Project description:The complete plastid genome sequence of the red macroalga Grateloupia taiwanensis S.-M.Lin & H.-Y.Liang (Halymeniaceae, Rhodophyta) is presented here. Comprising 191,270 bp, the circular DNA contains 233 protein-coding genes and 29 tRNA sequences. In addition, several genes previously unknown to red algal plastids are present in the genome of G. taiwanensis. The plastid genomes from G. taiwanensis and another florideophyte, Gracilaria tenuistipitata var. liui, are very similar in sequence and share significant synteny. In contrast, less synteny is shared between G. taiwanensis and the plastid genome representatives of Bangiophyceae and Cyanidiophyceae. Nevertheless, the gene content of all six red algal plastid genomes here studied is highly conserved, and a large core repertoire of plastid genes can be discerned in Rhodophyta.
Project description:In this study, we sequenced and annotated the complete chloroplast genome of Grateloupia turuturu Yamada (GenBank accession number: MN853877). The total length of the chloroplast genome is 188,547 bps, including 196 protein-encoding genes, 23 tRNA genes and 3 rRNA. The complete chloroplast genome of G. turuturu is 30.68% C + G, which is lower than that of A + T. The phylogenetic tree, which is based on core genes, shows that G. turuturu is clustered into the Grateloupia clade and has close genetic relationships with algae Grateloupia filicina and Grateloupia taiwanensis. These data will provide more information to understand the phylogenetic status of G. turuturu.
Project description:Grateloupia livida protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reducing power assays. The results suggested that hydrolysates obtained by neutral protease 1 h hydrolysis displayed the highest antioxidant activity (DPPH IC50 value of 3.96 mg/mL ± 0.41 mg/mL, ABTS IC50 value of 0.88 ± 0.13 mg/mL and reducing power of 0.531 ± 0.012 at 8 mg/mL), and had low molecular weight distribution (almost 99% below 3 kDa). Three fractions (F1-F3) were then isolated from the hydrolysates by using semi-preparative RP-HPLC, and the fraction F3 showed the highest antioxidant ability. Four antioxidant peptides were identified as LYEEMKESKVINADK, LEADNVGVVLMGDGR, LIDDSFGTDAPVPERL, and GLDELSEEDRLT from the F3 by LC-MS/MS. Online prediction showed that the four peptides possessed good water solubility, non-toxic and non-allergenic characteristics. Moreover, the LYEEMKESKVINADK exhibited the highest antioxidant ability. Molecular docking revealed that these peptides could all well bind with Kelch-like ECH-associated protein 1 (Keap1), among which LYEEMKESKVINADK had the lowest docking energy (-216.878 kcal/mol). These results demonstrated that the antioxidant peptides from Grateloupia livida could potentially be used as natural antioxidant.