Identification and characterization of a novel antioxidant peptide from feather keratin hydrolysate
Objectives To improve the potential value of feather, which is a valuable protein resource, we have separated and identified antioxidant peptide(s) from feather hydrolysate. Results Feather hydrolysate was prepared by fermentation with Bacillus subtilis S1–4. Antioxidative peptides were separated by sequential acid precipitation, cation exchange, and reversed-phase fast performance liquid chromatography. Finally, a peptide with antioxidative activity was identified as Ser-Asn-Leu-Cys-Arg-Pro-Cys-Gly by MALDI time-of-flight (TOF)/TOF analysis, and determined to represent a portion of feather keratin near its N-terminal. A synthesized peptide with the same sequence was used to characterize its antioxidative properties, including scavenging free radicals, reducing power, and $ Fe^{2+} $ chelation. In terms of the peptide’s amino acid composition, the antioxidative activity might be mainly attributed to Cys and other amino acid residues. Conclusion Feather keratin is a good source for the quantitative preparation of antioxidative peptides..
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2015 |
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Erschienen: |
2015 |
Enthalten in: |
Zur Gesamtaufnahme - volume:38 |
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Enthalten in: |
Biotechnology letters - 38(2015), 4 vom: 19. Dez., Seite 643-649 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Wan, Min-Yuan [VerfasserIn] |
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Links: |
Volltext [lizenzpflichtig] |
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BKL: | |
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Themen: |
Anmerkungen: |
© Springer Science+Business Media Dordrecht 2015 |
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doi: |
10.1007/s10529-015-2016-9 |
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funding: |
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PPN (Katalog-ID): |
OLC2111680710 |
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100 | 1 | |a Wan, Min-Yuan |e verfasserin |4 aut | |
245 | 1 | 0 | |a Identification and characterization of a novel antioxidant peptide from feather keratin hydrolysate |
264 | 1 | |c 2015 | |
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520 | |a Objectives To improve the potential value of feather, which is a valuable protein resource, we have separated and identified antioxidant peptide(s) from feather hydrolysate. Results Feather hydrolysate was prepared by fermentation with Bacillus subtilis S1–4. Antioxidative peptides were separated by sequential acid precipitation, cation exchange, and reversed-phase fast performance liquid chromatography. Finally, a peptide with antioxidative activity was identified as Ser-Asn-Leu-Cys-Arg-Pro-Cys-Gly by MALDI time-of-flight (TOF)/TOF analysis, and determined to represent a portion of feather keratin near its N-terminal. A synthesized peptide with the same sequence was used to characterize its antioxidative properties, including scavenging free radicals, reducing power, and $ Fe^{2+} $ chelation. In terms of the peptide’s amino acid composition, the antioxidative activity might be mainly attributed to Cys and other amino acid residues. Conclusion Feather keratin is a good source for the quantitative preparation of antioxidative peptides. | ||
650 | 4 | |a Antioxidative peptide | |
650 | 4 | |a Degradation | |
650 | 4 | |a Feather | |
650 | 4 | |a Hydrolysate | |
650 | 4 | |a Keratin | |
700 | 1 | |a Dong, Ge |4 aut | |
700 | 1 | |a Yang, Bin-Qing |4 aut | |
700 | 1 | |a Feng, Hong |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Biotechnology letters |d Springer Netherlands, 1979 |g 38(2015), 4 vom: 19. Dez., Seite 643-649 |h Online-Ressource |w (DE-627)312808356 |w (DE-600)2012203-2 |w (DE-576)107586002 |x 1573-6776 |7 nnns |
773 | 1 | 8 | |g volume:38 |g year:2015 |g number:4 |g day:19 |g month:12 |g pages:643-649 |
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