Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)
Identifieur interne : 000019 ( PascalFrancis/Corpus ); précédent : 000018; suivant : 000020Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)
Auteurs : LIN WANG ; QIUFANG LIANG ; ZHENBIN WANG ; JUNMIN XU ; YANG LIU ; HAILE MASource :
- Food chemistry [ 0308-8146 ] ; 2014.
Descripteurs français
English descriptors
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.
Notice en format standard (ISO 2709)
Pour connaître la documentation sur le format Inist Standard.
| pA |
|
|---|
Format Inist (serveur)
| NO : | PASCAL 14-0116013 INIST |
|---|---|
| ET : | Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii) |
| AU : | LIN WANG; QIUFANG LIANG; ZHENBIN WANG; JUNMIN XU; YANG LIU; HAILE MA |
| AF : | School of Food and Biological Engineering, Jiangsu University/Zhenjiang 212013/Chine (1 aut., 2 aut., 3 aut., 6 aut.); Zhenjiang Kehua Aquaculture Development Company Limited/Zhenjiang 212134/Chine (4 aut.); Zhenjiang Entry-Exit Inspection and Quarantine Burea/Zhenjiang 212008/Chine (5 aut.) |
| DT : | Publication en série; Niveau analytique |
| SO : | Food chemistry; ISSN 0308-8146; Coden FOCHDJ; Royaume-Uni; Da. 2014; Vol. 148; Pp. 410-414; Bibl. 3/4 p. |
| LA : | Anglais |
| EA : | 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. |
| CC : | 002B03H |
| FD : | Collagène; Peau |
| ED : | Collagen; Skin |
| SD : | Colágeno; Piel |
| LO : | INIST-17810.354000506178600590 |
| ID : | 14-0116013 |
Links to Exploration step
Pascal:14-0116013Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en" level="a">Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)</title><author><name sortKey="Lin Wang" sort="Lin Wang" uniqKey="Lin Wang" last="Lin Wang">LIN WANG</name><affiliation><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></affiliation></author><author><name sortKey="Qiufang Liang" sort="Qiufang Liang" uniqKey="Qiufang Liang" last="Qiufang Liang">QIUFANG LIANG</name><affiliation><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></affiliation></author><author><name sortKey="Zhenbin Wang" sort="Zhenbin Wang" uniqKey="Zhenbin Wang" last="Zhenbin Wang">ZHENBIN WANG</name><affiliation><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></affiliation></author><author><name sortKey="Junmin Xu" sort="Junmin Xu" uniqKey="Junmin Xu" last="Junmin Xu">JUNMIN XU</name><affiliation><inist:fA14 i1="02"><s1>Zhenjiang Kehua Aquaculture Development Company Limited</s1><s2>Zhenjiang 212134</s2><s3>CHN</s3><sZ>4 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Yang Liu" sort="Yang Liu" uniqKey="Yang Liu" last="Yang Liu">YANG LIU</name><affiliation><inist:fA14 i1="03"><s1>Zhenjiang Entry-Exit Inspection and Quarantine Burea</s1><s2>Zhenjiang 212008</s2><s3>CHN</s3><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Haile Ma" sort="Haile Ma" uniqKey="Haile Ma" last="Haile Ma">HAILE MA</name><affiliation><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></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">INIST</idno><idno type="inist">14-0116013</idno><date when="2014">2014</date><idno type="stanalyst">PASCAL 14-0116013 INIST</idno><idno type="RBID">Pascal:14-0116013</idno><idno type="wicri:Area/PascalFrancis/Corpus">000019</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)</title><author><name sortKey="Lin Wang" sort="Lin Wang" uniqKey="Lin Wang" last="Lin Wang">LIN WANG</name><affiliation><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></affiliation></author><author><name sortKey="Qiufang Liang" sort="Qiufang Liang" uniqKey="Qiufang Liang" last="Qiufang Liang">QIUFANG LIANG</name><affiliation><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></affiliation></author><author><name sortKey="Zhenbin Wang" sort="Zhenbin Wang" uniqKey="Zhenbin Wang" last="Zhenbin Wang">ZHENBIN WANG</name><affiliation><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></affiliation></author><author><name sortKey="Junmin Xu" sort="Junmin Xu" uniqKey="Junmin Xu" last="Junmin Xu">JUNMIN XU</name><affiliation><inist:fA14 i1="02"><s1>Zhenjiang Kehua Aquaculture Development Company Limited</s1><s2>Zhenjiang 212134</s2><s3>CHN</s3><sZ>4 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Yang Liu" sort="Yang Liu" uniqKey="Yang Liu" last="Yang Liu">YANG LIU</name><affiliation><inist:fA14 i1="03"><s1>Zhenjiang Entry-Exit Inspection and Quarantine Burea</s1><s2>Zhenjiang 212008</s2><s3>CHN</s3><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Haile Ma" sort="Haile Ma" uniqKey="Haile Ma" last="Haile Ma">HAILE MA</name><affiliation><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></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. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen.</s0></fC01><fC02 i1="01" i2="X"><s0>002B03H</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Collagène</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Collagen</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Colágeno</s0><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Peau</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Skin</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Piel</s0><s5>02</s5></fC03><fN21><s1>153</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard><server><NO>PASCAL 14-0116013 INIST</NO><ET>Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)</ET><AU>LIN WANG; QIUFANG LIANG; ZHENBIN WANG; JUNMIN XU; YANG LIU; HAILE MA</AU><AF>School of Food and Biological Engineering, Jiangsu University/Zhenjiang 212013/Chine (1 aut., 2 aut., 3 aut., 6 aut.); Zhenjiang Kehua Aquaculture Development Company Limited/Zhenjiang 212134/Chine (4 aut.); Zhenjiang Entry-Exit Inspection and Quarantine Burea/Zhenjiang 212008/Chine (5 aut.)</AF><DT>Publication en série; Niveau analytique</DT><SO>Food chemistry; ISSN 0308-8146; Coden FOCHDJ; Royaume-Uni; Da. 2014; Vol. 148; Pp. 410-414; Bibl. 3/4 p.</SO><LA>Anglais</LA><EA>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.</EA><CC>002B03H</CC><FD>Collagène; Peau</FD><ED>Collagen; Skin</ED><SD>Colágeno; Piel</SD><LO>INIST-17810.354000506178600590</LO><ID>14-0116013</ID></server></inist></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Eau/explor/EsturgeonV1/Data/PascalFrancis/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000019 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PascalFrancis/Corpus/biblio.hfd -nk 000019 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Eau
|area= EsturgeonV1
|flux= PascalFrancis
|étape= Corpus
|type= RBID
|clé= Pascal:14-0116013
|texte= Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii)
}}
| This area was generated with Dilib version V0.6.27. |  |