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Antioxidant peptides isolated from the marine rotifer, Brachionus rotundiformis

Paper ID Volume ID Publish Year Pages File Format Full-Text
35482 45092 2009 5 PDF Available
Title
Antioxidant peptides isolated from the marine rotifer, Brachionus rotundiformis
Abstract

Protein derived from the rotifer Brachionus rotundiformis was hydrolyzed using different proteases (Alcalase, α-chymotrypsin, Neutrase, papain, pepsin and trypsin) for production of antioxidant peptide. Antioxidant activities of hydrolysates were evaluated using DPPH radical scavenging activity. Peptic hydrolysate exhibited the highest antioxidative activity compared to other hydrolysates. To identify antioxidant peptides, peptic hydrolysate was purified using consecutive chromatographic methods, and antioxidant peptides were identified to be Leu-Leu-Gly-Pro-Gly-Leu-Thr-Asn-His-Ala (1076 Da), and Asp-Leu-Gly-Leu-Gly-Leu-Pro-Gly-Ala-His (1033 Da) by Q-TOF ESI mass spectroscopy. EC50 values of purified peptides were 189.8 and 167.7 μM, respectively. Antioxidant activities of peptides purified from the rotifer protein hydrolysate were evaluated, with results showing that peptides significantly quenched free radicals.

Keywords
Antioxidant; Marine rotifer; Hydrolysate; Peptide; Enzymatic hydrolysis
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Antioxidant peptides isolated from the marine rotifer, Brachionus rotundiformis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 8, August 2009, Pages 842–846
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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