期刊
ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS
卷 20, 期 -, 页码 22-34出版社
ELSEVIER
DOI: 10.1016/j.algal.2016.09.006
关键词
Neochloris oleoabundans heterotrophic growth; Glucose; Nitrogen-limitation; Proteomics; Lipid and carbohydrate anabolism
资金
- NIEHS [ES06694]
- NIH/NCI [CA023074]
- BIO5 Institute of the University of Arizona
- NIH/NCRR [1S10 RR028868-01]
- University of Arizona, FSG (Faculty Seed Grant)
- Universidad Nacional Autonoma de Mexico (UNAM) [DGAPA/PAPIIT/UNAM IT200312]
- Mexican Council of Science and Technology (CONACyT)
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 metabolismpath ways were also found to be highly activated to redirect the carbon flow to ward 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. (C) 2016 Elsevier B.V. All rights reserved.
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