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: 7Citation - Scopus: 8Thermoalkalophilic Recombinant Esterase Entrapment in Chitosan/Calcium Beads and Its Characterization(Wiley, 2021) Tercan, Cisem; Sürmeli, Yusuf; Şanlı Mohamed, GülşahBACKGROUND Esterases (EC 3.1.1.1), a class of hydrolases, degrade the ester bonds of lipids into alcohol and carboxylic acids and synthesize carboxylic ester bonds. They are used in a variety of biotechnological, industrial, environmental, and pharmaceutical applications due to their many valuable properties. Particularly, extremophilic esterases with many superior properties are of great interest for various reactions. Immobilization of enzymes may provide some advantages over free enzymes not only to improve the properties of enzymes but also to increase the reusability of biocatalyst in industrial applications. Therefore, many different immobilization applications for enzymes have been reported in various studies. To our knowledge, a thermophilic esterase has not so far been immobilized by entrapment using chitosan/calcium/alginate-blended beads. Here, we reported the immobilization of thermoalkalophilic recombinant esterase by entrapment using chitosan/calcium/alginate-blended beads, and then the entrapped esterase was characterized biochemically in details. RESULTS In the present study, a thermophilic recombinant esterase was immobilized by entrapment in chitosan/calcium/alginate-blended beads for the first time. The 0.5 mg mL(-1) purified recombinant esterase was entrapped in 1% chitosan, 2% alginate, and 0.7 M CaCl2 blended beads. The results showed that immobilization yield and entrapment efficiency of the entrapped esterase were 69.5% and 80.4%, respectively. SEM micrograph showed that the surface of the beads resembled a mesh and very compact structures. Chitosan/calcium/alginate-blended beads exhibited an 18.8% swelling ratio and had a moderate porous structure. The entrapment technique highly enhanced the thermostability of the esterase and shifted its optimum temperature from 65 to 80 degrees C. The immobilized esterase was very stable in a wide range of pH (8.5-11) displaying maximum activity at pH 9. ZnCl2 slightly increased the activity of immobilized esterase whereas several metal ions reduced the enzyme activity. When the enzyme was immobilized in chitosan/calcium/alginate-blended beads, its K-m increased about 2 times and V-max value decreased almost 1.5 times. Immobilization allowed repeated uses of the esterase having good operational stability in a continuous process. CONCLUSION The results revealed that the immobilization of a thermophilic recombinant esterase by entrapment in chitosan/calcium/alginate-blended beads exhibited considerably better compared to other immobilization processes with various entrapment strategies. (c) 2021 Society of Chemical Industry (SCI).