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Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus.

ABSTRACT: The physicochemical and functional properties of myofibrillar protein (MP), sarcoplasmic protein (SP), and myostromin (MY) in Hypomesus olidus muscle were evaluated and reported in this study. These fractions are rich in Glu. Three proteins exhibited significantly different morphologies, colors, and particle sizes. The main protein bands of MP, SP, and MY are 15-220 kDa, 26-60 kDa, and 15-245 kDa, respectively. In particular, MP is more hydrophobic. Three proteins exhibited a maximum UV absorption peak at 270 nm, and all amide I secondary structures were shown to be composed of repetitive units (e.g., α-helices and β-sheets). The three proteins demonstrated a predominantly amorphous halo, with T_d values of 52.22 °C, 59.16 °C, and 58.09 °C. Regarding their properties in water/oil absorption, emulsification, and foaming, MP is the most preferred, followed by SP and MY. In conclusion, Hypomesus olidus muscle proteins are novel and potential functional nutrition ingredients for the food industry.

SUBMITTER: Fu Y

PROVIDER: S-EPMC9615135 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature

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Physicochemical and functional properties of the muscle protein fraction of <i>Hypomesus olidus</i>.

Fu Yuan Y Liu Chuanhao C Yan Xiaohui X Jiang Guochuan G Dang Qiao Q Wang Liyan L Liu Xuejun X

Food chemistry: X 20221020

The physicochemical and functional properties of myofibrillar protein (MP), sarcoplasmic protein (SP), and myostromin (MY) in <i>Hypomesus olidus</i> muscle were evaluated and reported in this study. These fractions are rich in Glu. Three proteins exhibited significantly different morphologies, colors, and particle sizes. The main protein bands of MP, SP, and MY are 15-220 kDa, 26-60 kDa, and 15-245 kDa, respectively. In particular, MP is more hydrophobic. Three proteins exhibited a maximum UV a ...[more]

PMID: 36313272

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Project description:Lyophilization is the process of drying and improving the stability of various pharmaceutical preparations. In this work we evaluated the properties of 11 hydrophilic gels calcium dobesilate with liposomes based on soybean lecithin, subjected to the freeze-drying procedure. Liposomes were produced by using method thin lipid film. Lyophilization was carried out under conditions of temperature equal (-30 °C) and pressure 0.37 mbar. We evaluated the preparations with dynamic light scattering (DLS) method, optical microscopy and Fourier-transform infrared spectroscopy (FTIR). In this work we presented the average results for the particle diameter in the sample and PDI (polydispersity index) value for the samples that produced the results. When testing using the DLS method on a Malvern Zetaseizer, results for 7 samples were not obtained. Two of next four samples were characterized by an increased size of the liposome particle resulting from a lower concentration of ethanol compared to the rest of them. Three samples under the microscope did not show any differences. It was possible only to see single crystals probably of undissolved calcium dobesilate. Some clusters were observed in the 4 samples, and when they appeared they were very small. The aggregates and irregular liposomes present in the rest of the samples may have been formed due to the destabilizing activity of ethanol towards lipid membranes. In the FTIR spectrum for MC, the peak was observed at the wavenumber of ca. 2900 cm-1 and of about 1050 cm-1. In case of pure calcium dobesilate we observed low pick at the wavenumber of about 3400 cm-1. The spectrum has a low peak at the wavenumber of 1450 cm-1 and intense peaks ranging from approx. 1000 cm-1 to approx. 1200 cm-1. Decay of the lecithin peak in formulations with liposomes at 1725 cm-1 wavelength may indicate the occurrence of the hydrolysis reaction in the system. Probably there was a hydrolysis of the ester bond connecting the rest of the phosphoric acid and the choline with the glycerol residue.

Dataset Information

Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus.

Publications

Physicochemical and functional properties of the muscle protein fraction of <i>Hypomesus olidus</i>.

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