Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii).
Identifieur interne : 000169 ( Main/Exploration ); précédent : 000168; suivant : 000170Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii).
Auteurs : Lin Wang [République populaire de Chine] ; Qiufang Liang ; Zhenbin Wang ; Junmin Xu ; Yang Liu ; Haile MaSource :
- Food chemistry [ 0308-8146 ] ; 2014.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Collagen, Fish Proteins.
- chemical , isolation & purification : Collagen, Fish Proteins.
- chemistry : Skin.
- Animals, Electrophoresis, Polyacrylamide Gel, Fishes, Hydrogen Bonding, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared.
Abstract
The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P₂.₄ (92.40%) and P₄.₀ (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P₂.₄ and P₄.₀ might be classified as type I collagen (PSC-I) and type V collagen (PSC-V), respectively. These collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperatures of PSC-V (35.92 and 122.86 °C) were significantly higher than PSC-I (32.52 and 116.01 °C) assessed by CD and DSC, which could be attributed to its higher imino acid content (23.43%) and degree of hydroxylation (52.18%). FTIR confirmed their triple helical structure, and indicated more intermolecular crosslinks in PSC-I and more hydrogen bond in PSC-V. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen.
DOI: 10.1016/j.foodchem.2013.10.074
PubMed: 24262576
Affiliations:
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xml:lang="en"><term>Animals</term><term>Collagen (chemistry)</term><term>Collagen (isolation & purification)</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Fish Proteins (chemistry)</term><term>Fish Proteins (isolation & purification)</term><term>Fishes</term><term>Hydrogen Bonding</term><term>Protein Structure, Secondary</term><term>Skin (chemistry)</term><term>Spectroscopy, Fourier Transform Infrared</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Collagen</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Collagen</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Skin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Fishes</term><term>Hydrogen Bonding</term><term>Protein Structure, Secondary</term><term>Spectroscopy, Fourier Transform Infrared</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P₂.₄ (92.40%) and P₄.₀ (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P₂.₄ and P₄.₀ might be classified as type I collagen (PSC-I) and type V collagen (PSC-V), respectively. These collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperatures of PSC-V (35.92 and 122.86 °C) were significantly higher than PSC-I (32.52 and 116.01 °C) assessed by CD and DSC, which could be attributed to its higher imino acid content (23.43%) and degree of hydroxylation (52.18%). FTIR confirmed their triple helical structure, and indicated more intermolecular crosslinks in PSC-I and more hydrogen bond in PSC-V. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Liang, Qiufang" sort="Liang, Qiufang" uniqKey="Liang Q" first="Qiufang" last="Liang">Qiufang Liang</name><name sortKey="Liu, Yang" sort="Liu, Yang" uniqKey="Liu Y" first="Yang" last="Liu">Yang Liu</name><name sortKey="Ma, Haile" sort="Ma, Haile" uniqKey="Ma H" first="Haile" last="Ma">Haile Ma</name><name sortKey="Wang, Zhenbin" sort="Wang, Zhenbin" uniqKey="Wang Z" first="Zhenbin" last="Wang">Zhenbin Wang</name><name sortKey="Xu, Junmin" sort="Xu, Junmin" uniqKey="Xu J" first="Junmin" last="Xu">Junmin Xu</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Wang, Lin" sort="Wang, Lin" uniqKey="Wang L" first="Lin" last="Wang">Lin Wang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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