Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis
Actinopyga lecanora, commonly known as sea cucumber, is a rich protein source. This marine protein source was hydrolyzed using six proteases to generate anti-inflammatory hydrolysates and bioactive peptides. Bromelain hydrolysates after 1 h hydrolysis exhibited the highest nitric oxide (NO) inhibito...
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| Format: | Article |
| Language: | English |
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Taylor & Francis
2016
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| Online Access: | http://psasir.upm.edu.my/id/eprint/53702/ http://psasir.upm.edu.my/id/eprint/53702/1/Purification%20and%20characterization%20of%20nitric%20oxide%20inhibitory%20peptides%20from%20Actinopyga%20lecanora%20through%20enzymatic%20hydrolysis.pdf |
| _version_ | 1848852353646592000 |
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| author | Ghanbari, Raheleh Ebrahimpour, Afshin Zarei, Mohammad Ismail, Amin Abdul Hamid, Azizah Saari, Nazamid |
| author_facet | Ghanbari, Raheleh Ebrahimpour, Afshin Zarei, Mohammad Ismail, Amin Abdul Hamid, Azizah Saari, Nazamid |
| author_sort | Ghanbari, Raheleh |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Actinopyga lecanora, commonly known as sea cucumber, is a rich protein source. This marine protein source was hydrolyzed using six proteases to generate anti-inflammatory hydrolysates and bioactive peptides. Bromelain hydrolysates after 1 h hydrolysis exhibited the highest nitric oxide (NO) inhibitory activity reflecting anti-inflammatory activity. A sequence of two fractionation methods was employed to fractionate the peptides based on their hydrophobicity using a semi-preparative RP-HPLC and isoelectric points using isoelectric focusing technique. Based on these fractionation methods, basic peptides with relatively higher hydrophobicity provided higher NO-inhibitory activity than did acidic peptides. Furthermore, using Q-TOF mass spectrometry; 12 peptide sequences were successfully identified. The inhibitory effect of the purified peptides from A. lecanora on NO production by lipopolysaccharide (LPS)-stimulated RAW 264.7 cells was investigated. The three identified bioactive peptides, namely LREMLSTMCTARGA, AVGPAGPRG and VAPAWGPWPKG, exhibited the highest NO-inhibitory activity with values of 76.3, 66.6 and 69.9%, respectively. These results revealed that A. lecanora could be used as an economical protein source for the production of high-value bioactive peptides with potent anti-inflammatory activity using RAW 264.7 cell lines as model. These peptides may be useful ingredients in food and pharmaceutical applications. |
| first_indexed | 2025-11-15T10:36:44Z |
| format | Article |
| id | upm-53702 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T10:36:44Z |
| publishDate | 2016 |
| publisher | Taylor & Francis |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-537022018-01-09T08:24:18Z http://psasir.upm.edu.my/id/eprint/53702/ Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis Ghanbari, Raheleh Ebrahimpour, Afshin Zarei, Mohammad Ismail, Amin Abdul Hamid, Azizah Saari, Nazamid Actinopyga lecanora, commonly known as sea cucumber, is a rich protein source. This marine protein source was hydrolyzed using six proteases to generate anti-inflammatory hydrolysates and bioactive peptides. Bromelain hydrolysates after 1 h hydrolysis exhibited the highest nitric oxide (NO) inhibitory activity reflecting anti-inflammatory activity. A sequence of two fractionation methods was employed to fractionate the peptides based on their hydrophobicity using a semi-preparative RP-HPLC and isoelectric points using isoelectric focusing technique. Based on these fractionation methods, basic peptides with relatively higher hydrophobicity provided higher NO-inhibitory activity than did acidic peptides. Furthermore, using Q-TOF mass spectrometry; 12 peptide sequences were successfully identified. The inhibitory effect of the purified peptides from A. lecanora on NO production by lipopolysaccharide (LPS)-stimulated RAW 264.7 cells was investigated. The three identified bioactive peptides, namely LREMLSTMCTARGA, AVGPAGPRG and VAPAWGPWPKG, exhibited the highest NO-inhibitory activity with values of 76.3, 66.6 and 69.9%, respectively. These results revealed that A. lecanora could be used as an economical protein source for the production of high-value bioactive peptides with potent anti-inflammatory activity using RAW 264.7 cell lines as model. These peptides may be useful ingredients in food and pharmaceutical applications. Taylor & Francis 2016 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/53702/1/Purification%20and%20characterization%20of%20nitric%20oxide%20inhibitory%20peptides%20from%20Actinopyga%20lecanora%20through%20enzymatic%20hydrolysis.pdf Ghanbari, Raheleh and Ebrahimpour, Afshin and Zarei, Mohammad and Ismail, Amin and Abdul Hamid, Azizah and Saari, Nazamid (2016) Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis. Food Biotechnology, 30 (4). pp. 263-277. ISSN 0890-5436; ESSN: 1532-4249 http://www.tandfonline.com/doi/abs/10.1080/08905436.2016.1234391?journalCode=lfbt20 10.1080/08905436.2016.1234391 |
| spellingShingle | Ghanbari, Raheleh Ebrahimpour, Afshin Zarei, Mohammad Ismail, Amin Abdul Hamid, Azizah Saari, Nazamid Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis |
| title | Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis |
| title_full | Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis |
| title_fullStr | Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis |
| title_full_unstemmed | Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis |
| title_short | Purification and characterization of nitric oxide inhibitory peptides from Actinopyga lecanora through enzymatic hydrolysis |
| title_sort | purification and characterization of nitric oxide inhibitory peptides from actinopyga lecanora through enzymatic hydrolysis |
| url | http://psasir.upm.edu.my/id/eprint/53702/ http://psasir.upm.edu.my/id/eprint/53702/ http://psasir.upm.edu.my/id/eprint/53702/ http://psasir.upm.edu.my/id/eprint/53702/1/Purification%20and%20characterization%20of%20nitric%20oxide%20inhibitory%20peptides%20from%20Actinopyga%20lecanora%20through%20enzymatic%20hydrolysis.pdf |