期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 70, 期 45, 页码 14488-14498出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.2c05211
关键词
fermented barley protein; lipid-lowering; protein purification; HepG2 cell
资金
- priority academic program development of Jiangsu Higher education institutions
- National Natural Science Foundation of China
- China Postdoctoral Science Foundation
- [32072200]
- [2019M651747]
In this study, a protein with lipid-lowering activity was isolated, purified, and identified from barley using Lactiplantibacillus plantarum dy-1 fermentation. The purified protein, LFBEP-C1, showed the best lipid-lowering potential and had a structural composition rich in hydrophobic amino acids. The findings suggest that LFBEP-C1 could be a potential therapeutic candidate for lipid-lowering treatment.
Previous studies have found that the protein in barley extract fermented by Lactiplantibacillus plantarum dy-1 has the ability to inhibit lipid accumulation. However, the isolation, purification, and structural identification of the protein with lipid-lowering activity were still needed. In the present study, barley protein fermented by L. plantarum dy-1 with the optimal lipid-lowering ability was isolated and purified in three steps: using ammonium sulfate precipitation, anion-exchange chromatography, and size-exclusion chromatography. Combined with the model of HepG2 cells induced by oleic acid, the results showed that the pure protein LFBEP-C1 had the best lipid-lowering potential. Furthermore, our research found that LFBEP-C1 enriched the content of hydrophobic amino acids in LFBEP-C1. Ultraviolet spectroscopy analysis indicated that the glycosidic bond in LFBEP-C1 was an O-type glycosidic bond. The FTIR and circular dichroism spectra indicated that alpha-helix and random coil were the main secondary structures of LFBEP-C1. Mass spectrometry determined the theoretical molecular weight of LFBEP-C1 as 48 kDa, and its amino acid coverage was 63%. These findings suggest that the protein LFBEP-C1 with the best lipid-lowering activity was isolated and purified, and its structural characteristics were identified.
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