ABSTRACT
We measured total mercury (Hg) and selenium (Se) concentrations as well as stable nitrogen (N) isotopic composition in flyingfish and squid muscle tissues from the eastern Indian Ocean and western South China Sea. The results showed that the mean Hg concentration in squid muscle from the western South China Sea was lower than that in the eastern Indian Ocean. The Hg concentrations in flyingfish and squid muscle samples were positively correlated with organism size (length and weight) and δ15N in all the study areas. Furthermore, we found a negative correlation between Se and Hg in molar content of flyingfish and squid muscle from the western South China Sea. The Se:Hg molar ratio was significantly negative correlated with fish weight and δ15N, suggesting that the Se:Hg molar ratio decreases with the increase of fish size and trophic level in the food web.
Subject(s)
Beloniformes/metabolism , Decapodiformes/metabolism , Environmental Monitoring/methods , Mercury/analysis , Selenium/analysis , Water Pollutants, Chemical/analysis , Animals , China , Food Chain , Indian Ocean , Mercury/metabolism , Muscles/chemistry , Seafood/analysis , Selenium/metabolism , Water Pollutants, Chemical/metabolismABSTRACT
We purified and characterized Type I collagen from the scales of the Pacific saury (Cololabis saira) and compared it with collagen from other organisms. Subunit composition of C. saira collagen (2α1+α2) was similar to that of red sea bream (Pagrus major) and porcine collagen. C. saira collagen did not form a firm gel after neutralization of pH in solution. The temperature of denaturation (24-25 °C) of C. saira collagen was slightly lower than that of P. major collagen (26-27 °C). The contents of proline and hydroxyproline were lower in red sea bream and Pacific saury collagen than in porcine collagen. Circular dichroism spectra and Fourier-transformed infrared spectra showed that heat denaturation caused unfolding of the triple helices in all three collagens.
Subject(s)
Beloniformes/metabolism , Collagen/chemistry , Animals , Circular Dichroism , Gels/chemistry , Hydrogen-Ion Concentration , Hydroxyproline/chemistry , Proline/chemistry , Protein Denaturation , Protein Stability , Protein Structure, Secondary , Sea Bream/metabolism , Spectroscopy, Fourier Transform Infrared , Swine , Transition TemperatureABSTRACT
In the present study, protein of muscles of commercially important marine fishes Nemipterus japonicus and Exocoetus volitans were extracted by trypsin and their hydrolysis conditions viz., temperature, time, and enzyme to substrate concentration on degree of hydrolysis were studied by response surface methodology. The optimum values for N. japonicus was found as temperature, 30°C, hydrolysis time of 100 min an enzyme/substrate concentration of 1.59% whereas, for E. volitans muscle protein, optimum hydrolysis conditions were temperature, 30°C, hydrolysis time of 115 min and enzyme/substrate concentration of 1.67%. Furthermore, amino acid sequence of antioxidant peptides derived after chromatographic purification was identified by ESI-MS/MS. The analysis of peptides showed sequences as Glu-Ser-Asp-Arg-Pro (620.3 Da) and Gly-Trp-Met-Gly-Cys-Trp (747.3) for N. japonicus and E. volitans muscle, respectively. The peptides contained important antioxidant amino acids and acted as good antioxidant peptides to scavenge free radicals.
