2000Korean Journal of Fisheries and Aquatic SciencesRequires access

Purification and Characterization of Antioxidative Peptides from Enzymatic Hydrolysate of Cod Teiset Protein

Se‐Kwon Kim, Choi Yong-Ri, Pyo‐Jam Park, Jeoung-Ho Choi, Sung-Hoon Moon

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Abstract

In order to utilize by-products which would normally be discarded in marine processing plants, cod teiset protein was hydrolyzed and antioxidative actiTity of the hydrolysate was investigated. AntioxidatiTe peptide was isolated using ultrafiltration membrane, ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, high performance liquid chromatography on an ODS column, and capillary electrophoresis chromatography. Antioxidative activities of the cod teiset hydrolysate were compared with , one of the commercial antioxidant. The hydrolysate passed through a membrane with molecular weight cut-off (MWCO) 1 kDa was shown the strongest antioxidative activity, and the activity was higher as compared with . In addition, the peptide isolated by ion-exchange chromatography, gel filtration, and HPLC, respectively, was higher as compared with , and the amino acid sequence was Ser-Asn-Pro-Glu-Trp-Ser-Trp-Asn.

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What this paper is about

In order to utilize by-products which would normally be discarded in marine processing plants, cod teiset protein was hydrolyzed and antioxidative actiTity of the hydrolysate was investigated. AntioxidatiTe peptide was isolated using ultrafiltration membrane, ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, high performance liquid chromatography on an ODS column, and capillary electrophoresis chromatography. Antioxidative activities of the cod teiset hydrolysate were compared with , one of the commercial antioxidant. The hydrolysate passed through a membrane with molecular weight cut-off (MWCO) 1 kDa was shown the strongest antioxidative activity, and the activity was higher as compared with . In addition, the peptide isolated by ion-exchange chromatography, gel filtration, and HPLC, respectively, was higher as compared with , and the amino acid sequence was Ser-Asn-Pro-Glu-Trp-Ser-Trp-Asn.

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Available abstract

In order to utilize by-products which would normally be discarded in marine processing plants, cod teiset protein was hydrolyzed and antioxidative actiTity of the hydrolysate was investigated. AntioxidatiTe peptide was isolated using ultrafiltration membrane, ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, high performance liquid chromatography on an ODS column, and capillary electrophoresis chromatography. Antioxidative activities of the cod teiset hydrolysate were compared with , one of the commercial antioxidant. The hydrolysate passed through a membrane with molecular weight cut-off (MWCO) 1 kDa was shown the strongest antioxidative activity, and the activity was higher as compared with . In addition, the peptide isolated by ion-exchange chromatography, gel filtration, and HPLC, respectively, was higher as compared with , and the amino acid sequence was Ser-Asn-Pro-Glu-Trp-Ser-Trp-Asn.

Key concepts: Hydrolysate, Sephadex, Chromatography, Chemistry, Size-exclusion chromatography, Ultrafiltration (renal), Hydrolysis, High-performance liquid chromatography

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