Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof
With the development of camel-derived food and pharmaceutical cosmetics, camel hoof, as a unique by-product of the camel industry, has gradually attracted the attention of scientific researchers in the fields of nutrition, health care, and biomaterial development. In this study, the protein composit...
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MDPI AG
2023-09-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/17/3303 |
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| author | Yingli Wang Le Song Chengcheng Guo Rimutu Ji |
| author_facet | Yingli Wang Le Song Chengcheng Guo Rimutu Ji |
| author_sort | Yingli Wang |
| collection | DOAJ |
| description | With the development of camel-derived food and pharmaceutical cosmetics, camel hoof, as a unique by-product of the camel industry, has gradually attracted the attention of scientific researchers in the fields of nutrition, health care, and biomaterial development. In this study, the protein composition and collagen type of Bactrian camel hoof collagen extract (CHC) were analyzed by LC-MS/MS, and the functional properties of CHC were further investigated, including its rheological characteristics, emulsification and emulsion stability, and hygroscopicity and humectancy. Proteomic identification confirmed that CHC had 13 collagen subunits, dominated by type I collagen (α1, α2), with molecular weights mainly in the 100–200 KDa range and a pI of 7.48. An amino acid study of CHC revealed that it carried the standard amino acid profile of type I collagen and was abundant in Gly, Pro, Glu, Ala, and Arg. Additionally, studies using circular dichroism spectroscopy and Fourier transform infrared spectroscopy revealed that CHC contains a collagen-like triple helix structure that is stable and intact. Different concentrations of CHC solutions showed shear-thinning flow behavior. Its tan δ did not differ much with increasing concentration. The CHC has good emulsifying ability and stability, humectancy, and hygroscopicity. This study provides a basis for utilizing and developing Bactrian camel hoof collagen as a functional ingredient. |
| first_indexed | 2024-03-10T23:22:59Z |
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| id | doaj.art-d8c8f963457a44429b19350cf5c9290a |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T23:22:59Z |
| publishDate | 2023-09-01 |
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| spelling | doaj.art-d8c8f963457a44429b19350cf5c9290a2023-11-19T08:09:40ZengMDPI AGFoods2304-81582023-09-011217330310.3390/foods12173303Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) HoofYingli Wang0Le Song1Chengcheng Guo2Rimutu Ji3College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, ChinaCollege of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, ChinaCollege of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, ChinaCollege of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, ChinaWith the development of camel-derived food and pharmaceutical cosmetics, camel hoof, as a unique by-product of the camel industry, has gradually attracted the attention of scientific researchers in the fields of nutrition, health care, and biomaterial development. In this study, the protein composition and collagen type of Bactrian camel hoof collagen extract (CHC) were analyzed by LC-MS/MS, and the functional properties of CHC were further investigated, including its rheological characteristics, emulsification and emulsion stability, and hygroscopicity and humectancy. Proteomic identification confirmed that CHC had 13 collagen subunits, dominated by type I collagen (α1, α2), with molecular weights mainly in the 100–200 KDa range and a pI of 7.48. An amino acid study of CHC revealed that it carried the standard amino acid profile of type I collagen and was abundant in Gly, Pro, Glu, Ala, and Arg. Additionally, studies using circular dichroism spectroscopy and Fourier transform infrared spectroscopy revealed that CHC contains a collagen-like triple helix structure that is stable and intact. Different concentrations of CHC solutions showed shear-thinning flow behavior. Its tan δ did not differ much with increasing concentration. The CHC has good emulsifying ability and stability, humectancy, and hygroscopicity. This study provides a basis for utilizing and developing Bactrian camel hoof collagen as a functional ingredient.https://www.mdpi.com/2304-8158/12/17/3303Bactrian camel hoofcollagenproteomic analysischaracterization |
| spellingShingle | Yingli Wang Le Song Chengcheng Guo Rimutu Ji Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof Foods Bactrian camel hoof collagen proteomic analysis characterization |
| title | Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof |
| title_full | Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof |
| title_fullStr | Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof |
| title_full_unstemmed | Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof |
| title_short | Proteomic Identification and Characterization of Collagen from Bactrian Camel (<i>Camelus bactrianus</i>) Hoof |
| title_sort | proteomic identification and characterization of collagen from bactrian camel i camelus bactrianus i hoof |
| topic | Bactrian camel hoof collagen proteomic analysis characterization |
| url | https://www.mdpi.com/2304-8158/12/17/3303 |
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