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Production of an antioxidative peptide from hairy basil seed waste by a recombinant Escherichia coli
Objective To circumvent the time-consuming and costly problems associated with natural product extraction, a potential antioxidative peptide selected from hairy basil waste after oil extraction was produced by recombinant DNA technology. Results Because the target peptide is short, the recombinant p...
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Published in: | Biotechnology letters 2016-07, Vol.38 (7), p.1195-1201 |
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container_title | Biotechnology letters |
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creator | Kongcharoen, Apapun Poolex, Wannapun Wichai, Thanaporn Boonsombat, Ruethairat |
description | Objective
To circumvent the time-consuming and costly problems associated with natural product extraction, a potential antioxidative peptide selected from hairy basil waste after oil extraction was produced by recombinant DNA technology.
Results
Because the target peptide is short, the recombinant peptide containing seven repeats of the target sequence, QTFQYSRGWTN, and the DNA fragment coding this sequence was cloned into the pQE-30 Xa expression vector and transformed into
Escherichia coli
. After 6 h of recombinant peptide expression in
E. coli
, the target peptide was purified by Ni
2+
affinity chromatography and gel extraction. The expected 15 kDa recombinant target peptide construct was verified by modified dot blot analysis. Compared with the chemically synthesized peptide, the recombinant peptide revealed significantly higher antioxidant activities (
p
|
doi_str_mv | 10.1007/s10529-016-2096-1 |
format | article |
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To circumvent the time-consuming and costly problems associated with natural product extraction, a potential antioxidative peptide selected from hairy basil waste after oil extraction was produced by recombinant DNA technology.
Results
Because the target peptide is short, the recombinant peptide containing seven repeats of the target sequence, QTFQYSRGWTN, and the DNA fragment coding this sequence was cloned into the pQE-30 Xa expression vector and transformed into
Escherichia coli
. After 6 h of recombinant peptide expression in
E. coli
, the target peptide was purified by Ni
2+
affinity chromatography and gel extraction. The expected 15 kDa recombinant target peptide construct was verified by modified dot blot analysis. Compared with the chemically synthesized peptide, the recombinant peptide revealed significantly higher antioxidant activities (
p
< 0.05), as determined by DPPH and ABTS radical scavenging assays, and in vitro DNA damage induced by hydroxyl radicals.
Conclusion
This approach provides an alternative to produce an antioxidative peptide that provides a potential scaffold for the further development of antioxidative peptides for industrial applications.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-016-2096-1</identifier><identifier>PMID: 27094844</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Antioxidants ; Antioxidants - metabolism ; Applied Microbiology ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Deoxyribonucleic acid ; E coli ; Escherichia coli ; Escherichia coli - metabolism ; Extraction ; Flowers & plants ; Gene sequencing ; Hydroxyl radicals ; Life Sciences ; Microbiology ; Ocimum basilicum ; Ocimum basilicum - chemistry ; Ocimum basilicum - metabolism ; Original Research Paper ; Peptides ; Peptides - metabolism ; Recombinant ; Seeds - chemistry ; Seeds - metabolism ; Wastes</subject><ispartof>Biotechnology letters, 2016-07, Vol.38 (7), p.1195-1201</ispartof><rights>Springer Science+Business Media Dordrecht 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c545t-51472d6b024c7ca77246e0439a3d9bd5e61a48cbb826afc80b84f6c08531d4e53</citedby><cites>FETCH-LOGICAL-c545t-51472d6b024c7ca77246e0439a3d9bd5e61a48cbb826afc80b84f6c08531d4e53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27094844$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kongcharoen, Apapun</creatorcontrib><creatorcontrib>Poolex, Wannapun</creatorcontrib><creatorcontrib>Wichai, Thanaporn</creatorcontrib><creatorcontrib>Boonsombat, Ruethairat</creatorcontrib><title>Production of an antioxidative peptide from hairy basil seed waste by a recombinant Escherichia coli</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>Objective
To circumvent the time-consuming and costly problems associated with natural product extraction, a potential antioxidative peptide selected from hairy basil waste after oil extraction was produced by recombinant DNA technology.
Results
Because the target peptide is short, the recombinant peptide containing seven repeats of the target sequence, QTFQYSRGWTN, and the DNA fragment coding this sequence was cloned into the pQE-30 Xa expression vector and transformed into
Escherichia coli
. After 6 h of recombinant peptide expression in
E. coli
, the target peptide was purified by Ni
2+
affinity chromatography and gel extraction. The expected 15 kDa recombinant target peptide construct was verified by modified dot blot analysis. Compared with the chemically synthesized peptide, the recombinant peptide revealed significantly higher antioxidant activities (
p
< 0.05), as determined by DPPH and ABTS radical scavenging assays, and in vitro DNA damage induced by hydroxyl radicals.
Conclusion
This approach provides an alternative to produce an antioxidative peptide that provides a potential scaffold for the further development of antioxidative peptides for industrial applications.</description><subject>Antioxidants</subject><subject>Antioxidants - metabolism</subject><subject>Applied Microbiology</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Deoxyribonucleic acid</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Extraction</subject><subject>Flowers & plants</subject><subject>Gene sequencing</subject><subject>Hydroxyl radicals</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Ocimum basilicum</subject><subject>Ocimum basilicum - chemistry</subject><subject>Ocimum basilicum - metabolism</subject><subject>Original Research Paper</subject><subject>Peptides</subject><subject>Peptides - metabolism</subject><subject>Recombinant</subject><subject>Seeds - chemistry</subject><subject>Seeds - metabolism</subject><subject>Wastes</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqNkUuLFDEURoMoTjv6A9xIwI2b0pt3spRhfMCALnQd8io7Q1WlTarU_vdm7FFEEIXAJdzzfSEchB4TeE4A1ItGQFAzAJEDBSMHcgftiFBskErJu2gHhJNBcEPP0IPWrgHAKFD30RlVYLjmfIfi-1riFtZcFlxG7JZ--uVbjm7NXxI-pMOaY8JjLTPeu1yP2LuWJ9xSivira2vC_ogdrimU2eelx_FlC_tUc9hnh0OZ8kN0b3RTS49u5zn6-Oryw8Wb4erd67cXL6-GILhYB0G4olF6oDyo4JSiXCbgzDgWjY8iSeK4Dt5rKt0YNHjNRxlAC0YiT4Kdo2en3kMtn7fUVjvnFtI0uSWVrVmiqeAKhJH_gYKWVEuj_40qwwyAZKyjT_9Ar8tWl_7nH5TUQJnpFDlRoZbWahrtoebZ1aMlYG_E2pNY28XaG7GW9MyT2-bNzyn-Svw02QF6AlpfLZ9S_e3pv7Z-B1iFrHI</recordid><startdate>20160701</startdate><enddate>20160701</enddate><creator>Kongcharoen, Apapun</creator><creator>Poolex, Wannapun</creator><creator>Wichai, Thanaporn</creator><creator>Boonsombat, Ruethairat</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20160701</creationdate><title>Production of an antioxidative peptide from hairy basil seed waste by a recombinant Escherichia coli</title><author>Kongcharoen, Apapun ; Poolex, Wannapun ; Wichai, Thanaporn ; Boonsombat, Ruethairat</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c545t-51472d6b024c7ca77246e0439a3d9bd5e61a48cbb826afc80b84f6c08531d4e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Antioxidants</topic><topic>Antioxidants - metabolism</topic><topic>Applied Microbiology</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Deoxyribonucleic acid</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Extraction</topic><topic>Flowers & plants</topic><topic>Gene sequencing</topic><topic>Hydroxyl radicals</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Ocimum basilicum</topic><topic>Ocimum basilicum - chemistry</topic><topic>Ocimum basilicum - metabolism</topic><topic>Original Research Paper</topic><topic>Peptides</topic><topic>Peptides - metabolism</topic><topic>Recombinant</topic><topic>Seeds - chemistry</topic><topic>Seeds - metabolism</topic><topic>Wastes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kongcharoen, Apapun</creatorcontrib><creatorcontrib>Poolex, Wannapun</creatorcontrib><creatorcontrib>Wichai, Thanaporn</creatorcontrib><creatorcontrib>Boonsombat, Ruethairat</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Proquest Health & Medical Complete</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kongcharoen, Apapun</au><au>Poolex, Wannapun</au><au>Wichai, Thanaporn</au><au>Boonsombat, Ruethairat</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of an antioxidative peptide from hairy basil seed waste by a recombinant Escherichia coli</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2016-07-01</date><risdate>2016</risdate><volume>38</volume><issue>7</issue><spage>1195</spage><epage>1201</epage><pages>1195-1201</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>Objective
To circumvent the time-consuming and costly problems associated with natural product extraction, a potential antioxidative peptide selected from hairy basil waste after oil extraction was produced by recombinant DNA technology.
Results
Because the target peptide is short, the recombinant peptide containing seven repeats of the target sequence, QTFQYSRGWTN, and the DNA fragment coding this sequence was cloned into the pQE-30 Xa expression vector and transformed into
Escherichia coli
. After 6 h of recombinant peptide expression in
E. coli
, the target peptide was purified by Ni
2+
affinity chromatography and gel extraction. The expected 15 kDa recombinant target peptide construct was verified by modified dot blot analysis. Compared with the chemically synthesized peptide, the recombinant peptide revealed significantly higher antioxidant activities (
p
< 0.05), as determined by DPPH and ABTS radical scavenging assays, and in vitro DNA damage induced by hydroxyl radicals.
Conclusion
This approach provides an alternative to produce an antioxidative peptide that provides a potential scaffold for the further development of antioxidative peptides for industrial applications.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>27094844</pmid><doi>10.1007/s10529-016-2096-1</doi><tpages>7</tpages></addata></record> |
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ispartof | Biotechnology letters, 2016-07, Vol.38 (7), p.1195-1201 |
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language | eng |
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source | Springer Nature |
subjects | Antioxidants Antioxidants - metabolism Applied Microbiology Biochemistry Biomedical and Life Sciences Biotechnology Deoxyribonucleic acid E coli Escherichia coli Escherichia coli - metabolism Extraction Flowers & plants Gene sequencing Hydroxyl radicals Life Sciences Microbiology Ocimum basilicum Ocimum basilicum - chemistry Ocimum basilicum - metabolism Original Research Paper Peptides Peptides - metabolism Recombinant Seeds - chemistry Seeds - metabolism Wastes |
title | Production of an antioxidative peptide from hairy basil seed waste by a recombinant Escherichia coli |
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