Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii).
Identifieur interne : 000529 ( Ncbi/Merge ); précédent : 000528; suivant : 000530Preparation 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 ; Zhenbin Wang ; Junmin Xu ; Yang Liu ; Haile MaSource :
- Food chemistry [ 0308-8146 ] ; 2014.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Collagen, Fish Proteins.
- chemical , isolation & purification : Collagen, Fish Proteins.
- chemistry : Skin.
- Animals, Electrophoresis, Polyacrylamide Gel, Fishes, Hydrogen Bonding, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared.
Abstract
The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P₂.₄ (92.40%) and P₄.₀ (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P₂.₄ and P₄.₀ 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-I 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.
DOI: 10.1016/j.foodchem.2013.10.074
PubMed: 24262576
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SDS-PAGE and amino acid profile suggested that the P₂.₄ and P₄.₀ 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-I 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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24262576</PMID><DateCreated><Year>2013</Year><Month>11</Month><Day>22</Day></DateCreated><DateCompleted><Year>2014</Year><Month>06</Month><Day>27</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0308-8146</ISSN><JournalIssue CitedMedium="Internet"><Volume>148</Volume><PubDate><Year>2014</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Food chemistry</Title><ISOAbbreviation>Food Chem</ISOAbbreviation></Journal><ArticleTitle>Preparation and characterisation of type I and V collagens from the skin of Amur sturgeon (Acipenser schrenckii).</ArticleTitle><Pagination><MedlinePgn>410-4</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.foodchem.2013.10.074</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0308-8146(13)01519-7</ELocationID><Abstract><AbstractText>The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P₂.₄ (92.40%) and P₄.₀ (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P₂.₄ and P₄.₀ 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-I 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.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Lin</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, PR China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liang</LastName><ForeName>Qiufang</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Zhenbin</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Junmin</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Yang</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Haile</ForeName><Initials>H</Initials></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>2013</Year><Month>10</Month><Day>25</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="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="D000818" MajorTopicYN="N">Animals</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="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></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></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012867" MajorTopicYN="N">Skin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017550" MajorTopicYN="N">Spectroscopy, Fourier Transform Infrared</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Amur sturgeon (Acipenser schrenckii)</Keyword><Keyword MajorTopicYN="N">Characterisation</Keyword><Keyword MajorTopicYN="N">Collagen</Keyword><Keyword MajorTopicYN="N">Preparation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>07</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>10</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>10</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>11</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>6</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24262576</ArticleId><ArticleId IdType="pii">S0308-8146(13)01519-7</ArticleId><ArticleId IdType="doi">10.1016/j.foodchem.2013.10.074</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Liang, Qiufang" sort="Liang, Qiufang" uniqKey="Liang Q" first="Qiufang" last="Liang">Qiufang Liang</name><name sortKey="Liu, Yang" sort="Liu, Yang" uniqKey="Liu Y" first="Yang" last="Liu">Yang Liu</name><name sortKey="Ma, Haile" sort="Ma, Haile" uniqKey="Ma H" first="Haile" last="Ma">Haile Ma</name><name sortKey="Wang, Zhenbin" sort="Wang, Zhenbin" uniqKey="Wang Z" first="Zhenbin" last="Wang">Zhenbin Wang</name><name sortKey="Xu, Junmin" sort="Xu, Junmin" uniqKey="Xu J" first="Junmin" last="Xu">Junmin Xu</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Wang, Lin" sort="Wang, Lin" uniqKey="Wang L" first="Lin" last="Wang">Lin Wang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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