Akademik Veri Yönetim Sistemi
JOURNAL OF SURFACTANTS AND DETERGENTS, 2024 (SCI-Expanded)
This study aims to produce an active lipase detergent additive dry powder using spray drying. Staphylococcus aureus HA25, growing at a pH range of 5.0-8.5, was isolated from Erzurum gogermis cheese and purified using a three-phase partitioning technique. Optimal immobilization processing conditions were determined for 0.1% wt/wt chitosan, alginate, and chitosan/alginate concentrations of pure lipase enzyme. Morphological features of the immobilized enzyme structure were determined using scanning electron microscopy (SEM) analysis, and structural characterizations were determined using x-ray diffraction (XRD), Fourier transform infrared (FTIR) spectroscopy, and thermogravimetric (TG) analysis. The results showed that the natural structure of the lipase was largely restored upon reconstitution of the spray-dried immobilized lipase structures in water. While the free enzyme removed 52.6% of the oil added to the cotton fabric, the immobilized lipase@alginate enzyme removed similar to 98% of the oil added to the cotton fabric at the highest rate when used as a detergent additive. It was found that the reusability activity of chitosan@lipase, alginate@lipase, and chitosan/alginate@lipase enzymes remained at 86.4%, 92.8%, and 88.6% of their original activity, respectively. The study suggests that immobilized variations of the lipase enzyme within chitosan, alginate, and chitosan/alginate matrices may serve as a natural, secure, and efficient substitute for conventional chemical detergents, offering a non-toxic alternative for additive materials.