Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus.
Identifieur interne : 000219 ( Main/Merge ); précédent : 000218; suivant : 000220Biochemical 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.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Amino Acids, Collagen, Fish Proteins.
- chemistry : Animal Structures, Skin.
- genetics : Fishes.
- chemical , isolation & purification : Collagen, Fish Proteins.
- Animals, Circular Dichroism, Hybridization, Genetic, Swine, 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.
DOI: 10.1016/j.foodchem.2014.03.075
PubMed: 24799243
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Electronic address: ocean_zhangxi@yahoo.co.jp.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611</wicri:regionArea><wicri:noRegion>Hokkaido 041-8611</wicri:noRegion></affiliation></author><author><name sortKey="Ookawa, Mika" sort="Ookawa, Mika" uniqKey="Ookawa M" first="Mika" last="Ookawa">Mika Ookawa</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611</wicri:regionArea><wicri:noRegion>Hokkaido 041-8611</wicri:noRegion></affiliation></author><author><name sortKey="Tan, Yongkai" sort="Tan, Yongkai" uniqKey="Tan Y" first="Yongkai" last="Tan">Yongkai Tan</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611</wicri:regionArea><wicri:noRegion>Hokkaido 041-8611</wicri:noRegion></affiliation></author><author><name sortKey="Ura, Kazuhiro" sort="Ura, Kazuhiro" uniqKey="Ura K" first="Kazuhiro" last="Ura">Kazuhiro Ura</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611</wicri:regionArea><wicri:noRegion>Hokkaido 041-8611</wicri:noRegion></affiliation></author><author><name sortKey="Adachi, Shinji" sort="Adachi, Shinji" uniqKey="Adachi S" first="Shinji" last="Adachi">Shinji Adachi</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611</wicri:regionArea><wicri:noRegion>Hokkaido 041-8611</wicri:noRegion></affiliation></author><author><name sortKey="Takagi, Yasuaki" sort="Takagi, Yasuaki" uniqKey="Takagi Y" first="Yasuaki" last="Takagi">Yasuaki Takagi</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611</wicri:regionArea><wicri:noRegion>Hokkaido 041-8611</wicri:noRegion></affiliation></author></analytic><series><title level="j">Food chemistry</title><idno type="ISSN">0308-8146</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (chemistry)</term><term>Animal Structures (chemistry)</term><term>Animals</term><term>Circular Dichroism</term><term>Collagen (chemistry)</term><term>Collagen (isolation & purification)</term><term>Fish Proteins (chemistry)</term><term>Fish Proteins (isolation & purification)</term><term>Fishes (genetics)</term><term>Hybridization, Genetic</term><term>Skin (chemistry)</term><term>Swine</term><term>Temperature</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Collagen</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Animal Structures</term><term>Skin</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Collagen</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Circular Dichroism</term><term>Hybridization, Genetic</term><term>Swine</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><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></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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