Enzymatic Preparation and Structural Identification of Antioxidant Peptides from Bass Protein
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Abstract:
In order to prepare the bass protein peptide with strong antioxidant activity, bass proteins were hydrolyzed by flavorzyme, protamex, alcalase 2.4 L, neutrase and papain under appropriate condition. The degree of hydrolysis (DH), protein recovery rate and antioxidant activity (oxygen radical absorbance capacity and 2,2‘-azinobis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) free radical scavenging capacity) of the hydrolysate of bass proteins were determined by ultra performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS). The peptide structure of the hydrolyzed product with good antioxidant activity was analyzed and identified, and the peptide was further synthesized to verify its activity. The results showed that the papain hydrolysate of bass protein not only exhibited the highest DH (25.61%) and protein recovery rate (78.71%) among five hydrolysates,but also revealed the most potent ORAC and TEAC values of 783.56 and 734.55 μmol TE/g, respectively. UPLC-MS/MS analysis was applied for structural identification of papain hydrolysate. A total of 9 peptides were found by searching in the Uniprot, and 3 of them showed antioxidant activity, which were EYGTVVVFQ, HRDRLCVVQ and GGGAGMLLK. EYGTVVVFQ possessed the most potent ORAC and TEAC values of 1.43 and 2.34 μmol TE/μmol, respectively. This study provided theoretical guidance for the development and utilization of bass antioxidant peptides as well as marine proteins.
