β-1,3-Glucanase from Delftia tsuruhatensis Strain MV01 and Its Potential Application in Vinification
Autor: | Melanie Larisika, Peter Pfeiffer, A. Eich, Helmut König, J. Eckelt, Christoph Nowak, V. Blättel |
---|---|
Rok vydání: | 2011 |
Předmět: |
beta-Glucans
Glycoside Hydrolases Wine Applied Microbiology and Biotechnology Cell Wall Food Preservation Yeasts Food Industry Pediococcus Delftia chemistry.chemical_classification Ecology biology food and beverages Glucanase biology.organism_classification Yeast Enzyme chemistry Biochemistry Delftia tsuruhatensis Food Microbiology Bacteria Food Science Biotechnology |
Zdroj: | Applied and Environmental Microbiology. 77:983-990 |
ISSN: | 1098-5336 0099-2240 |
DOI: | 10.1128/aem.01943-10 |
Popis: | During vinification microbial activities can spoil wine quality. As the wine-related lactic acid bacterium Pediococcus parvulus is able to produce slimes consisting of a β-1,3-glucan, must and wine filtration can be difficult or impossible. In addition, the metabolic activities of several wild-type yeasts can also negatively affect wine quality. Therefore, there is a need for measures to degrade the exopolysaccharide from Pediococcus parvulus and to inhibit the growth of certain yeasts. We examined an extracellular β-1,3-glucanase from Delftia tsuruhatensis strain MV01 with regard to its ability to hydrolyze both polymers, the β-1,3-glucan from Pediococcus and that from yeast cell walls. The 29-kDa glycolytic enzyme was purified to homogeneity. It exhibited an optimal activity at 50°C and pH 4.0. The sequencing of the N terminus revealed significant similarities to β-1,3-glucanases from different bacteria. In addition, the investigations indicated that this hydrolytic enzyme is still active under wine-relevant parameters such as elevated ethanol, sulfite, and phenol concentrations as well as at low pH values. Therefore, the characterized enzyme seems to be a useful tool to prevent slime production and undesirable yeast growth during vinification. |
Databáze: | OpenAIRE |
Externí odkaz: |