EsturgeonV1, PascalFrancis, Curation, bibRecord, 000357

Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus

Identifieur interne : 000357 ( PascalFrancis/Curation ); précédent : 000356; suivant : 000358

Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus

Auteurs : XI ZHANG [Japon] ; Mika Ookawa [Japon] ; YONGKAI TAN [Japon] ; Kazuhiro Ura [Japon] ; Shinji Adachi [Japon] ; Yasuaki Takagi [Japon]

Source :

Food chemistry [ 0308-8146 ] ; 2014.

RBID : Pascal:14-0133454

Descripteurs français

Pascal (Inist)
- Fibrille, Collagène type I, Extrait, Collagène type II, Dénaturation, Température, Microscopie électronique balayage.
Wicri :
- topic : Dénaturation.

English descriptors

KwdEn :
- Collagen type I, Collagen type II, Denaturation, Extract, Fibril, Scanning electron microscopy, Temperature.

Abstract

Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.

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A03		`1`		`@0 Food chem.`
A05				`@2 160`
A08	`01`	`1`	`ENG`	`@1 Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus`
A11	`01`	`1`		`@1 XI ZHANG`
A11	`02`	`1`		`@1 OOKAWA (Mika)`
A11	`03`	`1`		`@1 YONGKAI TAN`
A11	`04`	`1`		`@1 URA (Kazuhiro)`
A11	`05`	`1`		`@1 ADACHI (Shinji)`
A11	`06`	`1`		`@1 TAKAGI (Yasuaki)`
A14	`01`			`@1 Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho @2 Hakodate, Hokkaido 041-8611 @3 JPN @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut. @Z 6 aut.`
A20				`@1 305-312`
A21				`@1 2014`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 17810 @5 354000507537070440`
A44				`@0 0000 @1 © 2014 INIST-CNRS. All rights reserved.`
A45				`@0 3/4 p.`
A47	`01`	`1`		`@0 14-0133454`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Food chemistry`
A66	`01`			`@0 GBR`
C01	`01`		`ENG`	@0 Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.
C02	`01`	`X`		`@0 002B03H`
C03	`01`	`X`	`FRE`	`@0 Fibrille @5 01`
C03	`01`	`X`	`ENG`	`@0 Fibril @5 01`
C03	`01`	`X`	`SPA`	`@0 Fibrilla @5 01`
C03	`02`	`X`	`FRE`	`@0 Collagène type I @5 02`
C03	`02`	`X`	`ENG`	`@0 Collagen type I @5 02`
C03	`02`	`X`	`SPA`	`@0 Colágeno tipo I @5 02`
C03	`03`	`X`	`FRE`	`@0 Extrait @5 03`
C03	`03`	`X`	`ENG`	`@0 Extract @5 03`
C03	`03`	`X`	`SPA`	`@0 Extracto @5 03`
C03	`04`	`X`	`FRE`	`@0 Collagène type II @5 04`
C03	`04`	`X`	`ENG`	`@0 Collagen type II @5 04`
C03	`04`	`X`	`SPA`	`@0 Colágeno tipo II @5 04`
C03	`05`	`X`	`FRE`	`@0 Dénaturation @5 07`
C03	`05`	`X`	`ENG`	`@0 Denaturation @5 07`
C03	`05`	`X`	`SPA`	`@0 Desnaturalización @5 07`
C03	`06`	`X`	`FRE`	`@0 Température @5 08`
C03	`06`	`X`	`ENG`	`@0 Temperature @5 08`
C03	`06`	`X`	`SPA`	`@0 Temperatura @5 08`
C03	`07`	`X`	`FRE`	`@0 Microscopie électronique balayage @5 13`
C03	`07`	`X`	`ENG`	`@0 Scanning electron microscopy @5 13`
C03	`07`	`X`	`SPA`	`@0 Microscopía electrónica barrido @5 13`
N21				`@1 174`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

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Pascal:14-0133454

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus</title>
<author><name sortKey="Xi Zhang" sort="Xi Zhang" uniqKey="Xi Zhang" last="Xi Zhang">XI ZHANG</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho</s1>
<s2>Hakodate, Hokkaido 041-8611</s2>
<s3>JPN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
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<author><name sortKey="Ookawa, Mika" sort="Ookawa, Mika" uniqKey="Ookawa M" first="Mika" last="Ookawa">Mika Ookawa</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho</s1>
<s2>Hakodate, Hokkaido 041-8611</s2>
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<author><name sortKey="Yongkai Tan" sort="Yongkai Tan" uniqKey="Yongkai Tan" last="Yongkai Tan">YONGKAI TAN</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho</s1>
<s2>Hakodate, Hokkaido 041-8611</s2>
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<author><name sortKey="Ura, Kazuhiro" sort="Ura, Kazuhiro" uniqKey="Ura K" first="Kazuhiro" last="Ura">Kazuhiro Ura</name>
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<author><name sortKey="Adachi, Shinji" sort="Adachi, Shinji" uniqKey="Adachi S" first="Shinji" last="Adachi">Shinji Adachi</name>
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</author>
<author><name sortKey="Takagi, Yasuaki" sort="Takagi, Yasuaki" uniqKey="Takagi Y" first="Yasuaki" last="Takagi">Yasuaki Takagi</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho</s1>
<s2>Hakodate, Hokkaido 041-8611</s2>
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<series><title level="j" type="main">Food chemistry</title>
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</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Collagen type I</term>
<term>Collagen type II</term>
<term>Denaturation</term>
<term>Extract</term>
<term>Fibril</term>
<term>Scanning electron microscopy</term>
<term>Temperature</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Fibrille</term>
<term>Collagène type I</term>
<term>Extrait</term>
<term>Collagène type II</term>
<term>Dénaturation</term>
<term>Température</term>
<term>Microscopie électronique balayage</term>
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<front><div type="abstract" xml:lang="en">Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.</div>
</front>
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<fA08 i1="01" i2="1" l="ENG"><s1>Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus</s1>
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<fA11 i1="01" i2="1"><s1>XI ZHANG</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>OOKAWA (Mika)</s1>
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<fA11 i1="03" i2="1"><s1>YONGKAI TAN</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>URA (Kazuhiro)</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>ADACHI (Shinji)</s1>
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<fA11 i1="06" i2="1"><s1>TAKAGI (Yasuaki)</s1>
</fA11>
<fA14 i1="01"><s1>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho</s1>
<s2>Hakodate, Hokkaido 041-8611</s2>
<s3>JPN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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<fC01 i1="01" l="ENG"><s0>Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002B03H</s0>
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<fC03 i1="01" i2="X" l="FRE"><s0>Fibrille</s0>
<s5>01</s5>
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<fC03 i1="01" i2="X" l="ENG"><s0>Fibril</s0>
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<fC03 i1="02" i2="X" l="FRE"><s0>Collagène type I</s0>
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<fC03 i1="03" i2="X" l="FRE"><s0>Extrait</s0>
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<s5>03</s5>
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<fC03 i1="04" i2="X" l="FRE"><s0>Collagène type II</s0>
<s5>04</s5>
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<fC03 i1="04" i2="X" l="ENG"><s0>Collagen type II</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Colágeno tipo II</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Dénaturation</s0>
<s5>07</s5>
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<fC03 i1="05" i2="X" l="ENG"><s0>Denaturation</s0>
<s5>07</s5>
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<fC03 i1="05" i2="X" l="SPA"><s0>Desnaturalización</s0>
<s5>07</s5>
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<s5>08</s5>
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<fC03 i1="06" i2="X" l="ENG"><s0>Temperature</s0>
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Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus

Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus

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