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http://krishi.icar.gov.in/jspui/handle/123456789/15019| Title: | Sequence Determination of an Antioxidant Peptide Obtained by Enzymatic Hydrolysis of Oyster Crassostrea madrasensis (Preston) |
| Other Titles: | Not Available |
| Authors: | Asha, K.K. Remyakumari, K.R. Ashok kumar, K. Chatterjee, N.S. Anandan, R. Suseela Mathew |
| ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
| Author's Affiliated institute: | ICAR::Central Institute of Fisheries Technology |
| Published/ Complete Date: | 2016-03-14 |
| Project Code: | Not Available |
| Keywords: | Crassostrea madrasensis Protein hydrolysate Antioxidant activity RP-HPLC Peptide sequence |
| Publisher: | Springer Netherlands |
| Citation: | Asha, K.K., Remyakumari, K.R., Ashok Kumar, K., Chatterjee, N.S., Anandan, R. and Suseela Mathew (2016) - Sequence determination of an antioxidant peptide obtained by enzymatic hydrolysis of oyster Crassostrea madrasensis (Preston), Intl J. Peptide Res. Therapeut.,22(3): 421–433 DOI 10.1007/s10989-016-9521-0 |
| Series/Report no.: | Not Available; |
| Abstract/Description: | Soft tissue from cultured farm fresh oysters (Crassostrea madrasensis) was subjected to two standard enzymatic peptide extraction procedures using pepsin and papain. The crude extracts obtained were partially purified by column chromatography and were freeze-dried. The hydrolysates obtained were compared with respect to their degree of hydrolysis (DH), antioxidant potential (AP) and total phenolic content (TPC). The hydrolysate showing better antioxidant property was further subjected to purification by high performance liquid chromatography and characterized by LC-MS/MS. Papain-digested oyster protein (OPHpap) hydrolysate showed higher DH, AP and TPC. OPHpap was further subjected to ultrafiltration and fractionated into 3 sizes namely, above 10, 3–10 and 1–3 kDa according to the molecular size. Antioxidant capacity of\3 kDa fraction OPHpap-3 evaluated by DPPH free radical scavenging assay, metal chelating activity, linoleic acid autoxidation assay showed maximum effectiveness. Of the seven fractions collected by purification of OPH-pap-3 on semi-preparative RP-HPLC, fraction 7 that showed the highest antioxidant activity was further characterized by LC-ESI-MS/MS and its sequence determined. An antioxidant peptide molecule with thirteen amino acids was identified in oyster protein hydrolysate obtained by papain digestion that may find application as a nutraceutical or may be utilized in food industry for prevention of rancidity in foods. |
| Description: | Not Available |
| ISSN: | 1573-3149 (Print) 1573-3904 (Online) |
| Type(s) of content: | Research Paper |
| Sponsors: | Not Available |
| Language: | English |
| Name of Journal: | International Journal of Peptide Research and Therapeutics |
| NAAS Rating: | 7.5 |
| Volume No.: | 22(3) |
| Page Number: | 421–433 |
| Name of the Division/Regional Station: | Not Available |
| Source, DOI or any other URL: | https://doi.org/10.1007/s10989-016-9521-0 |
| URI: | http://krishi.icar.gov.in/jspui/handle/123456789/15019 |
| Appears in Collections: | FS-CIFT-Publication |
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