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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
Main Authors: Kongcharoen, Apapun, Poolex, Wannapun, Wichai, Thanaporn, Boonsombat, Ruethairat
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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
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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  &lt; 0.05), as determined by DPPH and ABTS radical scavenging assays, and in vitro DNA damage induced by hydroxyl radicals. 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ispartof Biotechnology letters, 2016-07, Vol.38 (7), p.1195-1201
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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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