Purification and Identification of Antioxidant Peptides from Enzymatic Hydrolysates of Tilapia (Oreochromis niloticus) Frame Protein

Molecules

Jian Fan¹  Jintang He¹  Yongliang Zhuang¹ 

[1] College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming 650500, China;

关键词: tilapia frame protein;    enzymatic hydrolysis;    antioxidant peptide;    purification;    amino acid sequence;   

DOI  :  10.3390/molecules171112836

来源: mdpi

【 摘 要 】

Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC₅₀ values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (^•O₂), hydrogen peroxides (H₂O₂) and hydroxyl radical (•OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC₅₀ values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.

【 授权许可】

CC BY   
© 2012 by the authors; licensee MDPI, Basel, Switzerland.