Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate
Patin sarcoplasmic protein was hydrolysed with Alcalase and papain. The antioxidant activities of sarcoplasmic protein hydrolysates (SPHs) were assessed by evaluating 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2014-07-01
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| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464614001741 |
| _version_ | 1818406161884381184 |
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| author | Leila Najafian Abdul Salam Babji |
| author_facet | Leila Najafian Abdul Salam Babji |
| author_sort | Leila Najafian |
| collection | DOAJ |
| description | Patin sarcoplasmic protein was hydrolysed with Alcalase and papain. The antioxidant activities of sarcoplasmic protein hydrolysates (SPHs) were assessed by evaluating 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical-scavenging activities, reducing power and metal chelating activity. The Alcalase hydrolysate was purified by ultrafiltration, ion exchange and gel filtration chromatography and RP-HPLC. The most potent fraction (SI 3) obtained from RP-HPLC showed DPPH radical-scavenging activity by 1.83 times higher than SPH. Three antioxidant peptide sequences, Asp-Pro-Gln-His-Pro-Val-Met-Pro-Arg, Leu-Val-Val-Asp-Ile-Pro-Ala-Ala-Leu-Gln-His-Ala and Gly-Val-Asp-Asn-Pro-Gly-His-Pro, were identified by HPLC connected to electrospray ionisation-time-of-flight mass spectrometer (ESI-TOF MS/MS). The presence of a hydrophobic amino acid (Val), hydrophilic amino acids (His and Pro) and an acidic amino acid (Asp) in the peptide sequences is believed to contribute to high antioxidant activity of SPH. Hence, antioxidative peptides from patin protein may be produced for development as natural antioxidant ingredients in functional foods. |
| first_indexed | 2024-12-14T09:07:33Z |
| format | Article |
| id | doaj.art-e5e75ace68244c1eb21fbf84ecceea01 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-14T09:07:33Z |
| publishDate | 2014-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-e5e75ace68244c1eb21fbf84ecceea012022-12-21T23:08:40ZengElsevierJournal of Functional Foods1756-46462014-07-019280289Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysateLeila Najafian0Abdul Salam Babji1Corresponding author. Tel.: +60 3 89215988; fax: +60 3 89213232.; School of Chemical Sciences and Food Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaSchool of Chemical Sciences and Food Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaPatin sarcoplasmic protein was hydrolysed with Alcalase and papain. The antioxidant activities of sarcoplasmic protein hydrolysates (SPHs) were assessed by evaluating 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical-scavenging activities, reducing power and metal chelating activity. The Alcalase hydrolysate was purified by ultrafiltration, ion exchange and gel filtration chromatography and RP-HPLC. The most potent fraction (SI 3) obtained from RP-HPLC showed DPPH radical-scavenging activity by 1.83 times higher than SPH. Three antioxidant peptide sequences, Asp-Pro-Gln-His-Pro-Val-Met-Pro-Arg, Leu-Val-Val-Asp-Ile-Pro-Ala-Ala-Leu-Gln-His-Ala and Gly-Val-Asp-Asn-Pro-Gly-His-Pro, were identified by HPLC connected to electrospray ionisation-time-of-flight mass spectrometer (ESI-TOF MS/MS). The presence of a hydrophobic amino acid (Val), hydrophilic amino acids (His and Pro) and an acidic amino acid (Asp) in the peptide sequences is believed to contribute to high antioxidant activity of SPH. Hence, antioxidative peptides from patin protein may be produced for development as natural antioxidant ingredients in functional foods.http://www.sciencedirect.com/science/article/pii/S1756464614001741Patin (Pangasius sutchi)Antioxidative peptidesEnzymatic hydrolysisSarcoplasmic fractionsAmino acid sequencing |
| spellingShingle | Leila Najafian Abdul Salam Babji Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate Journal of Functional Foods Patin (Pangasius sutchi) Antioxidative peptides Enzymatic hydrolysis Sarcoplasmic fractions Amino acid sequencing |
| title | Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate |
| title_full | Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate |
| title_fullStr | Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate |
| title_full_unstemmed | Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate |
| title_short | Production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin (Pangasius sutchi) sarcoplasmic protein hydolysate |
| title_sort | production of bioactive peptides using enzymatic hydrolysis and identification antioxidative peptides from patin pangasius sutchi sarcoplasmic protein hydolysate |
| topic | Patin (Pangasius sutchi) Antioxidative peptides Enzymatic hydrolysis Sarcoplasmic fractions Amino acid sequencing |
| url | http://www.sciencedirect.com/science/article/pii/S1756464614001741 |
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