Algal Biology Research

Mass cultivation of Euglena gracilis in Open raceways

This study opens a window into the remarkable adaptability of Euglena gracilis (E. gracilis) under challenging nitrogen-starved conditions. Conducted in open ponds, the research uncovers a nuanced interplay between growth rates, paramylon content, and cell physiology in E. gracilis subjected to extended semi-continuous nitrogen starvation.

Tisochrysis Lutea lipidbody proteomics

In this study we focussed on the proteomic analysis of lipid bodies (LBs) in the alkenone-producing marine haptophyte alga Tisochrysis lutea. LBs, recognized as cellular carbon and energy storage organelles of microalgae. Here we successfully isolated and characterized the LBs from T. lutea. The isolated LBs, predominantly containing alkenones, were aptly named "alkenone bodies (ABs)." Proteins extracted from ABs were analyzed, revealing the presence of 514 proteins. Notable proteins included V-ATPase, a hypothetical protein found in other alkenone-producing haptophytes, and a lipid raft-associated SPFH domain-containing protein. The study suggests that the ABs of T. lutea are enveloped by a lipid membrane, potentially originating from the endoplasmic reticulum or the chloroplast, and serve as the storage site for alkenones and alkenes.

Unravelling carbon allocation mechanisms in the marine haptophyte Emiliania Huxleyi

Alkenones, unique long-chain methyl/ethyl ketones predominantly found in marine haptophytes like Emiliania huxleyi, remain enigmatic in terms of their physiological functions and metabolic profile. This study focused on unraveling the contribution of alkenones to energy storage and cellular carbon partitioning, particularly in relation to other vital cellular components.

Biosynthesis of modified fatty acids in bacteria and cyanobacteria

The study delves into unraveling the biosynthetic pathway of 10-methyl stearic acid (19:0Me10), a distinctive methyl-branched fatty acid synthesized by specific bacteria. The primary objective is to pinpoint novel S-adenosyl-L-methionine-dependent methyltransferases from Mycobacterium chlorophenolicum that play a role in the synthesis of 19:0Me10. This was confirmed by expression of the methyl transferases in E. coli and  in the alga Synechocystis sp.