Saccharomyces cerevisiae mannoproteins that protect wine from protein haze: their release during fermentation and lees contact and a proposal for their mechanism of action.

A fraction containing the mannoproteins released during fermentation from the winemaking strain of Saccharomyces cerevisiae, Maurivin PDM, was able to reduce the visible protein haze in white wine. This fraction of haze protective mannoprotein material (HPM) could be recovered by either ultrafiltration or ethanol precipitation. The kinetics of the release of both mannose- and glucose-containing polymers during the growth cycle of PDM were determined as a guide to the release of HPM. Active HPM was first detected in the culture supernatant when the cells were exponentially growing. HPM was also released into the medium under an environment simulating winemaking conditions by PDM cells during fermentation as well as during storage on yeast lees. Since the amounts of HPM released during fermentation are greater than those subsequently extracted from the cell wall, fermentation would be a more viable procedure than extraction from yeast cells for the commercial production of HPM. Yeast invertase, a mannoprotein with haze protective activity, was used as a model substrate to investigate the mechanism of haze protection. Invertase was found to reduce visible turbidity but not prevent protein precipitation. Invertase itself did not precipitate but remained soluble in the wine. On the basis of these observations, we propose that the mechanism of haze protection may be one of competition between HPM and wine proteins for unknown wine component(s), the latter being required for the formation of large insoluble aggregates of denatured protein. As the available concentration of these components decreases, due to the presence of HPM, the particle size of the haze decreases and thus visible turbidity declines.