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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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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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
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ISSN: | 0141-5492 1573-6776 |
DOI: | 10.1007/s10529-016-2096-1 |