Showing papers on "Salinispora arenicola published in 2019"
TL;DR: Salinaphthoquinones A-E (1-5) were isolated from a marine Salininispora arenicola strain, recovered from sediments of the St Peter and St. Paul Archipelago, Brazil, and a plausible biosynthetic pathway for 1-5 is proposed.
Abstract: Salinaphthoquinones A-E (1-5) were isolated from a marine Salininispora arenicola strain, recovered from sediments of the St. Peter and St. Paul Archipelago, Brazil. The structures of the compounds were elucidated using a combination of spectroscopic (NMR, IR, HRESIMS) data, including single-crystal X-ray diffraction analysis. A plausible biosynthetic pathway for 1-5 is proposed. Compounds 1 to 4 displayed moderate activity against Staphylococcus aureus and Enterococcus faecalis with MIC values of 125 to 16 μg/mL.
11 citations
TL;DR: Thin layer chromatography results confirmed that monosaccharide, disaccharides and maltotriose are the hydrolysis products and suggest that this α-amylase has considerable potential in industrial applications.
Abstract: α-Amylases are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. In this study, a novel gene encoding α-amylase was cloned from marine bacterium Salinispora arenicola CNP193 and the protein was expressed in Escherichia coli. The α-amylase gene from S. arenicola CNP193 had a length of 1839 bp and encoded a α-amylase with an estimated molecular mass of 74 kDa. The optimum temperature and pH for the recombinant α-amylase was 50 °C and 7 respectively. Na+, K+ and Ca2+ increased the activity of the recombinant α-amylase whereas the enzyme was inhibited by Cu2+, Zn2+, Hg2+, Pb2+, Fe3+ and Mn2+. Thin layer chromatography results confirmed that monosaccharide, disaccharide and maltotriose are the hydrolysis products. The results of our study suggest that this enzyme has considerable potential in industrial applications.
6 citations
TL;DR: Three new 3-hydroxy-N-methyl-2-oxindole (1 and 2) and 4-Hydroxy-pyran- 2-one (3) derivatives, along with the known 3- Hydrolysis-Methoxy-N -methyl-3-methylisatin derivatives, were isolated from a marine Salinispora arenicola strain from sediments of the St. Peter and St. Paul Archipelago, Brazil.
4 citations
TL;DR: A new gene from the amidase signature (AS) family, designated am, from the marine actinomycete Salinispora arenicola CNS-205, exhibited a wide substrate spectrum and showed amidase, aryl acylamidase, and acyl transferase activities.
Abstract: We cloned a new gene from the amidase signature (AS) family, designated am, from the marine actinomycete Salinispora arenicola CNS-205. As indicated by bioinformatics analysis and site-directed mutagenesis, the AM protein belonged to the AS family. AM was expressed, purified, and characterised in Escherichia coli BL21 (DE3), and the AM molecular mass was determined to be 51 kDa. The optimal temperature and pH were 40 °C and pH 8.0, respectively. AM exhibited a wide substrate spectrum and showed amidase, aryl acylamidase, and acyl transferase activities. AM had high activity towards aromatic and aliphatic amides. The AM substrate specificity for anilides was very narrow; only propanil could be used as an effective substrate. The extensive substrate range of AM indicates it may have broad potential applications in biosynthetic processes and biodegradation.
1 citations