Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation
This study aimed to characterize and identify calcium-chelating peptides from rabbit bone collagen and explore the underlying chelating mechanism. Collagen peptides and calcium were extracted from rabbit bone by instant ejection steam explosion (ICSE) combined with enzymatic hydrolysis, followed by...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2024-05-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | https://www.sciopen.com/article/10.26599/FSHW.2022.9250125 |
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| author | Fuhuan Yuan Yu Fu Liang Ma Hankun Zhu Yong Yu Xin Feng Yi Sun Hongjie Dai Xin Liu Zhengfang Liu Yuhao Zhang |
| author_facet | Fuhuan Yuan Yu Fu Liang Ma Hankun Zhu Yong Yu Xin Feng Yi Sun Hongjie Dai Xin Liu Zhengfang Liu Yuhao Zhang |
| author_sort | Fuhuan Yuan |
| collection | DOAJ |
| description | This study aimed to characterize and identify calcium-chelating peptides from rabbit bone collagen and explore the underlying chelating mechanism. Collagen peptides and calcium were extracted from rabbit bone by instant ejection steam explosion (ICSE) combined with enzymatic hydrolysis, followed by chelation reaction to prepare rabbit bone peptide-calcium chelate (RBCP-Ca). The chelating sites were further analyzed by liquid chromatography-tandem mass (LC-MS/MS) spectrometry while the chelating mechanism and binding modes were investigated. The structural characterization revealed that RBCP successfully chelated with calcium ions. Furthermore, LC-MS/MS analysis indicated that the binding sites included both acidic amino acids (Asp and Glu) and basic amino acids (Lys and Arg). Interestingly, three binding modes, namely Inter-Linking, Loop-Linking and Mono-Linking were for the first time found, while Inter-Linking mode accounted for the highest proportion (75.1%), suggesting that chelation of calcium ions frequently occurred between two peptides. Overall, this study provides a theoretical basis for the elucidation of chelation mechanism of calcium-chelating peptides. |
| format | Article |
| id | doaj-art-bbeae42d90244784938a98121d6861a5 |
| institution | Kabale University |
| issn | 2097-0765 2213-4530 |
| language | English |
| publishDate | 2024-05-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-bbeae42d90244784938a98121d6861a52025-01-10T06:54:23ZengTsinghua University PressFood Science and Human Wellness2097-07652213-45302024-05-011331485149310.26599/FSHW.2022.9250125Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidationFuhuan Yuan0Yu Fu1Liang Ma2Hankun Zhu3Yong Yu4Xin Feng5Yi Sun6Hongjie Dai7Xin Liu8Zhengfang Liu9Yuhao Zhang10College of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaAngel Yeast Co., Ltd., Yichang 443003, ChinaAngel Yeast Co., Ltd., Yichang 443003, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaThis study aimed to characterize and identify calcium-chelating peptides from rabbit bone collagen and explore the underlying chelating mechanism. Collagen peptides and calcium were extracted from rabbit bone by instant ejection steam explosion (ICSE) combined with enzymatic hydrolysis, followed by chelation reaction to prepare rabbit bone peptide-calcium chelate (RBCP-Ca). The chelating sites were further analyzed by liquid chromatography-tandem mass (LC-MS/MS) spectrometry while the chelating mechanism and binding modes were investigated. The structural characterization revealed that RBCP successfully chelated with calcium ions. Furthermore, LC-MS/MS analysis indicated that the binding sites included both acidic amino acids (Asp and Glu) and basic amino acids (Lys and Arg). Interestingly, three binding modes, namely Inter-Linking, Loop-Linking and Mono-Linking were for the first time found, while Inter-Linking mode accounted for the highest proportion (75.1%), suggesting that chelation of calcium ions frequently occurred between two peptides. Overall, this study provides a theoretical basis for the elucidation of chelation mechanism of calcium-chelating peptides.https://www.sciopen.com/article/10.26599/FSHW.2022.9250125rabbit bonecollagen peptidepeptide-calcium chelatechelation mechanismliquid chromatography-tandem mass (lc-ms/ms) |
| spellingShingle | Fuhuan Yuan Yu Fu Liang Ma Hankun Zhu Yong Yu Xin Feng Yi Sun Hongjie Dai Xin Liu Zhengfang Liu Yuhao Zhang Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation Food Science and Human Wellness rabbit bone collagen peptide peptide-calcium chelate chelation mechanism liquid chromatography-tandem mass (lc-ms/ms) |
| title | Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation |
| title_full | Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation |
| title_fullStr | Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation |
| title_full_unstemmed | Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation |
| title_short | Calcium-chelating peptides from rabbit bone collagen:characterization, identif ication and mechanism elucidation |
| title_sort | calcium chelating peptides from rabbit bone collagen characterization identif ication and mechanism elucidation |
| topic | rabbit bone collagen peptide peptide-calcium chelate chelation mechanism liquid chromatography-tandem mass (lc-ms/ms) |
| url | https://www.sciopen.com/article/10.26599/FSHW.2022.9250125 |
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