Invertase from Saccharomyces cerevisiae: Reversible inactivation by components of industrial molasses media
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In the upper range of growth temperatures ethanol, at physiological concentrations, affects the viability of cells of Saccharomyces cerevisiae and similar yeasts by enhancing thermal death. There is evidence, however, that yeast viability may also be affected by ethanol in such concentrations at much lower temperatures. Difficulties with yeast viability in the brewing of high-alcohol beers at low temperatures point in the same direction. Here the authors present results indicating that in addition to ethanol-enhanced thermal death, another form of ethanol-induced death occurs in S. cerevisiae that can be distinguished from the former by its temperature relations and its thermodynamic activation parameters.
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The effect of concanavalin A on biosynthesis of nucleic acids, proteins, structural polysaccharides and glycoproteins of the yeast cell membrane and of enzymes having different localization in the cell as well as on other processes occurring in spheroplasts of the yeasts Saccharomyces cerevisiae IBPhM-350 and CCY 21-4-13 were studied. In both yeast strains lectin strongly inhibited total protein synthesis and produced a weaker inhibiting effect on DNA and RNA synthesis. This was accompanied by a decrease of the activity of the majority of already known enzymes (acid phosphatase, invertase, alpha-glucosidase, polyphosphatase, pyrophosphatase, ATPase) and glucose consumption. In addition concanavalin A inhibited the synthesis of structural components of the yeast cell membrane, i.e. mannane and glucane. The data obtained suggest that lectin (50 microgram/ml or higher) has a toxic effect on yeast spheroplasts (or protoplasts).
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Tunicamycin apparently inhibited the biosynthesis of glucose, galactose, and maltose transport systems in Saccharomyces cerevisiae. Under the conditions used, the antibiotic also blocked the biosynthesis of invertase, a well-known yeast glycoprotein, as well as the glycosylation of a marker mannoprotein of the yeast cell wall. However, the antibiotic did not affect certain proteins which did not contain carbohydrate. It seems, therefore, that these sugar carriers are glycoproteins.
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The effects of temperature on the kinetics and efficiency of secretion of cloned invertase were investigated in a recombinant yeast system. This system consisted of the baker's yeast Saccharomyces cerevisiae (SEY2102) transformed with the 2mu-based plasmid pBR58 which contains the entire SUC2 gene including the promoter, signal sequence, and structural gene. The recombinant yeast produces the naturally secreted yeast enzyme invertase. In transition experiments done at temperatures ranging from 25 degrees to 45 degrees C, the maximum invertase level and secretion rate exhibited maxima of 5.5 U/mL . OD and 4.6 U/mL . OD per hour, respectively, at 35 degrees C. Experiments involving the use of cycloheximide showed that it took approximately 15 min for secreted invertase to move through the secretion pathway, which held 0.4 U/mL . OD of specific activity. (c) 1995 John Wiley & Sons, Inc.
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Abstract The ability of yeast to secrete intracellular and extracellular forms of invertase has been demonstrated by studies, however not much research has focused on intracellular invertase. Here we report the biochemical and chromatographic properties of intracellular invertase from invertase hyperproducer obtained from Abagboro village, Ile-Ife, Nigeria and compared it with that from a brewery which had been commercially selected. Saccharomyces cerevisiae and Saccharomyces carlsbergensis were isolated from fresh palm wine obtained from Abagboro village, Ile-Ife and from green beer obtained from a local brewery, respectively. Isolates were grown on liquefied cassava-soy bean mash for 72 hours. Yeast biomass harvested was homogenized to obtain crude intracellular invertase and purified by chromatographic techniques. Physicochemical properties and kinetic parameters ( K m and V max ) of the enzymes was studied. Native and subunit molecular weights of purified invertase from an hyperproducer ( Saccharomyces cerevisiae ) and brewer’s yeast ( Saccharomyces carlsbergensis ) were 118.3 kDa and 113.38 ± 4.9 kDa; 39.12 ± 1.2 kDa and 39.34 ± 1.71 kDa, respectively. Invertase was stable for 1 hour at 50 o C, with optimum temperature of 50 o C and 55 o C for Saccharomyces cerevisiae and Saccharomyces carlsbergensis , while their activation energies were 36.225 ± 4.015 kJmol − 1 and 33.06 ± 1.810 kJmol − 1 respectively. Invertase from Saccharomyces cerevisiae and Saccharomyces carlsbergensis had optimum activity at pH 5.0 and 4.0 respectively. Both enzymes utilized similar substrates with highest affinities for sucrose. The newly identified intracellular invertase from Abagboro yeast share similar physicochemical properties with that from commercial yeast ( Saccharomyces carlsbergensis ).
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