Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - WoS: 5Citation - Scopus: 6A Novel Enzymatic Delamination Method for Sustainable Recycling of Crystal Silicon Photovoltaic (c-Si Pv) Modules(Elsevier, 2025) Karagoz, Sadik Can; Gundogdu, Tugba Keskin; Sarialtin, Huseyin; Celiktas, Melih SonerDue to the growing effects of global warming, there has been a surge in the demand for renewable energy sources. In particular, the most important player in this increase is the installation of photovoltaic (PV) modules. At this critical stage, it has become a priority to identify strategic approaches for the recycling of end-of-life PV panels with a strong focus on environmental protection. This study examined the impact of enzymatic delamination on the separation of the EVA (Ethylne Viniyl Aceate Co polymer) layer, a crucial stage in the recycling process of PV panels. Notably, this investigation is the first of its kind in the existing literature. To investigate this, delamination effects of lipase, laccase, and lecitase enzymes were analyzed according to experimental design methods. Furthermore, sunflower oil was employed for the first time in the existing body of literature to facilitate delamination, resulting in a delamination rate of 100 %. The environmental impacts of these biotechnological techniques, which serve as alternatives to the commonly used toluene, were also comparatively assessed by life cycle assessment (LCA) method to analyze the environmental impact. LCA methodology was performed from gate to gate and the Recipe impact methodology was used. Oil assisted enzymatic delamination method was shown to be an alternative from environmental point of view to solvent based method such as toluene.Article Citation - Scopus: 6Functional Characterization of a Novel Cyp119 Variant To Explore Its Biocatalytic Potential(John Wiley and Sons Inc, 2022) Sakalli, T.; Surmeli, N.B.Biocatalysts are increasingly applied in the pharmaceutical and chemical industry. Cytochrome P450 enzymes (P450s) are valuable biocatalysts due to their ability to hydroxylate unactivated carbon atoms using molecular oxygen. P450s catalyze reactions using nicotinamide adenine dinucleotide phosphate (NAD(P)H) cofactor and electron transfer proteins. Alternatively, P450s can utilize hydrogen peroxide (H2O2) as an oxidant, but this pathway is inefficient. P450s that show higher efficiency with peroxides are sought after in industrial applications. P450s from thermophilic organisms have more potential applications as they are stable toward high temperature, high and low pH, and organic solvents. CYP119 is an acidothermophilic P450 from Sulfolobus acidocaldarius. In our previous study, a novel T213R/T214I (double mutant [DM]) variant of CYP119 was obtained by screening a mutant library for higher peroxidation activity utilizing H2O2. Here, we characterized the substrate scope; stability toward peroxides; and temperature and organic solvent tolerance of DM CYP119 to identify its potential as an industrial biocatalyst. DM CYP119 displayed higher stability than wild-type (WT) CYP119 toward organic peroxides. It shows higher peroxidation activity for non-natural substrates and higher affinity for progesterone and other bioactive potential substrates compared to WT CYP119. DM CYP119 emerges as a new biocatalyst with a wide range of potential applications in the pharmaceutical and chemical industry. © 2021 International Union of Biochemistry and Molecular Biology, Inc.Book Part Citation - Scopus: 1Enzyme Technology in Value Addition of Wine and Beer Processing(Elsevier, 2022) Uzuner, SibelSome endogeneous and exogeneous enzymes participate in the brewery and winery technologies. Industrial enzymes provide quantitative advantages (increased juice yields) and qualitative advantages (enhanced extraction and flavor) for processing (shorter maceration, settling, and filtration time). This review aims to explain the flow process of brewing and wine-making, discuss different enzymes used in brewery and wine-making industry. Also, this chapter summarizes the key enzymes used at different stages of wine-making and brewing, and the challenges of the exogeneous, commercial and immobilized enzymes. Finally, the use of immobilized enzymes is presented as a significant strategy to improve catalyst during brewing and wine-making.Article Citation - WoS: 6Citation - Scopus: 6Functional Characterization of a Novel Cyp119 Variant To Explore Its Biocatalytic Potential(Wiley, 2021) Sakallı, Tuğçe; Sürmeli, Nur BaşakBiocatalysts are increasingly applied in the pharmaceutical and chemical industry. Cytochrome P450 enzymes (P450s) are valuable biocatalysts due to their ability to hydroxylate unactivated carbon atoms using molecular oxygen. P450s catalyze reactions using nicotinamide adenine dinucleotide phosphate (NAD(P)H) cofactor and electron transfer proteins. Alternatively, P450s can utilize hydrogen peroxide (H2O2) as an oxidant, but this pathway is inefficient. P450s that show higher efficiency with peroxides are sought after in industrial applications. P450s from thermophilic organisms have more potential applications as they are stable toward high temperature, high and low pH, and organic solvents. CYP119 is an acidothermophilic P450 from Sulfolobus acidocaldarius. In our previous study, a novel T213R/T214I (double mutant [DM]) variant of CYP119 was obtained by screening a mutant library for higher peroxidation activity utilizing H2O2. Here, we characterized the substrate scope; stability toward peroxides; and temperature and organic solvent tolerance of DM CYP119 to identify its potential as an industrial biocatalyst. DM CYP119 displayed higher stability than wild-type (WT) CYP119 toward organic peroxides. It shows higher peroxidation activity for non-natural substrates and higher affinity for progesterone and other bioactive potential substrates compared to WT CYP119. DM CYP119 emerges as a new biocatalyst with a wide range of potential applications in the pharmaceutical and chemical industry.