Toward an understanding of lipid and starch accumulation in microalgae: A proteomic study of Neochloris oleoabundans cultivated under N-limited heterotrophic conditions
Autor: | Daniela Morales-Sánchez, Kimberly L. Ogden, Alfredo Martinez, John Kyndt |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
biology 020209 energy Dehydrogenase Lipid metabolism 02 engineering and technology Metabolism Carbohydrate Pentose phosphate pathway Neochloris oleoabundans biology.organism_classification Pyruvate dehydrogenase complex 03 medical and health sciences 030104 developmental biology Biochemistry 0202 electrical engineering electronic engineering information engineering biology.protein Starch synthase Agronomy and Crop Science |
Zdroj: | Algal Research. 20:22-34 |
ISSN: | 2211-9264 |
DOI: | 10.1016/j.algal.2016.09.006 |
Popis: | Neochloris oleoabundans is an oleaginous microalga of biotechnological and commercial interest. A proteomic study was performed to compare the abundance of proteins under two different culture conditions: preferential lipid accumulation and preferential carbohydrate accumulation. When N. oleoabundans was cultivated under long periods of nitrogen starvation, the acyl carrier protein and the protein biotin carboxylase from the lipid synthesis pathway were found to be upregulated. The central metabolism pathways were also found to be highly activated to redirect the carbon flow toward pyruvate dehydrogenase and ATP synthesis. Pyruvate dehydrogenase was upregulated to supply the precursors for lipid production. Furthermore, in the pentose phosphate pathway, specifically glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were upregulated to supply reducing power in the form of NADPH for lipid synthesis and inorganic nitrogen assimilation. Carbohydrate synthesis-related enzymes that channel carbon to starch and sugar synthesis, such as UDP-glucose pyrophosphorylase and starch synthase, were upregulated when short durations of nitrogen limitation were applied during N. oleoabundans cultivation. However, ADP-glucose pyrophosphorylase was upregulated under preferential lipid accumulation conditions, indicating that under prolonged nitrogen starvation conditions, this enzyme potentially hydrolyzes starch chains to channel the carbon flow to lipid synthesis, which indicates a dual function of this protein. |
Databáze: | OpenAIRE |
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