Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)
Identifieur interne : 000002 ( PascalFrancis/Checkpoint ); précédent : 000001; suivant : 000003Preparation 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 [République populaire de Chine] ; ZHENBIN WANG [République populaire de Chine] ; JUNMIN XU [République populaire de Chine] ; YANG LIU [République populaire de Chine] ; HAILE MA [République populaire de Chine]Source :
- Food chemistry [ 0308-8146 ] ; 2014.
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Abstract
The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P2.4 (92.40%) and P40 (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P2.4 and P40 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-1 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.
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sort="Haile Ma" uniqKey="Haile Ma" last="Haile Ma">HAILE MA</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>School of Food and Biological Engineering, Jiangsu University</s1><s2>Zhenjiang 212013</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>République populaire de Chine</country><wicri:noRegion>Zhenjiang 212013</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Food chemistry</title><title level="j" type="abbreviated">Food chem.</title><idno type="ISSN">0308-8146</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Food chemistry</title><title level="j" type="abbreviated">Food chem.</title><idno type="ISSN">0308-8146</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Collagen</term><term>Skin</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Collagène</term><term>Peau</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, P<sub>2.4</sub> (92.40%) and P<sub>40</sub> (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P<sub>2.4</sub> and P<sub>40</sub> 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-1 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><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0308-8146</s0></fA01><fA02 i1="01"><s0>FOCHDJ</s0></fA02><fA03 i2="1"><s0>Food chem.</s0></fA03><fA05><s2>148</s2></fA05><fA08 i1="01" i2="1" l="ENG"><s1>Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)</s1></fA08><fA11 i1="01" i2="1"><s1>LIN WANG</s1></fA11><fA11 i1="02" i2="1"><s1>QIUFANG LIANG</s1></fA11><fA11 i1="03" i2="1"><s1>ZHENBIN WANG</s1></fA11><fA11 i1="04" i2="1"><s1>JUNMIN XU</s1></fA11><fA11 i1="05" i2="1"><s1>YANG LIU</s1></fA11><fA11 i1="06" i2="1"><s1>HAILE MA</s1></fA11><fA14 i1="01"><s1>School of Food and Biological Engineering, Jiangsu University</s1><s2>Zhenjiang 212013</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>6 aut.</sZ></fA14><fA14 i1="02"><s1>Zhenjiang Kehua Aquaculture Development Company Limited</s1><s2>Zhenjiang 212134</s2><s3>CHN</s3><sZ>4 aut.</sZ></fA14><fA14 i1="03"><s1>Zhenjiang Entry-Exit Inspection and Quarantine Burea</s1><s2>Zhenjiang 212008</s2><s3>CHN</s3><sZ>5 aut.</sZ></fA14><fA20><s1>410-414</s1></fA20><fA21><s1>2014</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>17810</s2><s5>354000506178600590</s5></fA43><fA44><s0>0000</s0><s1>© 2014 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>3/4 p.</s0></fA45><fA47 i1="01" i2="1"><s0>14-0116013</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Food chemistry</s0></fA64><fA66 i1="01"><s0>GBR</s0></fA66><fC01 i1="01" l="ENG"><s0>The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P<sub>2.4</sub> (92.40%) and P<sub>40</sub> (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P<sub>2.4</sub> and P<sub>40</sub> 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-1 and more hydrogen bond in PSC-V. 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