Effect of Temperature and Light Intensity on the Polar Lipidome of Endophytic Brown Algae Streblonema corymbiferum and Streblonema sp. In Vitro.

The effect of temperature and light intensity on the polar lipidome of endophytic brown algae Streblonema corymbiferum and Streblonema sp. in vitro was investigated. More than 460 molecular species have been identified in four glycoglycerolipids classes, five phosphoglycerolipids classes and one betaine lipid class. The lipids glucuronosyldiacylglycerol and diacylglyceryl-N,N,N-trimethyl-homoserine were found in the algae of the order Ectocarpales for the first time. A decrease in cultivation temperature led to an increase in the unsaturation level in all classes of polar lipids. Thus, at low temperatures, the content of 18:4/18:4 monogalactosyldiacylglycerol (MGDG), 20:5/18:4 digalactosyldiacylglycerol (DGDG), 18:3/16:0 sulfoquinovosyldiacylglycerol (SQDG), 18:3/18:3 and 18:3/18:4 phosphatidylglycerol (PG), 20:4/20:5 and 20:5/20:5 phosphatidylethanolamine (PE), 14:0/20:5, 16:0/20:5 and 20:5/20:5 phosphatidylcholine (PC), 20:5/20:4 phosphatidylhydroxyethylglycine and 18:1/18:2 DGTS increased. At high temperatures, an increase in the content of chloroplast-derived MGDG, DGDG and PG was observed. Both low and high light intensities caused an increase in 20:5/18:3 MGDG and 18:3/16:1 PG. At low light intensity, the content of DGDG with fatty acid (FA) 18:3 increased, and at high light intensity, it was with FA 20:5. The molecular species composition of extraplastid lipids also showed a dependence on light intensity. Thus, the content of PC and PE species with C20-polyunsaturated FA at both sn-positions, 18:1/18:1 DGTS and 16:0/18:1 phosphatidylinositol increased. Low light intensity induced a significant increase in the content of chloroplast-derived 18:1/16:1 phosphatidylethanolamine.

The Effect of Fucoidan from the Brown Alga Fucus evanescence on the Activity of α-N-Acetylgalactosaminidase of Human Colon Carcinoma Cells.

α-N-acetylgalactosaminidase (EC 3.2.1.49) (alpha-NaGalase) catalyzes the hydrolysis of N-acetamido-2-deoxy-α-d-galactoside residues from non-reducing ends of various complex carbohydrates and glycoconjugates. It is known that human cancer cells express an alpha-NaGalase, which accumulates in the blood plasma of patients. The enzyme deglycosylates the Gc protein-derived macrophage activating factor (GcMAF) and inhibits macrophage activity acting as an immunosuppressor. The high specific activity 0.033 ± 0.002 μmol mg−1 min−1 of the enzyme was found in human colon carcinoma cells DLD-1. The alpha-NaGalase of DLD-1 cells was isolated and biochemical characterized. The enzyme exhibits maximum activity at pH 5.2 and temperature 55 °C. The Km is 2.15 mM, Vmax⁻0.021 μmol min−1 mL−1, kcat⁻1.55 min−1 and kcat/Km⁻0.72 min−1 mM−1 at 37 °C, pH 5.2. The effects of fucoidan from the brown alga Fucus evanescence on the activity of alpha-NaGalase in human colon carcinoma DLD-1 cells and on the biosynthesis of this enzyme were investigated. It was shown that fucoidan did not inhibit free alpha-NaGalase, however, it reduced the expression of the enzyme in the DLD-1 cells at IC50 73 ± 4 μg mL−1.