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作 者:Panagiotis Dritsas George Aggelis
出 处:《Carbon Resources Conversion》2023年第4期326-333,共8页碳资源转化(英文)
基 金:financed by the Green Fund of the Hellenic Ministry of Environment and Energy,under the funding program“National Environment and Innovation Activities 2022”,Priority Axis“Research&Application”,Project“Sustainable technology for converting pomegranate residues into bioproducts and bioactive compounds”with the acronym“POMEGRANATE”.
摘 要:Over the past few years,it is observed an increased interest for oleaginous microorganisms in the perspective to produce microbial oils of great commercial interest through the consumption of low/zero cost substrates.In this paper,the physiology of the fungus Umbelopsis isabellina growing on blends of glycerol and glucose was investigated.In all experiments the fungus completely consumed glucose and produced satisfactory quantities of biomass containing reserve lipids in high percentages.However,glycerol concentration in the growth medium was negatively correlated to glucose assimilation rate,mainly during the balanced-growth phase.Nevertheless,at high initial concentrations,glycerol was partially consumed and seemed to contribute positively to the suppression of lipid degradation.Following the discovery of this complex regulatory mechanism regarding glucose and glycerol co-assimilation,the activity of three key-enzymes namely aldolase,glycerol kinase and glycerol dehydrogenase,which are implicated in glycerol and glucose assimilation,was investigated.The experiments revealed a clear preference of the fungus for glucose over glycerol.On the other hand,storage polysaccharides are degraded instead of storage lipid at the late oleaginous phase for maintenance purpose.These new biochemical features will enable the design of appropriate growth media for the co-fermentation of these two substrates by U.isabellina with the aim to maximize lipid accumulation.
关 键 词:Oleaginous microorganisms Umbelopsis isabellina Glucose and glycerol co-assimilation ALDOLASE Glycerol kinase Glycerol dehydrogenase
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