PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7645

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Access type: Metadata onlyPublisher: search.filters.publisher.Taylor & Francis Ltd

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  • Article
    Enhancement of Corchorus Olitorius L. on Osteogenic Differentiation of MC3T3-E1 Pre-Osteoblast Cells by Increasing Alkaline Phosphatase and Hydroxyproline
    (Taylor & Francis Ltd, 2025) Ertugruloglu, Pinar; Baris, Elif; Okkali, Gaye Sumer; Boke Sarikahya, Nazli; 01. Izmir Institute of Technology
    Corchorus olitorius L. (jute mallow or molehiya) belongs to the Malvaceae family valued for its nutritional and medicinal properties. In this study, the potential to enhance osteogenesis in MC3T3-E1(Murine Calvaria-derived 3T3 Subclone E1) pre-osteoblastic cells was investigated to support bone formation and mineralisation. Leaf ethanolic extract was prepared and applied to MC3T3-E1 cells. Osteogenic effects were evaluated through three methods: MTT assays for cell viability, Alizarin Red S staining for calcium deposition, enzymatic analyses for alkaline phosphatase (ALP) and hydroxyproline (HYP). A non-cytotoxic concentration of C. olitorius extract (0.5 mg/mL) significantly increased ALP and HYP levels, promoting osteogenic differentiation in both undifferentiated and differentiated cells. HYP levels were notably elevated in differentiated cells. The findings suggested that C. olitorius extract may be a promising natural agent for enhancing bone health, warranting further in vivo and clinical studies to confirm its therapeutic potential.
  • 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) Sofuoğlu, Aysun; Rosales, Emilio; Curras, Marta Pazos; Sofuoglu, Aysun; Sanroman, M. A.; 01. Izmir Institute of Technology; 03. Faculty of Engineering; 03.02. Department of Chemical Engineering
    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.