Isolation, characterisation, and selection of wine yeast strains in Etyek-Buda wine district, Hungary

Initiated by the Association “Wine Route of Etyek Wine District”, the objectives of this study were to isolate and identify autochthonous yeast strains from local wines and to determine their oenologically important properties. The first aim of this work was to characterize the taxonomic and phenotypic diversity of the representative Saccharomyces yeast strains that dominate the spontaneous fermentations in this wine district. The results obtained by molecular ribotyping (ARDRA) revealed a strong dominance of S. cerevisiae, but S. bayanus var. uvarum was also present sporadically. Some of the natural isolates exhibited high volatile acid production or poor fermentation capacity, which imply a quality risk in spontaneous fermentations. Most of the isolates, however, displayed good oenological features during lab scale fermentations. As the second aim of this work, the most promising, selected strains were further tested for oenological properties in microvinification scale and, finally, in large scale fermentations. The analytical and sensory analysis proved that selected strains, including S. bayanus var. uvarum, can be used as local starter cultures, which may contribute to the typicality of the local wines in comparison with commercial starters

STC1 and PTHrP modify carbohydrate and lipid metabolism in liver of a teleost fish

Stanniocalcin 1 (STC1) and parathyroid hormone-related protein (PTHrP) are calciotropic hormones in vertebrates. Here, a recently hypothesized metabolic role for these hormones is tested on European sea bass treated with: (i) teleost PTHrP(1-34), (ii) PTHrP(1-34) and anti-STC1 serum (pro-PTHrP groups), (iii) a PTHrP antagonist PTHrP(7-34) or (iv) PTHrP(7-34) and STC1 (pro-STC1 groups). Livers were analysed using untargeted metabolic profiling based on proton nuclear magnetic resonance (1H-NMR) spectroscopy. Concentrations of branched-chain amino acid (BCAA), alanine, glutamine and glutamate increased in pro-STC1 groups suggesting their mobilization from the muscle to the liver for degradation and gluconeogenesis from alanine and glutamine. In addition, only STC1 treatment decreased the concentrations of succinate, fumarate and acetate, indicating slowing of the citric acid cycle. In the pro-PTHrP groups the concentrations of glucose, erythritol and lactate decreased, indicative of gluconeogenesis from lactate. Taurine, trimethylamine, trimethylamine N-oxide and carnitine changed in opposite directions in the pro-STC1 versus the pro-PTHrP groups, suggesting opposite effects, with STC1 stimulating lipogenesis and PTHrP activating lipolysis/β-oxidation of fatty acids. These findings suggest a role for STC1 and PTHrP related to strategic energy mechanisms that involve the production of glucose and safeguard of liver glycogen reserves for stressful situations.Portuguese Foundation for Science and Technology (FCT) SFRH/BD/103185/2014info:eu-repo/semantics/publishedVersio

Assembly scaffold NifEN: A structural and functional homolog of the nitrogenase catalytic component

NifEN is a biosynthetic scaffold for the cofactor of Mo-nitrogenase (designated the M-cluster). Previous studies have revealed the sequence and structural homology between NifEN and NifDK, the catalytic component of nitrogenase. However, direct proof for the functional homology between the two proteins has remained elusive. Here we show that, upon maturation of a cofactor precursor (designated the L-cluster) on NifEN, the cluster species extracted from NifEN is spectroscopically equivalent and functionally interchangeable with the native M-cluster extracted from NifDK. Both extracted clusters display nearly indistinguishable EPR features, X-ray absorption spectroscopy/extended X-ray absorption fine structure (XAS/EXAFS) spectra and reconstitution activities, firmly establishing the M-cluster-bound NifEN (designated NifENM) as the only protein other than NifDK to house the unique nitrogenase cofactor. Iron chelation experiments demonstrate a relocation of the cluster from the surface to its binding site within NifENM upon maturation, which parallels the insertion of M-cluster into an analogous binding site in NifDK, whereas metal analyses suggest an asymmetric conformation of NifENM with an M-cluster in one alpha beta-half and an empty cluster-binding site in the other alpha beta-half, which led to the proposal of a stepwise assembly mechanism of the M-cluster in the two alpha beta-dimers of NifEN. Perhaps most importantly, NifENM displays comparable ATP-independent substrate-reducing profiles to those of NifDK, which establishes the M-cluster-bound alpha beta-dimer of NifENM as a structural and functional mimic of one catalytic alpha beta-half of NifDK while suggesting the potential of this protein as a useful tool for further investigations of the mechanistic details of nitrogenase

Ergebnisse zur Abscheidung kleiner Troepfchen nach der Extraktion in Wiederaufarbeitungsanlagen fuer Kernbrennstoffe Schlussbericht

With 18 refs., 3 tabs., 33 figs.SIGLECopy held by FIZ Karlsruhe; available from UB/TIB Hannover / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekDEGerman

Morphological Changes in Saccharomyces cerevisiae during the Second Fermentation of Sparkling Wines

This study shows the morphological changes of Saccharomyces cerevisiae EC1118 during the second fermentation of Spanish cava wines, in relation with progression of fermentation and aging. In the first stages of active fermentation, and associated with the increase in viable counts, budding cells and a relative homogeneity in cell size were observed. Close to the moment of sugar exhaustion cells acquired the morphology of stationary phase, to finally enter in a death phase with cell size reduction, and cytoplasm alterations including inhomogeneity, refringency, and detachment of the cell wall. At the beginning of this step structures reminiscent to autophagosomes are observed. This is in accordance with the appearance of molecular markers of autophagy described elsewhere in similar winemaking conditions.This work was funded by the Spanish Ministerio de Ciencia y Tecnología (25506 FUN C FOOD CONSOLIDER-IMAGENIO 2010; AGL2006-02558 and AGL2004-06933-CO2-01/ALI), and the Comunidad Autónoma de Madrid (ALIBIRD-CM S-0505/AGR-0153).Peer reviewe

Assembly scaffold NifEN: A structural and functional homolog of the nitrogenase catalytic component

NifEN is a biosynthetic scaffold for the cofactor of Mo-nitrogenase (designated the M-cluster). Previous studies have revealed the sequence and structural homology between NifEN and NifDK, the catalytic component of nitrogenase. However, direct proof for the functional homology between the two proteins has remained elusive. Here we show that, upon maturation of a cofactor precursor (designated the L-cluster) on NifEN, the cluster species extracted from NifEN is spectroscopically equivalent and functionally interchangeable with the native M-cluster extracted from NifDK. Both extracted clusters display nearly indistinguishable EPR features, X-ray absorption spectroscopy/extended X-ray absorption fine structure (XAS/EXAFS) spectra and reconstitution activities, firmly establishing the M-cluster–bound NifEN (designated NifEN(M)) as the only protein other than NifDK to house the unique nitrogenase cofactor. Iron chelation experiments demonstrate a relocation of the cluster from the surface to its binding site within NifEN(M) upon maturation, which parallels the insertion of M-cluster into an analogous binding site in NifDK, whereas metal analyses suggest an asymmetric conformation of NifEN(M) with an M-cluster in one αβ-half and an empty cluster-binding site in the other αβ-half, which led to the proposal of a stepwise assembly mechanism of the M-cluster in the two αβ-dimers of NifEN. Perhaps most importantly, NifEN(M) displays comparable ATP-independent substrate-reducing profiles to those of NifDK, which establishes the M-cluster–bound αβ-dimer of NifEN(M) as a structural and functional mimic of one catalytic αβ-half of NifDK while suggesting the potential of this protein as a useful tool for further investigations of the mechanistic details of nitrogenase