Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine
Porcine blood is rich in protein and has always been the focus of research. Heme-peptides prepared from porcine hemoglobin are susceptible to oxidative degeneration during preparation and storage, thus affecting their function and stability. This study evaluated the enhancement effects of L-lysine (...
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2025-01-01
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| author | Yinghui Zhang Wei Cui Hui Zhou Lifang Zou Zhaoming Wang Kezhou Cai Baocai Xu |
| author_facet | Yinghui Zhang Wei Cui Hui Zhou Lifang Zou Zhaoming Wang Kezhou Cai Baocai Xu |
| author_sort | Yinghui Zhang |
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| description | Porcine blood is rich in protein and has always been the focus of research. Heme-peptides prepared from porcine hemoglobin are susceptible to oxidative degeneration during preparation and storage, thus affecting their function and stability. This study evaluated the enhancement effects of L-lysine (Lys) on recovery rate, antioxidant activity, stability, and structure. The results indicated that adding 1% Lys during enzymatic hydrolysis significantly increased the recovery rate of ferrous heme and peptide content by 93.88% and 15.30% (<i>p</i> < 0.05), respectively, and maximally enhanced antioxidant activity by 37.85% (<i>p</i> < 0.05). The contents of iron, ferrous ion, and ferrous heme in the heme-peptides were significantly increased by 97.52%, 121. 97%, and 74.45% (<i>p</i> < 0.05), respectively. Additionally, Lys improved the resistance to pH, temperature, metal ions, pepsin, and trypsin. Meanwhile, the effects of Lys resulted in heme-peptides with a smaller particle size, higher zeta potentials, and a smoother micromorphology. Fourier-transform infrared spectroscopy and fluorescence spectroscopy analysis showed that Lys enhanced the conformational stability of the heme-peptides. Molecular docking further suggested that hydrogen bonding was the main driver of the connections between Lys and the heme-peptides. This study provides theoretical guidance for the efficient utilization of heme-peptides in the food industry. |
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| institution | Kabale University |
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| language | English |
| publishDate | 2025-01-01 |
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| spelling | doaj-art-d057ce0c28374f109573bb779b04064f2025-01-24T13:32:49ZengMDPI AGFoods2304-81582025-01-0114219210.3390/foods14020192Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-LysineYinghui Zhang0Wei Cui1Hui Zhou2Lifang Zou3Zhaoming Wang4Kezhou Cai5Baocai Xu6Key Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaKey Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaKey Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaKey Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaKey Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaSchool of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, ChinaKey Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaPorcine blood is rich in protein and has always been the focus of research. Heme-peptides prepared from porcine hemoglobin are susceptible to oxidative degeneration during preparation and storage, thus affecting their function and stability. This study evaluated the enhancement effects of L-lysine (Lys) on recovery rate, antioxidant activity, stability, and structure. The results indicated that adding 1% Lys during enzymatic hydrolysis significantly increased the recovery rate of ferrous heme and peptide content by 93.88% and 15.30% (<i>p</i> < 0.05), respectively, and maximally enhanced antioxidant activity by 37.85% (<i>p</i> < 0.05). The contents of iron, ferrous ion, and ferrous heme in the heme-peptides were significantly increased by 97.52%, 121. 97%, and 74.45% (<i>p</i> < 0.05), respectively. Additionally, Lys improved the resistance to pH, temperature, metal ions, pepsin, and trypsin. Meanwhile, the effects of Lys resulted in heme-peptides with a smaller particle size, higher zeta potentials, and a smoother micromorphology. Fourier-transform infrared spectroscopy and fluorescence spectroscopy analysis showed that Lys enhanced the conformational stability of the heme-peptides. Molecular docking further suggested that hydrogen bonding was the main driver of the connections between Lys and the heme-peptides. This study provides theoretical guidance for the efficient utilization of heme-peptides in the food industry.https://www.mdpi.com/2304-8158/14/2/192by-productsheme-peptidesL-lysinestabilitystructure |
| spellingShingle | Yinghui Zhang Wei Cui Hui Zhou Lifang Zou Zhaoming Wang Kezhou Cai Baocai Xu Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine Foods by-products heme-peptides L-lysine stability structure |
| title | Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine |
| title_full | Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine |
| title_fullStr | Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine |
| title_full_unstemmed | Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine |
| title_short | Enhancement of Antioxidant Activity, Stability, and Structure of Heme-Peptides by L-Lysine |
| title_sort | enhancement of antioxidant activity stability and structure of heme peptides by l lysine |
| topic | by-products heme-peptides L-lysine stability structure |
| url | https://www.mdpi.com/2304-8158/14/2/192 |
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