Diacetyl (2,3-butanedione) is an important flavour active, oxidative compound that has significant impact on cellular health as well as financial impact in industrial fermentations. The presence of diacetyl in certain fermented beverages, such as beer, results in an unpleasant butterscotch-like flavour and its concentration needs to be reduced by yeast to below the taste threshold prior to filtration and packaging. This results in significant process inefficiency. Furthermore, diacetyl negatively impacts cellular health and has been associated with neurodegenerative diseases and general cell aging amongst others. The reduction of this compound is therefore essential for cellular health. / Several yeast cell enzymatic mechanisms responsible for diacetyl reduction were identified and characterised, including Old Yellow Enzyme (OYE) isoforms and D-Arabinose Dehydrogenase (ARA1). OYE isoforms displayed different micromolar affinities and catalytic turnover rates for diacetyl and catalysed diacetyl reduction in a biphasic manner. ARA1 catalysed diacetyl reduction in a monophasic manner with a millimolar Michaelis constant. / Knowledge gained in these studies was applied in investigations of diacetyl production and reduction in industrial brewing operations and the enzymatic systems further exploited for the development of a novel enzyme based assay to determine diacetyl concentrations in beer samples. Concentrations as low as 0.2 muM were detectable with high repeatability.
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.103015 |
Date | January 2006 |
Creators | Van Bergen, Barry. |
Publisher | McGill University |
Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
Language | English |
Detected Language | English |
Type | Electronic Thesis or Dissertation |
Format | application/pdf |
Coverage | Doctor of Philosophy (Department of Bioresource Engineering.) |
Rights | © Barry Van Bergen, 2006 |
Relation | alephsysno: 002600238, proquestno: AAINR32250, Theses scanned by UMI/ProQuest. |
Page generated in 0.0017 seconds