Anti-S. cerevisiae polyclonal antibody

Till now, very few studies are focused on the interactive effect of wine-associated microbes including non-Saccharomyces, Saccharomyces, and lactic acid bacteria on modulating the organoleptic quality of black raspberry wines. In our study, Torulaspora delbrueckii, a widely studied non-Saccharomyces yeast, and Lactobacillus plantarum, a promising malolactic fermentation starter, were used in combination with S. cerevisiae for the production of black raspberry wine by three inoculation modes, i.e., sequential inoculation of three species (SE), co-culture of S. cerevisiae and L. plantarum (CO) and T. delbrueckii/S. cerevisiae sequential inoculation plus a spontaneous malolactic fermentation (SP), on the quality of black raspberry wine. A total of 34 aromatic compounds were identified by HS-GC-IMS technology. CO was found to boost the production of many fruity ester compounds, and scored the highest for 'fruity', 'sweet', and 'total aroma' attributes during sensory evaluation. SP was characterized by the lowest production of most volatile components and obtained the lowest rating. Principal component analysis showed that three samples were quite different from each other. Overall, CO had greater potential to be used in the production of black raspberry wine.

Fungal alpha-mannosidase Ams1 and its mammalian homolog MAN2C1 hydrolyze terminal alpha-linked mannoses in free oligosaccharides released from misfolded glycoproteins or lipid-linked oligosaccharide donors. Ams1 is transported by selective autophagy into vacuoles. Here, we determine the tetrameric structure of Ams1 from the fission yeastSchizosaccharomyces pombeat 3.2 angstrom resolution by cryo-electron microscopy. Distinct from a low resolution structure ofS. cerevisiaeAms1,S. pombeAms1 has a prominent N-terminal tail that mediates tetramerization and an extra beta-sheet domain. Ams1 shares a conserved active site with other enzymes in glycoside hydrolase family 38, to which Ams1 belongs, but contains extra N-terminal domains involved in tetramerization. The atomic structure of Ams1 reported here will aid understanding of its enzymatic activity and transport mechanism.