Hanseniaspora species are the main yeasts isolated from grapes and grape musts. Regarding genetic and phenotypical characterization, especially fermentative behavior, they can be classified in two technological clusters: the fruit group and the fermentation group. Among the species belonging to the last group, Hanseniaspora osmophila and Hanseniaspora vineae have been previously isolated in spontaneous fermentations of grape must. In this work, the oenological aptitudes of the two species of the fermentation group were compared with Saccharomyces cerevisiae and the main species of the fruit group, Hanseniaspora uvarum. Both H. osmophila and H. vineae conferred a positive aroma to final wines and no sensory defects were detected. Wines fermented with H. vineae presented significantly higher concentrations of 2-phenylethyl, tryptophol and tyrosol acetates, acetoin, mevalonolactone, and benzyl alcohol compared to H. osmophila. Sensorial analysis showed increased intensity of fruity and flowery notes in wines vinificated with H. vineae. In an evolutionary context, the detoxification of alcohols through a highly acetylation capacity might explain an adaption to fermentative environments. It was concluded that, although H. vineae show close alcohol fermentation adaptations to H. osmophila, the increased activation of phenylpropanoid metabolic pathway is a particular characteristic of H. vineae within this important apiculate genus.
1 January 2019 in International Journal of Food Microbiology
Melatonin is a bioactive compound that is present in fermented beverages and synthesized by yeast during alcoholic fermentation. Many studies have shown that melatonin interacts with some mammalian proteins, such as sirtuins or orphan receptor family proteins. The aim of this study was to determine the intracellular synthesis profile of melatonin in Saccharomyces cerevisiae and to identify the proteins that may interact with this molecule in yeast cells. Melatonin from fermentation samples was analyzed by liquid chromatography mass spectrometry, and proteins bound to melatonin were immunopurified by melatonin-IgG-Dynabeads. Melatonin was produced intracellularly in the lag phase of yeast growth and was exported to the extracellular media during the stationary phase. During this period, melatonin was bound to six proteins with molecular weights from 55 to 35 kDa. Sequence analysis showed that most proteins shared high levels of homology with glycolytic enzymes. An RNA-binding protein was also identified, the elongation alpha factor, which is related to mitochondria. This study reports for the first time the interaction of melatonin and proteins inside yeast cells. These results highlight the possible role of melatonin as a signal molecule and provide a new perspective for understanding its role in yeast.
The present article reports the draft genome sequence of the strain Komagataeibacter europaeus CECT 8546, an acetic acid bacterium characterized by its ability to overproduce cellulose. This species is highly resistant to acetic acid and commonly found during vinegar elaboration.