@misc{13671,
  abstract     = {{The aging of biodiesel proceeds via multiple pathways, with oligomerization playing a central role. In this study, we investigated an epoxide-dependent oligomerization pathway, which had previously only been postulated. Using methyl oleate (C18:1) as a model monounsaturated fatty acid and acetic acid as a representative, reactive nucleophile and known biodiesel aging product with a suitable boiling point, oligomeric products were identified by size-exclusion chromatography (SEC) coupled with electrospray ionization quadrupole time-of-flight mass spectrometry (ESI-QTOF-MS). The concentration of 20 wt% was chosen to ensure a measurable kinetic effect while maintaining stable reaction conditions. Furthermore, the role of methyl oleate during biodiesel aging was addressed. Time-resolved analysis confirmed the proposed sequential order of reactions. It was pointed out that elimination reactions may occur. The data support the formation of epoxides, despite the isobaric overlap with ketones, and show that hydroxyl intermediates undergo esterification and etherification. Moreover, experiments with pure C18:1 demonstrated that acetic acid–derived oligomers are generated. Under Rancimat conditions, addition of 20 wt% acetic acid resulted in an approximately 1.1 – 2.6 increase in product yield. Kinetic analysis revealed structure-dependent formation and decay behavior of the aging products, with slightly faster epoxidation and shifted product distributions toward higher oligomeric species in the presence of acetic acid. Reactive intermediates were consumed more rapidly than oligomeric species and all decay processes followed apparent second-order kinetics. These findings provide direct experimental evidence for the involvement of epoxide-dependent pathways in biodiesel aging.}},
  author       = {{Türck, Julian and Funke, Carsten and Schmitt, Fabian and Schneider, Jan and Danneel, Hans-Jürgen and Türck, Ralf and Ruck, Wolfgang and Krahl, Jürgen}},
  booktitle    = {{Fuel : the science and technology of fuel and energy }},
  issn         = {{1873-7153}},
  keywords     = {{Biodiesel aging, Epoxide-dependent oligomerization, Acetic acid, Identification of aging products, Kinetics of aging products}},
  publisher    = {{Elsevier}},
  title        = {{{Kinetic study and confirmation of epoxide-dependent oligomerization of methyl oleate}}},
  doi          = {{10.1016/j.fuel.2026.139339}},
  volume       = {{424}},
  year         = {{2026}},
}

@misc{14057,
  abstract     = {{Bioactive peptides from plant proteins offer significant benefits. In this study, the structural and bioactive properties of sunflower protein isolate and its enzymatic hydrolysates were systematically investigated. The hydrolysates were fractionated using low-pressure preparative gradient chromatography (LP-PGC), and their antioxidant capacity, along with angiotensin-converting enzyme and dipeptidyl peptidase-IV inhibitory activities relevant to metabolic health, were assessed. Structural analyses via sodium dodecyl sulfate polyacrylamide gel electrophoresis and scanning electron microscopy revealed significant alterations in molecular weight distribution and surface morphology after hydrolysis and fractionation, confirming the generation of low-molecular-weight peptides linked to improved bioactivity. The results demonstrated a clear fraction-dependent bioactivity profile. MTT-based cell viability analysis of HepG2 and Caco-2 cells indicates that the non-toxicity of the hydrolysates depends on both their concentration and the cell type. Molecular docking studies were performed with the three highest-scoring peptides from each hydrolysate according to PeptideRanker. LP-PGC effectively reveals in vitro/in silico bioactivity of sunflower protein hydrolysates for multifunctional food use.}},
  author       = {{Güneş, Zeynep Saliha and Gülseren, İbrahim and Funke, Carsten and Danneel, Hans-Jürgen and Esatbeyoglu, Tuba}},
  booktitle    = {{Food Chemistry}},
  issn         = {{1873-7072}},
  keywords     = {{Sunflower protein hydrolysates, Fractionation, Bioactive peptides, ACE inhibition, DPP-IV inhibition, Mass spectrometry, In silico analysis}},
  publisher    = {{Elsevier BV}},
  title        = {{{Fractionation of sunflower protein hydrolysates by low pressure preparative gradient chromatography: An integrated in vitro and in silico assessment of bioactivities}}},
  doi          = {{10.1016/j.foodchem.2026.150976}},
  volume       = {{528}},
  year         = {{2026}},
}

@inproceedings{6842,
  author       = {{Pauli, Daniel and Neumaier, Michael and Scharf, Matthias and Funke, Carsten}},
  location     = {{Online}},
  title        = {{{Von der offline zur online Qualitätskontrolle mittels Echtzeit- und Fingerprint-Analytik}}},
  year         = {{2021}},
}