Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus.
Identifieur interne : 000566 ( Ncbi/Merge ); précédent : 000565; suivant : 000567Biochemical 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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24799243</PMID><DateCreated><Year>2014</Year><Month>05</Month><Day>06</Day></DateCreated><DateCompleted><Year>2015</Year><Month>05</Month><Day>20</Day></DateCompleted><DateRevised><Year>2014</Year><Month>05</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0308-8146</ISSN><JournalIssue CitedMedium="Internet"><Volume>160</Volume><PubDate><Year>2014</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>Food chemistry</Title><ISOAbbreviation>Food Chem</ISOAbbreviation></Journal><ArticleTitle>Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus.</ArticleTitle><Pagination><MedlinePgn>305-12</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.foodchem.2014.03.075</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0308-8146(14)00466-X</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xi</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan. Electronic address: ocean_zhangxi@yahoo.co.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ookawa</LastName><ForeName>Mika</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Yongkai</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ura</LastName><ForeName>Kazuhiro</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Adachi</LastName><ForeName>Shinji</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takagi</LastName><ForeName>Yasuaki</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate, Hokkaido 041-8611, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>03</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Food Chem</MedlineTA><NlmUniqueID>7702639</NlmUniqueID><ISSNLinking>0308-8146</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029941">Fish Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-34-5</RegistryNumber><NameOfSubstance UI="D003094">Collagen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000825" MajorTopicYN="N">Animal Structures</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003094" MajorTopicYN="N">Collagen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029941" MajorTopicYN="N">Fish Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006824" MajorTopicYN="N">Hybridization, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012867" MajorTopicYN="N">Skin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Denaturation temperature</Keyword><Keyword MajorTopicYN="N">Notochord</Keyword><Keyword MajorTopicYN="N">SEM</Keyword><Keyword MajorTopicYN="N">Type I collagen</Keyword><Keyword MajorTopicYN="N">Type II collagen</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>06</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>02</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>03</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>5</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>5</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24799243</ArticleId><ArticleId IdType="pii">S0308-8146(14)00466-X</ArticleId><ArticleId IdType="doi">10.1016/j.foodchem.2014.03.075</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Zhang, Xi" sort="Zhang, Xi" uniqKey="Zhang X" first="Xi" last="Zhang">Xi Zhang</name></noRegion><name sortKey="Adachi, Shinji" sort="Adachi, Shinji" uniqKey="Adachi S" first="Shinji" last="Adachi">Shinji Adachi</name><name sortKey="Ookawa, Mika" sort="Ookawa, Mika" uniqKey="Ookawa M" first="Mika" last="Ookawa">Mika Ookawa</name><name sortKey="Takagi, Yasuaki" sort="Takagi, Yasuaki" uniqKey="Takagi Y" first="Yasuaki" last="Takagi">Yasuaki Takagi</name><name sortKey="Tan, Yongkai" sort="Tan, Yongkai" uniqKey="Tan Y" first="Yongkai" last="Tan">Yongkai Tan</name><name sortKey="Ura, Kazuhiro" sort="Ura, Kazuhiro" uniqKey="Ura K" first="Kazuhiro" last="Ura">Kazuhiro Ura</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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