Factors affecting the ethanol productivity of yeast in molasses |
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| Institution: | 1. Food Biotechnology Group, Department of Chemistry, University of Patras, 26500 Patras, Greece;2. B.G. Spiliopoulos, 87-89 Akti Dimeon, 26333 Patras, Greece;3. I. Athanasopoulos and Co, 106b Lontou, 26224 Patras, Greece;1. College of Power and Energy Engineering, Harbin Engineering University, Harbin 150001, China;2. State Key Lab of Urban Water Resource and Environment, Harbin Institute of Technology, Harbin 150090, China;1. CBQF-Escola Superior de Biotecnologia, Universidade Católica Portuguesa, Rua Arquiteto Lobão Vital, 172, 4200-374, Porto, Portugal;2. Departamento de Farmacologia, NOVA Medical School, Faculdade de Ciências Médicas, Universidade Nova de Lisboa, Campo Mártires da Pátria 130, 1169-056, Lisboa, Portugal;3. Serviço de Doenças Infeciosas, Centro Hospitalar de Lisboa Central, Hospital de Curry Cabral, R. Beneficência 8, 1050-099, Lisboa, Portugal;1. University of Warmia and Mazury in Olsztyn, Faculty of Agriculture and Forestry, Department of Genetics, Plant Breeding and Bioresource Engineering, Plac ?ódzki 3, 10-719 Olsztyn, Poland;2. University of Warmia and Mazury in Olsztyn, Centre for Bioeconomy and Renewable Energies, Plac ?ódzki 3, 10-719 Olsztyn, Poland |
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| Abstract: | The ethanol production by a laboratory yeast strain, X2180-1B, was less than half that by an alcohol yeast, YOY655, in a molasses medium containing 30% sugars, although X2180-1B produced approximately the same amount of ethanol as YOY655 in a nutrition medium with the same sugar content. The weak productivity of X2180-1B in the molasses was ascribed to the limitation of sucrose hydrolysis in the molasses. The invertase activity of X2180-1B was 0.019 (mmol sucrose/min/mg protein) in the nutrition medium, but substantially zero in the molasses, while that of YOY655 was 1.75 in the nutrition medium and 1.15 even under the inhibitory conditions in molasses. External addition of invertase greatly enhanced the ethanol productivity of only X2180-1B. The inhibitory factors of invertase in molasses were heat-stable and dialyzable substances. |
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