 6 uses. Gaussian calculations with the HF/6-31++g(d,p) basis set were used to investigate, first solely boric acid and chitosan and then the immobilization product by combining the two. Furthermore, Aspergillus niger proteins (PDB ID: 3K4P and 7BLY) were investigated in molecular docking calculations, and ADME/T calculations were generated to examine the effects and impact of these molecules in human metabolism.