Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Enhanced Catalytic Performance of Rhizomucor Miehei Lipase on Di-N and Diethylhexyl Phthalates: Insights Into Substrate Specificity and Immobilization Strategy(Taylor & Francis Ltd, 2025) Balci, Esin; Rosales, Emilio; Curras, Marta Pazos; Sofuoglu, Aysun; Sanroman, M. A.Di-n-butyl (DnBP) and Diethylhexyl Phthalates (DEHP), known as potential endocrine disruptors, are priority pollutants categorized by many regulatory agencies. Enzymatic degradation is a green and efficient approach to remove PEs in the environment. In this study, the DnBP and DEHP degradation performance of Rhizomucor miehei lipase (palatase) in free and immobilized forms on Halloysite nanoclays (HNCs) in an aqueous system was investigated. Upon enzyme immobilization, the alterations in the palatase's secondary structure were examined using the circular dichroism (CD) analysis. The binding affinity of DnBP and DEHP to palatase was evaluated with molecular docking approaches. The enzyme's immobilization efficiency and relative activity were found to be 80.3% and 87.8%, respectively. CD results revealed that palatase retained its secondary structure to a significant extent. HNCs-palatase (HNCs-P) exhibited a high stability, as the structural integrity of palatase was mostly preserved. Both free palatase (FP) and HNCs-P fully degraded DnBP and DEHP (100 mg/L) to phthalic acid and a degradation pathway of DnBP and DEHP was suggested. Immobilization prevented the enzyme inhibition caused by the accumulation of metabolites. After seven consecutive uses, HNCs-P was still able to degrade DnBP (63.3%) and DEHP (72.8%). Molecular docking results showed that DEHP had a higher affinity for palatase than DnBP. This study suggests that enzyme immobilization onto HNCs can increase their stability and catalytic performance. FP and HNCs-P effectively hydrolyse ester bonds responsible for phthalate toxicity. Considering their high efficiency, FP and HNCs-P can be used as potential phthalate degraders in various environmental remediation processes.Article Citation - WoS: 15Citation - Scopus: 19Immobilization of Esterase From Bacillus Subtilis on Halloysite Nanotubes and Applications on Dibutyl Phthalate Degradation(Elsevier, 2023) Rosales, Emilio; Pazos, Marta; Sanroman, Maria Angeles; Balcı, Esin; Sofuoğlu, AysunDibutyl phthalate (DBP) is one of the listed phthalic acid esters (PAEs) known as the priority toxicants which exhibit carcinogenic and teratogenic properties and is responsible for endocrine disruption. Therefore, its removal has become a matter to tackle with. In this work, the feasibility of DBP degradation by esterase and lipase enzymes obtained from various microorganisms and the immobilization of the most effective in a clayey material were investigated. Esterase from Bacillus subtilis exhibited the highest degradation efficiency reaching a complete degradation. Its immobilization onto halloysite nanotubes (HNTs) by adsorption method was studied by response surface methodology using a central composite design face-centered. The four selected factors that affect the HNT-enzyme composite generation were: pH, adsorption time, enzyme/HNT (E/H) ratio, and adsorption temperature, and the optimal conditions were determined (pH 7, time 360 min, E/H ratio 0.2, temperature 30oC). Consequently, the activity did not significantly decrease by immobilization, and the adsorption efficiency and relative activity were determined to be 73.15% and 82.7%, respectively. Besides, the immobilization enhanced thermal and storage stability. As for enzyme reusability, after 7 continuous cycles, the composite maintained almost 75% of its initial activity. Both the free enzyme (1 mg/mL) and the composite degraded 100 mg/L DBP with 100% efficiency and several byproducts were detected. Moreover, the composite could be reused for 7 cycles keeping a remarkable catalytic activity. Overall, this study indicated that the HNT-enzyme composite may be used as an effective candidate for remediation of the environmental media contaminated with DBP and other PAEs.(c) 2023 The Author(s). Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).Article Citation - WoS: 4Citation - Scopus: 5Continuous Treatment of Diethyl Hexyl and Dibutyl Phthalates by Fixed-Bed Reactor: Comparison of Two Esterase Bionanocomposites(Elsevier, 2022) Sanroman, Maria Angeles; Balcı, Esin; Rosales, Emilio; Pazos, Marta; Sofuoğlu, AysunThe removal of Diethyl hexyl phthalate (DEHP) and Dibutyl phthalate (DBP) is of great importance due to their potential adverse effects on the environment and human health. In this study, two bionanocomposites prepared by immobilization of Bacillus subtilis esterase by crosslinking to halloysite and supported in chitosan and alginate beads were studied and proposed as a green approach. The esterase immobilization was confirmed by physical-chemical characterization. Bionanocomposite using chitosan showed the best degradation levels in batch tests attaining complete degradation of DBP and around 90% of DEHP. To determine the operational stability and efficiency of the system, two fixed bed reactors filled with both bionanocomposites were carried out operating in continuous mode. Chitosan based bionanocomposite showed the best performance being able to completely remove DBP and more than 85% of DEHP at the different flowrates. These results proved the potential of these synthesized bionanocomposites to effectively remove Phthalic Acid Esters.