Production and Purification of Antioxidant Peptides from Flatfish Skin Protein Hydrolysates
Antioxidant peptides of flatfish skin protein hydrolyzed by four enzymes (Papain, Pepsin, Trypsin and Neutrase, respectively)were investigated. The Trypsin hydrotysate obtained by hydrolysis exhibited the highest 1,1- dipheny-l-2-picrylhydrazyl(DPPH) radical scavenging activity (DRSA) compared with...
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Published in | Transactions of Tianjin University Vol. 21; no. 5; pp. 433 - 439 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Tianjin
Tianjin University
01.10.2015
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Subjects | |
Online Access | Get full text |
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Summary: | Antioxidant peptides of flatfish skin protein hydrolyzed by four enzymes (Papain, Pepsin, Trypsin and Neutrase, respectively)were investigated. The Trypsin hydrotysate obtained by hydrolysis exhibited the highest 1,1- dipheny-l-2-picrylhydrazyl(DPPH) radical scavenging activity (DRSA) compared with other hydrolysates. Re- sponse surface method ology (RSM), based on Box-Behnken design, was used to study the influence of hydrolysis conditions on the DRSA. The optimal hydrolysis conditions were as follows: pH 7.38, temperature 48.2~C and en- zyme/substrate (E/S)ratio 2 840 U/g. Under these conditions, the maximum DRSA was (22.85 + 0.57)%. The experimental values agreed with the value (23.09%) predicted by the model within a 95% confidence interval. By using gel filtration chromatography and reversed-phase high performance liquid chromatography (RP-HPLC), anti- oxidant peptide (D2-P)was isolated from flatfish skin protein hydrolysates (FSPH)and could exhibit a (54.28 ± 1.37) % scavenging activity on DPPH radical at the concentration of 5 mg/mL. This is the first report of a scientific basis for the preparation of antioxidant peptides from flatfish skin. The results suggested that the antioxidant pep- tides can be exploited into functional foods or used as a novel source of nutraceuticals. |
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Bibliography: | 12-1248/T flatfish skin; enzymatic hydrolysis; antioxidant peptides; optimization; purification Antioxidant peptides of flatfish skin protein hydrolyzed by four enzymes (Papain, Pepsin, Trypsin and Neutrase, respectively)were investigated. The Trypsin hydrotysate obtained by hydrolysis exhibited the highest 1,1- dipheny-l-2-picrylhydrazyl(DPPH) radical scavenging activity (DRSA) compared with other hydrolysates. Re- sponse surface method ology (RSM), based on Box-Behnken design, was used to study the influence of hydrolysis conditions on the DRSA. The optimal hydrolysis conditions were as follows: pH 7.38, temperature 48.2~C and en- zyme/substrate (E/S)ratio 2 840 U/g. Under these conditions, the maximum DRSA was (22.85 + 0.57)%. The experimental values agreed with the value (23.09%) predicted by the model within a 95% confidence interval. By using gel filtration chromatography and reversed-phase high performance liquid chromatography (RP-HPLC), anti- oxidant peptide (D2-P)was isolated from flatfish skin protein hydrolysates (FSPH)and could exhibit a (54.28 ± 1.37) % scavenging activity on DPPH radical at the concentration of 5 mg/mL. This is the first report of a scientific basis for the preparation of antioxidant peptides from flatfish skin. The results suggested that the antioxidant pep- tides can be exploited into functional foods or used as a novel source of nutraceuticals. |
ISSN: | 1006-4982 1995-8196 |
DOI: | 10.1007/s12209-015-2432-x |