Application of NMR spectroscopy for the detection and quantification of phthalic acid in fish muscles: The case of Atlantic Cod from Norwegian Sea.

Plastic litter might contain phthalates that can be transferred to marine environment or can be introduced into the marine food chain. Phthalic acid is the final product of phthalate decomposition in marine organisms. Here we used NMR spectroscopy to determine and quantify phthalic acid and dimethyl phthalate in fish muscles.

Nutritionally Enriched Muffins from Roselle Calyx Extract Using Response Surface Methodology.

, often called Roselle, is a flowering plant with a variety of traditional medicinal uses. Its calyx, with a bright and attractive red color, produces a tart and pleasant acidic taste. The purpose of this study was to develop a Roselle muffin and assess the acceptability, nutrition, and shelf life of the muffin using its ingredients.

Effect of Different Drying Methods on the Nutritional Value of Calyces as Revealed by NMR Metabolomics.

Red mature calyces of were collected from 16 different locations in Meghalaya, India. Samples were processed using shade drying (SD) and tray drying (TD). NMR spectroscopy was used to assess the metabolic composition of the calyces.

Assessment of Astaxanthin Accumulation in Hepatocytes of Atlantic Salmon Fed Different Diets Using NMR Spectroscopy.

This study aimed to assess the astaxanthin (Ax) accumulation in hepatocytes isolated from farmed Atlantic salmon fed different diets (rich marine, poor, poor with marine phospholipids (MPL) and poor with docosahexaenoic acid (DHA)). Nuclear magnetic resonance (NMR) spectroscopy was used for the Ax detection and quantification. The use of the C-enriched Ax allowed the assessment of short-time Ax metabolism.

Determination of Glyphosate in Dried Wheat by H-NMR Spectroscopy.

A wheat field was sprayed with a dosage of 1.1 kg a.i.

Differentiation of fresh and thawed Atlantic salmon using NMR metabolomics.

NMR metabolomics approach was used to distinguish fresh and thawed Atlantic salmon. Statistical analysis revealed significant differences in the concentration of some metabolites in reference and frozen-thawed fish during its storage. It was found that salmon freezing/thawing caused a significant increase in the concentration of fumarate and phenylalanine in stored salmon muscle.

Changes in the Composition of Atlantic Salmon upon the Brown Seaweed () Treatment.

This study shows the potential of improving the taste and shelf life of salmon by storing it in conjunction with sugar kelp. The influence of the addition of wet sugar kelp to Atlantic salmon fillet was assessed using a Nuclear Magnetic Resonance (NMR) metabolomics approach. Seaweed treatment caused significant changes in the polar and non-polar metabolic composition of salmon muscle upon its storage.

Development of a statistical model to detect quality and storage conditions of Atlantic salmon.

The ever-increasing demand for fish as a food, has led to the development of new handling and packaging technologies resulting in premium quality fish products. In order to avoid frauds reaching the market, fish quality assurance methods need to be developed. In this study, two statistical models of biochemical processes that occur in Atlantic salmon during two weeks of storage at 0 and 4 °C were developed.

Quality changes of salmon by-products during storage: Assessment and quantification by NMR.

Safe utilization of fish by-products is an important task due to increasing fish consumption. It can provide new valuable food/feed and will increase the economical profit and sustainability of the fishery industry. NMR spectroscopy is a reliable tool able to monitor qualitative and quantitative changes in by-products.

NMR approach for monitoring post-mortem changes in Atlantic salmon fillets stored at 0 and 4°C.

High resolution NMR technique has been used to monitor post-mortem changes in salmon (Salmo salar) fillets upon storage at 4 and 0°C. Thirty-one different fish metabolites influencing freshness and taste properties have been unequivocally assigned by NMR using either available standard compounds or ad hoc acquired 2D (1)H-(1)H TOCSY and (1)H-(13)С HSQC spectra. The monitored fish metabolites include amino acids, dipeptides, sugars, vitamins, biogenic amines, as well as different products of the ATP degradation.

Competitive cobalt for zinc substitution in mammalian methionine sulfoxide reductase B1 overexpressed in E. coli: structural and functional insight.

Expression of the mammalian enzyme methionine sulfoxide reductase B1 (MsrB1) in Escherichia coli growing in cobalt-containing media resulted in the reproducible appearance of the stable cobalt-containing protein MsrB1-Co. NMR studies and biocomputing using the programs AnisoFit and Amber allowed us to generate a structure of MsrB1-Co sharing the overall fold with the native zinc-containing protein MsrB1-Zn. Our data suggest that the N-terminus containing resolving cysteine tends to be closer to the protein's catalytic center than was previously reported.

Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase.

Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.48 ± 0.

Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin.

Maintenance of the cellular redox balance has vital importance for correcting organism functioning. Methionine sulfoxide reductases (Msrs) are among the key members of the cellular antioxidant defence system. To work properly, methionine sulfoxide reductases need to be reduced by their biological partner, thioredoxin (Trx).

Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2.

Methionine sulfoxide reductases are antioxidant enzymes that repair oxidatively damaged methionine residues in proteins. Mammals have three members of the methionine-R-sulfoxide reductase family, including cytosolic MsrB1, mitochondrial MsrB2, and endoplasmic reticulum MsrB3. Here, we report the solution structure of reduced Mus musculus MsrB2 using high resolution nuclear magnetic resonance (NMR) spectroscopy.

¹H, ¹³C, and ¹⁵N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR.

Two forms of the glutaredoxin (Grx) domain (full length Grx domain and short Grx lacking the N-terminal region) of Mus musculus thioredoxin glutathione reductase (TGR) were isotopically labelled with (15)N and (13)C isotopes, expressed and purified to homogeneity. We report here the (1)H, (13)C and (15)N NMR assignment for both Grx forms of this mouse TGR. This investigation represents the first NMR analysis of a mammalian TGR.

Interaction of selenoprotein W with 14-3-3 proteins: a computational approach.

SelW, a protein containing a selenocysteine (Sec) in a conserved Cys-X-X-Sec motif, has been suggested to have an antioxidant role in cell metabolism. SelW is known to specifically interact with different isoforms of 14-3-3 proteins. The latter are involved in several cellular processes such as regulation of the cell cycle, metabolism control, apoptosis, protein trafficking, and gene transcription.

Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis.

Methionine sulfoxide reductases protect cells by repairing oxidatively damaged methionine residues in proteins. Here, we report the first three-dimensional structure of the mammalian selenoprotein methionine sulfoxide reductase B1 (MsrB1), determined by high resolution NMR spectroscopy. Heteronuclear multidimensional spectra yielded NMR spectral assignments for the reduced form of MsrB1 in which catalytic selenocysteine (Sec) was replaced with cysteine (Cys).

Protonation of kanamycin A: detailing of thermodynamics and protonation sites assignment.

Protonation of an aminoglycoside antibiotic kanamycin A sulfate was studied by potentiometric titrations at variable ionic strength, sulfate concentration and temperature. From these results the association constants of differently protonated forms of kanamycin A with sulfate and enthalpy changes for protonation of each amino group were determined. The protonation of all amino groups of kanamycin A is exothermic, but the protonation enthalpy does not correlate with basicity as in a case of simple polyamines.

Biosynthesis of macrolactam BE-14106 involves two distinct PKS systems and amino acid processing enzymes for generation of the aminoacyl starter unit.

BE-14106 is a macrocyclic lactam with an acyl side chain previously identified in a marine-derived Streptomyces sp. The gene cluster for BE-14106 biosynthesis was cloned from a Streptomyces strain newly isolated from marine sediments collected in the Trondheimsfjord (Norway). Bioinformatics and experimental analyses of the genes in the cluster suggested an unusual mechanism for assembly of the molecule.

Insights into the evolution of macrolactam biosynthesis through cloning and comparative analysis of the biosynthetic gene cluster for a novel macrocyclic lactam, ML-449.

A new compound, designated ML-449, structurally similar to the known 20-membered macrolactam BE-14106, was isolated from a marine sediment-derived Streptomyces sp. Cloning and sequencing of the 83-kb ML-449 biosynthetic gene cluster revealed its high level of similarity to the BE-14106 gene cluster. Comparison of the respective biosynthetic pathways indicated that the difference in the compounds' structures stems from the incorporation of one extra acetate unit during the synthesis of the acyl side chain.

1H, 15N and 13C NMR assignments of mouse methionine sulfoxide reductase B2.

A recombinant mouse methionine-r-sulfoxide reductase 2 (MsrB2 Delta S) isotopically labeled with (15)N and (15)N/(13)C was generated. We report here the (1)H, (15)N, and (13)C NMR assignments of the reduced form of this protein.

Functions and evolution of selenoprotein methionine sulfoxide reductases.

Methionine sulfoxide reductases (Msrs) are thiol-dependent enzymes which catalyze conversion of methionine sulfoxide to methionine. Three Msr families, MsrA, MsrB, and fRMsr, are known. MsrA and MsrB are responsible for the reduction of methionine-S-sulfoxide and methionine-R-sulfoxide residues in proteins, respectively, whereas fRMsr reduces free methionine-R-sulfoxide.

Improved antifungal polyene macrolides via engineering of the nystatin biosynthetic genes in Streptomyces noursei.

Seven polyene macrolides with alterations in the polyol region and exocyclic carboxy group were obtained via genetic engineering of the nystatin biosynthesis genes in Streptomyces noursei. In vitro analyses of the compounds for antifungal and hemolytic activities indicated that combinations of several mutations caused additive improvements in their activity-toxicity properties. The two best analogs selected on the basis of in vitro data were tested for acute toxicity and antifungal activity in a mouse model.

Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins.

Selenium is a trace element with significant biomedical potential. It is essential in mammals due to its occurrence in several proteins in the form of selenocysteine (Sec). One of the most abundant mammalian Sec-containing proteins is selenoprotein W (SelW).