Production of a bioactive peptide (IIAEK) in Escherichia coli using soybean proglycinin A1ab1b as a carrier.
Identifieur interne : 001E85 ( PubMed/Checkpoint ); précédent : 001E84; suivant : 001E86Production of a bioactive peptide (IIAEK) in Escherichia coli using soybean proglycinin A1ab1b as a carrier.
Auteurs : Krisna Prak [Japon] ; Shigeru UtsumiSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2009.
Descripteurs français
- KwdFr :
- Anticholestérolémiants, Clonage moléculaire, Escherichia coli (génétique), Expression des gènes, Oligopeptides (biosynthèse), Oligopeptides (génétique), Oligopeptides (isolement et purification), Plasmides (génétique), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de soja (génétique), Protéines recombinantes (biosynthèse), Trypsine (métabolisme), Vecteurs génétiques (génétique).
- MESH :
- biosynthèse : Oligopeptides, Protéines recombinantes.
- génétique : Escherichia coli, Oligopeptides, Plasmides, Protéines de fusion recombinantes, Protéines de soja, Vecteurs génétiques.
- isolement et purification : Oligopeptides.
- métabolisme : Protéines de fusion recombinantes, Trypsine.
- Anticholestérolémiants, Clonage moléculaire, Expression des gènes.
English descriptors
- KwdEn :
- Anticholesteremic Agents, Cloning, Molecular, Escherichia coli (genetics), Gene Expression, Genetic Vectors (genetics), Oligopeptides (biosynthesis), Oligopeptides (genetics), Oligopeptides (isolation & purification), Plasmids (genetics), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Recombinant Proteins (biosynthesis), Soybean Proteins (genetics), Trypsin (metabolism).
- MESH :
- chemical , biosynthesis : Oligopeptides, Recombinant Proteins.
- chemical , genetics : Oligopeptides, Recombinant Fusion Proteins, Soybean Proteins.
- chemical , isolation & purification : Oligopeptides.
- chemical , metabolism : Recombinant Fusion Proteins, Trypsin.
- chemical : Anticholesteremic Agents.
- genetics : Escherichia coli, Genetic Vectors, Plasmids.
- Cloning, Molecular, Gene Expression.
Abstract
To produce large amounts of a peptide of fewer than 10 amino acid residues, construction of a gene encoding multimers of the small peptide is necessary. For this study a method was developed to facilitate the gene construction of high multimers of a small peptide with one step of cloning. A hypocholesterolemic peptide, IIAEK, from cow's milk beta-lactoglobulin was used as a model peptide for the construction of a gene encoding multimers of IIAEK and for the production of the peptide. Two systems for direct expression of 28-mers of IIAEK sequences (28IIAEK) and expression of 34 IIAEK sequences (4 IIAEK sequences in each of the disordered regions I, II, and III and 14 and 8 IIAEK sequences in disordered regions IV and V, respectively) in a mutant of soybean proglycinin A1aB1b lacking 31 residues in disordered region IV [A1aB1b(Delta31)-34IIAEK] were used. The protein produced from both systems formed inclusion bodies. The expression level of A1aB1b(Delta31)-34IIAEK was 29.9% of the total cell proteins and that of the 28IIAEK was 2.0%. The insoluble A1aB1b(Delta31)-34IIAEK was digested by trypsin without any help from urea or chemicals, and the produced IIAEK was purified using an octadecyl silica column. The yield of IIAEK was 58.6%. The results showed that A1aB1b as a carrier of multiple peptides and use of an Escherichia coli expression system are suitable for production of bioactive peptide.
DOI: 10.1021/jf8034258
PubMed: 19298043
Affiliations:
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scheme="KwdEn" xml:lang="en"><term>Anticholesteremic Agents</term><term>Cloning, Molecular</term><term>Escherichia coli (genetics)</term><term>Gene Expression</term><term>Genetic Vectors (genetics)</term><term>Oligopeptides (biosynthesis)</term><term>Oligopeptides (genetics)</term><term>Oligopeptides (isolation & purification)</term><term>Plasmids (genetics)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Recombinant Proteins (biosynthesis)</term><term>Soybean Proteins (genetics)</term><term>Trypsin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticholestérolémiants</term><term>Clonage moléculaire</term><term>Escherichia coli (génétique)</term><term>Expression des gènes</term><term>Oligopeptides (biosynthèse)</term><term>Oligopeptides (génétique)</term><term>Oligopeptides (isolement et purification)</term><term>Plasmides (génétique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines de soja (génétique)</term><term>Protéines recombinantes (biosynthèse)</term><term>Trypsine (métabolisme)</term><term>Vecteurs génétiques (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Oligopeptides</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oligopeptides</term><term>Recombinant Fusion Proteins</term><term>Soybean Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Fusion Proteins</term><term>Trypsin</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Anticholesteremic Agents</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Oligopeptides</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Genetic Vectors</term><term>Plasmids</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Oligopeptides</term><term>Plasmides</term><term>Protéines de fusion recombinantes</term><term>Protéines de soja</term><term>Vecteurs génétiques</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de fusion recombinantes</term><term>Trypsine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Gene Expression</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anticholestérolémiants</term><term>Clonage moléculaire</term><term>Expression des gènes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To produce large amounts of a peptide of fewer than 10 amino acid residues, construction of a gene encoding multimers of the small peptide is necessary. For this study a method was developed to facilitate the gene construction of high multimers of a small peptide with one step of cloning. A hypocholesterolemic peptide, IIAEK, from cow's milk beta-lactoglobulin was used as a model peptide for the construction of a gene encoding multimers of IIAEK and for the production of the peptide. Two systems for direct expression of 28-mers of IIAEK sequences (28IIAEK) and expression of 34 IIAEK sequences (4 IIAEK sequences in each of the disordered regions I, II, and III and 14 and 8 IIAEK sequences in disordered regions IV and V, respectively) in a mutant of soybean proglycinin A1aB1b lacking 31 residues in disordered region IV [A1aB1b(Delta31)-34IIAEK] were used. The protein produced from both systems formed inclusion bodies. The expression level of A1aB1b(Delta31)-34IIAEK was 29.9% of the total cell proteins and that of the 28IIAEK was 2.0%. The insoluble A1aB1b(Delta31)-34IIAEK was digested by trypsin without any help from urea or chemicals, and the produced IIAEK was purified using an octadecyl silica column. The yield of IIAEK was 58.6%. The results showed that A1aB1b as a carrier of multiple peptides and use of an Escherichia coli expression system are suitable for production of bioactive peptide.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19298043</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>30</Day></DateCompleted><DateRevised><Year>2009</Year><Month>05</Month><Day>06</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1520-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>57</Volume><Issue>9</Issue><PubDate><Year>2009</Year><Month>May</Month><Day>13</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J. Agric. Food Chem.</ISOAbbreviation></Journal><ArticleTitle>Production of a bioactive peptide (IIAEK) in Escherichia coli using soybean proglycinin A1ab1b as a carrier.</ArticleTitle><Pagination><MedlinePgn>3792-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jf8034258</ELocationID><Abstract><AbstractText>To produce large amounts of a peptide of fewer than 10 amino acid residues, construction of a gene encoding multimers of the small peptide is necessary. For this study a method was developed to facilitate the gene construction of high multimers of a small peptide with one step of cloning. A hypocholesterolemic peptide, IIAEK, from cow's milk beta-lactoglobulin was used as a model peptide for the construction of a gene encoding multimers of IIAEK and for the production of the peptide. Two systems for direct expression of 28-mers of IIAEK sequences (28IIAEK) and expression of 34 IIAEK sequences (4 IIAEK sequences in each of the disordered regions I, II, and III and 14 and 8 IIAEK sequences in disordered regions IV and V, respectively) in a mutant of soybean proglycinin A1aB1b lacking 31 residues in disordered region IV [A1aB1b(Delta31)-34IIAEK] were used. The protein produced from both systems formed inclusion bodies. The expression level of A1aB1b(Delta31)-34IIAEK was 29.9% of the total cell proteins and that of the 28IIAEK was 2.0%. The insoluble A1aB1b(Delta31)-34IIAEK was digested by trypsin without any help from urea or chemicals, and the produced IIAEK was purified using an octadecyl silica column. The yield of IIAEK was 58.6%. The results showed that A1aB1b as a carrier of multiple peptides and use of an Escherichia coli expression system are suitable for production of bioactive peptide.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Prak</LastName><ForeName>Krisna</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Utsumi</LastName><ForeName>Shigeru</ForeName><Initials>S</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Agric Food 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Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>3</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>3</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>7</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19298043</ArticleId><ArticleId IdType="doi">10.1021/jf8034258</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région du Kansai</li></region><settlement><li>Kyoto</li></settlement><orgName><li>Université de Kyoto</li></orgName></list><tree><noCountry><name sortKey="Utsumi, Shigeru" sort="Utsumi, Shigeru" uniqKey="Utsumi S" first="Shigeru" last="Utsumi">Shigeru Utsumi</name></noCountry><country name="Japon"><region name="Région du Kansai"><name sortKey="Prak, Krisna" sort="Prak, Krisna" uniqKey="Prak K" first="Krisna" last="Prak">Krisna Prak</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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