Formation mechanism of low-density lipoprotein gel induced by NaCl
| Autor: | Yonggang Tu, Lilan Xu, Mingsheng Xu, Yan Zhao, Xuliang Nie, Na Wu |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Food Handling
Eggs Sodium Chloride Protein Structure Secondary 03 medical and health sciences chemistry.chemical_compound Spectroscopy Fourier Transform Infrared Asian country Animals Food science Fourier transform infrared spectroscopy Eggshell Protein secondary structure Water content 030304 developmental biology 0303 health sciences 0402 animal and dairy science Salting 04 agricultural and veterinary sciences General Medicine 040201 dairy & animal science Lipoproteins LDL Ducks chemistry Low-density lipoprotein lipids (amino acids peptides and proteins) Animal Science and Zoology Gels Lipoprotein |
| Zdroj: | Poultry Science. 98:5166-5176 |
| ISSN: | 0032-5791 |
| DOI: | 10.3382/ps/pez232 |
| Popis: | Salted eggs, which are a traditional Chinese egg product, are favored by Chinese consumers and have become very popular in other Asian countries due to their unique features such as "fresh, fine, tender, loose, gritty and oily texture." In order to illuminate the forming process of salted egg, the gelation behavior and mechanism of low-density lipoprotein (LDL) induced by NaCl were investigated using marinated model outside the eggshell. Results showed that as the salting proceeded, the moisture content exhibited a decreasing trend. The NaCl content, oil exudation, hardness, and surface hydrophobicity showed constantly increasing trends. In the early stages of salting, the size of the LDL particles, soluble protein content, and T21 increased, whereas T21 (with D2O), T22, and the free sulfhydryl content declined. In the later stages of salting, LDL formed a multiple composite aggregate gel structure with filamentous apoproteins and non-spherical lipid particles intertwined with each other. The soluble protein content and T23 (without D2O) decreased, whereas T21 (with D2O), T22 and the free sulfhydryl content increased. Fourier transform infrared spectroscopy revealed that the fresh LDL mainly consisted of α-helix and β-sheet structures. After the gel becomes hardened, the LDL secondary structure was changed remarkably, characterized by the decrease of α-helix elements and increase of β-sheet elements. The results suggested that the oil exudation of salted LDL gels was mainly due to LDL destruction and the release of components (apoproteins, phospholipids, and neutral lipids) facilitated by increased interactions between apoproteins and lipids. |
| Databáze: | OpenAIRE |
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