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Article 2025 · 3 atıf

Spray-dried immobilized lipase from <i>Staphylococcus aureus</i> HA25 for application in detergent industry

Nadaroglu, Hayrunnisa, Baran, Alper, Bayrakceken, Hatice

Özet

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.

Anahtar Kelimeler
addictive alginate chitosan detergent immobilization lipase PURIFICATION ENZYME STRAIN
WoS Kategorileri
Chemistry, Applied Chemistry, Physical Engineering, Chemical
Künye
Dergi
JOURNAL OF SURFACTANTS AND DETERGENTS
Yıl
2025
Cilt
28
Sayı
1
Sayfa
107-121
ISSN
1097-3958
eISSN
1558-9293
DOI
10.1002/jsde.12784
WoS UID
WOS:001258053000001
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