Brazilian Journal of Chemical Engineering · 1997 · 15 citations · 13 references
Life SciencesBiochemistryMicrobiologyEnzymologyMicrobial MetabolismMicrobial PhysiologyAnaerobic MetabolismEnzyme KineticsEnzyme ProductionFermentation KineticsTemperature Effects On FermentationYeast BiologyEnvironmental Effects On Enzyme FunctionGlucose-6-phosphate Dehydrogenase RegulationInoculum EffectInvertase ActivityOxygen Concentration EffectsTemperature Dependence Of Enzyme ActivityTemperature Effects On Enzyme ActivityTemperature Effects On Fermentation Kinetics
The effect of pH (from 4.0 to 5.0), temperature (T) (from 30 oC to 40 oC) and dissolved oxygen concentration (DO) (from 0.2 to 6.0 mg O2/L) on glucose 6-phosphate dehydrogenase (G6PDH) (EC 1.1.1.49) and Invertase (EC 3.2.1.26) formation by S. cerevisiae were studied. The best culture conditions for G6PDH and Invertase formation were: 2.55 L culture medium (yeast extract, 3.0 g/L; 5peptone, 5.0 g/L; glucose, 2.0 g/L; sucrose, 15.0 g/L; Na2HPO4.12 H2O, 2.4 g/L; (NH4)2SO4, 5.1 g/L and MgSO4. 7H2O, 0.075 g/L); 0.45 L inoculum (0.70 g dry cell/L); pH = 4.5; T = 35 oC and DO = 4.0 mg/L. G6PDH was highly sensitive to pH, T and DO variation. The increase in G6PDH production was about three times when the DO ranged from 0.2 to 4.0 mg O2/L. Moreover, by shifting pH from 5.0 to 4.5 and temperature from 30 oC to 35 oC, G6PDH formation increased by 57% and 70%, respectively. Invertase activity (IA) of whole cells decreased at least 50% at extremes values of DO (2.0 and 6.0 mg O2/L) and pH (4.0 and 5.0). Furthermore, IA oscillated during the fermentation due to the glucose repression/derepression mechanism
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