Percorrer por autor "Todorovic, Smilja"
A mostrar 1 - 2 de 2
Resultados por página
Opções de ordenação
- Health benefits and risks of fermented foods : the PIMENTO initiativePublication . Todorovic, Smilja; Akpinar, Asli; Assunção, Ricardo; Bär, Cornelia; Bavaro, Simona L.; Kasikci, Muzeyyen Berkel; Domínguez-Soberanes, Julieta; Capozzi, Vittorio; Cotter, Paul D.; Doo, Eun-Hee; Ergün, Burcu Gündüz; Guzel, Mustafa; Harsa, Hayriye S.; Hastaoglu, Emre; Humblot, Christèle; Hyseni, Bahtir; Hosoglu, Muge I.; Issa, Aline; Karakaş-Budak, Barçın; Karakaya, Sibel; Kesenkas, Harun; Keyvan, Erhan; Künili, Ibrahim E.; Kütt, Mary-Liis; Laranjo, Marta; Louis, Sandrine; Mantzouridou, Fani T.; Matalas, Antonia; Mayo, Baltasar; Mojsova, Sandra; Mukherjee, Arghya; Nikolaou, Anastasios; Ortakci, Fatih; Paveljšek, Diana; Perrone, Giancarlo; Pertziger, Eugenia; Santa, Dushica; Sar, Taner; Savary-Auzeloux, Isabelle; Schwab, Clarissa; Starowicz, Małgorzata; Stojanović, Marko; Syrpas, Michail; Tamang, Jyoti P.; Yerlikaya, Oktay; Yilmaz, Birsen; Malagon-Rojas, Jeadran; Salminen, Seppo; Frias, Juana; Chassard, Christophe; Vergères, GuyWorldwide, fermented foods (FF) are recognized as healthy and safe. Despite the rapid increase of research papers, there is a lack of systematic evaluation of the health benefits and risks of FF. The COST Action CA20128 “Promoting innovation of fermented foods” (PIMENTO) aims to provide a comprehensive assessment on the available evidence by compiling a set of 16 reviews. Seven reviews will cover clinical and biological endpoints associated with major health indicators across several organ systems, including the cardiovascular, gastrointestinal, neurological, immune, and skeletal systems. Nine reviews will address broader biological questions associated with FF including bioactive compounds and vitamin production, nutrient bioavailability and bioaccessibility, the role of FF in healthy diets and personalized nutrition, food safety, regulatory practices, and finally, the health properties of novel and ethnic FF. For each outcome assessed in the reviews, an innovative approach will be adopted based on EFSA’s published guidance for health claim submissions. In particular, each review will be composed of three parts: (1) a systematic review of available human studies; (2) a non-systematic review of the mechanism of action related to the clinical endpoints measured by the human studies identified in part 1; and (3) a non-systematic review of the characterization of the FF investigated in the human studies identified in part 1. The evidence and research gaps derived from the reviews will be summarized and published in the form of a strategic road map that will pave the way for future research on FF.
- SERR spectroelectrochemical study of cytochrome cd1 nitrite reductase co-immobilized with physiological redox partner cytochrome c552 on biocompatible metal electrodesPublication . Silveira, Célia M.; Quintas, Pedro O.; Moura, Isabel; Moura, José J. G.; Hildebrandt, Peter; Almeida, M. Gabriela; Todorovic, Smilja"Cytochrome cd1 nitrite reductases (cd1NiRs) catalyze the one-electron reduction of nitrite to nitric oxide. Due to their catalytic reaction, cd1NiRs are regarded as promising components for biosensing, bioremediation and biotechnological applications. Motivated by earlier findings that catalytic activity of cd1NiR from Marinobacter hydrocarbonoclasticus (Mhcd1) depends on the presence of its physiological redox partner, cytochrome c552 (cyt c552), we show here a detailed surface enhanced resonance Raman characterization of Mhcd1 and cyt c552 attached to biocompatible electrodes in conditions which allow direct electron transfer between the conducting support and immobilized proteins. Mhcd1 and cyt c552 are co-immobilized on silver electrodes coated with self-assembled monolayers (SAMs) and the electrocatalytic activity of Ag // SAM // Mhcd1 // cyt c552 and Ag // SAM // cyt c552 // Mhcd1 constructs is tested in the presence of nitrite. Simultaneous evaluation of structural and thermodynamic properties of the immobilized proteins reveals that cyt c552 retains its native properties, while the redox potential of apparently intact Mhcd1 undergoes a ~150 mV negative shift upon adsorption. Neither of the immobilization strategies results in an active Mhcd1, reinforcing the idea that subtle and very specific interactions between Mhcd1 and cyt c552 govern efficient intermolecular electron transfer and catalytic activity of Mhcd1."