Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - Scopus: 1Esterase-Mediated Degradation of Dibutyl and Diethylhexyl Phthalates in Aqueous and Soil Systems(Elsevier Ltd, 2025) Balci, E.; Sanli-Mohamed, G.; Sofuoglu, A.Phthalate esters (PAEs), widely used as plasticizers, pose severe environmental and health risks. This study investigated the enzymatic hydrolysis of PAE congeners (dibutyl phthalate (DBP) and diethylhexyl phthalate (DEHP)) in aqueous and soil systems using Bacillus subtilis esterase and a new thermoalkaliphilic Geobacillus sp. esterase. A novel esterase secreted from Geobacillus sp. which was isolated from a geothermal region (Türkiye) was expressed in E.coli and purified. Geobacillus sp. esterase was able to degrade almost 30% of DBP and 40% of DEHP (100 mg/L) in the aqueous system within 336 h, while it degraded virtually 59% and 98% of DBP in agricultural area soil (soil-1) and forest area soil (soil-2), respectively, at the same time. To compare with Geobacillus sp. esterase, Bacillus subtilis esterase was used, which fully degraded DBP with 100 mg/L in the soil-1 and soil-2 for 72 h and 2 h, respectively. The performances of both esterases to degrade DEHP (100 mg/L) were similar in soil-1 (∼35%) and soil-2 (∼50%) for 336 h. Soil characteristics significantly influenced PAE degradation. Compared to that in the aqueous system, Geobacillus sp. esterase in soil systems had a higher degradation efficiency. This was likely due to its origin from a soil microorganism. Variations in the degradation ability of two enzymes most probably arose from substrate specificities and enzyme dynamics. Molecular docking results showed that DBP had a higher affinity to both enzymes than DEHP. Overall, this study offers important evidence that Bacillus subtilis esterase and Geobacillus sp. esterase are effective biocatalysts for removing the pollutants with ester bonds in the environment. © 2025 Elsevier LtdArticle 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: 49Citation - Scopus: 55Immobilization of Thermoalkalophilic Recombinant Esterase Enzyme by Entrapment in Silicate Coated Ca-Alginate Beads and Its Hydrolytic Properties(Elsevier Ltd., 2012) Gülay, Seçkin; Şanlı Mohamed, GülşahThermoalkalophilic esterase enzyme from Balçova (Agamemnon) geothermal site were aimed to be immobilized effectively via a simple and cost-effective protocol in silicate coated Calcium alginate (Ca-alginate) beads by entrapment. The optimal immobilization conditions of enzyme in Ca-alginate beads were investigated and obtained with 2% alginate using 0.5mg/ml enzyme and 0.7M CaCl 2 solution. In order to prevent enzyme from leaking out of the gel beads, Ca-alginate beads were then coated with silicate. Enzyme loading efficiency and immobilization yield for silicate coated beads was determined as 98.1% and 71.27%, respectively and compared with non-coated ones which were 68.5% and 45.80%, respectively. Surface morphologies, structure and elemental analysis of both silicate coated and non-coated alginate beads were also compared using Fourier Transform Infrared Spectroscopy (FT-IR) and Scanning Electron Microscope (SEM) equipped with Energy-dispersive X-ray spectroscopy (EDX). Moreover, silicate coated alginate beads enhanced reusability of esterase in continuous processes compared to non-coated beads. The hydrolytic properties of free and immobilized enzyme in terms of storage and thermal stability as well as the effects of the temperature and pH were determined. It was observed that operational, thermal and storage stabilities of the esterase were increased with immobilization.