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Dataset in the characterization of black spot Ehrenberg snapper and its proteins' denaturation inhibition by natural antioxidants.

ABSTRACT: The data represented in this paper describe techniques, methodologies and data obtained during the biochemical composition characterization of Blackspot Snapper (Ehrenberg's Snapper). Data analysis of protein, lipids, moisture, ash contents of Ehrenberg's snapper, total polyphenols, total flavonoids contents and the DPPH scavenging activities of Cinnamon (Cinnamomum verum J. Presl) bark (50 mg/50 g), cumin (Cuminum cyminum L.) (50 mg/50 g), turmeric (Turmerica longa L.) (50 mg/50 g), garlic (Allium sativum L.) (50 mg/50 g), ginger (Zingiber officinale Roscoe) (50 mg/50 g) and Vitamin C (25 mg/50 g) are represented. Data obtained from the Infrared spectroscopy (FTIR) analysis of the six spices and vitamin C treated and stored fillets at -25 °C, namely three vibrations, Amide A, NH stretching at 3300 cm-1; Amide I, C=O stretching 1600-1690 cm-1 and Amide II, CN stretching and NH bending at 1480-1575 cm-1. Differential scanning calorimetry (DSC) analysis data of three main denaturations; myosin, actin and sarcoplasmic proteins are presented.

SUBMITTER: Elgamouz A

PROVIDER: S-EPMC6920340 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Dataset in the characterization of black spot Ehrenberg snapper and its proteins' denaturation inhibition by natural antioxidants.

Elgamouz Abdelaziz A Alsaidi Rana R Alsaidi Alaa A Zahri Mostafa M Almehdi Ahmed A Bajou Khalid K

Data in brief 20191205

The data represented in this paper describe techniques, methodologies and data obtained during the biochemical composition characterization of Blackspot Snapper (Ehrenberg's Snapper). Data analysis of protein, lipids, moisture, ash contents of Ehrenberg's snapper, total polyphenols, total flavonoids contents and the DPPH scavenging activities of Cinnamon (Cinnamomum verum J. Presl) bark (50 mg/50 g), cumin (Cuminum cyminum L.) (50 mg/50 g), turmeric (Turmerica long ...[more]

PMID: 31879699

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Project description:This article describes the use of capillary electrophoresis (CE) to examine the influence of different cations (C(+); C(+) = Na(+) and tetra-n-alkylammonium, NR(4)(+), where R = Me, Et, Pr, and Bu) on the rates of denaturation of bovine carbonic anhydrase II (BCA) in the presence of anionic surfactant dodecylsulfate (DS(-)). An analysis of the denaturation of BCA in solutions of Na(+)DS(-) and NR(4)(+)DS(-) (in Tris-Gly buffer) indicated that the rates of formation of complexes of denatured BCA with DS(-) (BCA(D)-DS(-)(n,sat)) are indistinguishable and independent of the cation below the critical micellar concentration (cmc) and independent of the total concentration of DS(-) above the cmc. At concentrations of C(+)DS(-) above the cmc, BCA denatured at rates that depended on the cation; the rates decreased by a factor >10(4) in the order of Na(+) ? NMe(4)(+) > NEt(4)(+) > NPr(4)(+) > NBu(4)(+), which is the same order as the values of the cmc (which decrease from 4.0 mM for Na(+)DS(-) to 0.9 mM for NBu(4)(+)DS(-) in Tris-Gly buffer). The relationship between the cmc values and the rates of formation of BCA(D)-DS(-)(n,sat()) suggested that the kinetics of denaturation of BCA involve the association of this protein with monomeric DS(-) rather than with micelles of (C(+)DS(-))(n). A less-detailed survey of seven other proteins (?-lactalbumin, ?-lactoglobulin A, ?-lactoglobulin B, carboxypeptidase B, creatine phosphokinase, myoglobin, and ubiquitin) showed that the difference between Na(+)DS(-) and NR(4)(+)DS(-) observed with BCA was not general. Instead, the influence of NR(4)(+) on the association of DS(-) with these proteins depended on the protein. The selection of the cation contributed to the properties (including the composition, electrophoretic mobility, and partitioning behavior in aqueous two-phase systems) of aggregates of denatured protein and DS(-). These results suggest that the variation in the behavior of NR(4)(+)DS(-) with changes in R may be exploited in methods used to analyze and separate mixtures of proteins.

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Dataset in the characterization of black spot Ehrenberg snapper and its proteins' denaturation inhibition by natural antioxidants.

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Dataset in the characterization of black spot Ehrenberg snapper and its proteins' denaturation inhibition by natural antioxidants.

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