Amino acid profile of collagen fractions extracted from by-products of<i>Ophistonema libertate</i>and<i>Scomber japonicus</i>

García-Sifuentes, Celia Olivia; Lugo‐Sánchez, María Elena; Scheuren‐Acevedo, Susana María; Martínez‐Porchas, Marcel; Peralta-Martínez, V.

doi:10.1080/19476337.2015.1101711

Cited by 2 publications

(1 citation statement)

References 29 publications

(29 reference statements)

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“…CHC had the highest glycine (15.11 ± 1.78 g/100 g), followed by proline (9.54 ± 1.06 g/100 g), glutamic acid (7.28 ± 0.46 g/100 g), alanine (6.20 ± 0.38 g/100 g), and hydroxyproline (6.06 ± 1.16 g/100 g). The total content of hydroxyproline and proline was found to be 15.61 ± 1.28 g/100 g. In contrast to most proteins, collagen contains nearly 1/3 of glycine and is free of cysteine and tryptophan [24]. The sample comprised 153 proline, 97 hydroxyproline, and 243 glycine per 1000 residues of amino acids.…”

Section: Chc Amino Acid Compositionmentioning

confidence: 95%

Proteomic Identification and Characterization of Collagen from Bactrian Camel (Camelus bactrianus) Hoof

Wang,

Song,

Guo

et al. 2023

Foods

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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.

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Section: Chc Amino Acid Compositionmentioning

confidence: 95%

Proteomic Identification and Characterization of Collagen from Bactrian Camel (Camelus bactrianus) Hoof

Wang,

Song,

Guo

et al. 2023

Foods

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Characteristics of Collagen Preparations from Leather Wastes by the High Pressure Liquid Chromatography Method

Gendaszewska

Lasoń-Rydel

Ławińska

et al. 2021

FIBRES & TEXTILES in Eastern Europe

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The raw trimming waste from the leather industry is considered potential hazardous waste as a consequence of the chrome tanned leather process. On the other hand, leather waste contains a large amount of precious protein – collagen, which has many uses. Nowadays, collagen preparations obtained from leather waste are available on the market. This paper presents a procedure for the determination of amino acids in five collagen preparations of animal origin. Recent improvements in HPLC-based methods for analysing amino acids have made it feasible to analyse different sample types accurately. In this study the 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) derivatization procedure was applied. The amino acid analysis indicated the presence of 18 amino acids (Asp, Ser, Glu, His, Gly, Arg, Thr, Ala, Pro, Cys, Tyr, Val, Lys, Met, Ile, Leu, Phe and Hyp) in the collagen samples. Glycine, alanine, proline and hydroxyproline were the most abundant amino acid, whereas the lowest contents corresponded to serine, tyrosine, valine and izoleucine. The analysis proposed can be used with confidence in collagen quality control to guarantee appropriate amino acid content.

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Amino acid profile of collagen fractions extracted from by-products ofOphistonema libertateandScomber japonicus

Cited by 2 publications

References 29 publications

Proteomic Identification and Characterization of Collagen from Bactrian Camel (Camelus bactrianus) Hoof

Proteomic Identification and Characterization of Collagen from Bactrian Camel (Camelus bactrianus) Hoof

Characteristics of Collagen Preparations from Leather Wastes by the High Pressure Liquid Chromatography Method

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