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Purification and characterization of antioxidative peptides from round scad (Decapterus maruadsi) muscle protein hydrolysate
被引:119
作者:
Jiang, Haiping
[1
,3
]
Tong, Tianzhe
[2
]
Sun, Jianhua
[1
]
Xu, Yuanjin
[1
]
Zhao, Zhongxing
[1
]
Liao, Dankui
[1
,3
]
机构:
[1] Guangxi Univ, Sch Chem & Chem Engn, Nanning 530004, Guangxi, Peoples R China
[2] Univ Sci & Technol China, Sch Chem & Mat Sci, Hefei 230026, Anhui, Peoples R China
[3] Guangxi Key Lab Petrochem Resource Proc & Proc In, Nanning 530004, Guangxi, Peoples R China
来源:
关键词:
Round scad (Decapterus maruadsi);
Antioxidative peptide;
Purification;
Characterization;
Enzymatic hydrolysis;
RADICAL SCAVENGING ACTIVITY;
CONSECUTIVE CHROMATOGRAPHY;
IDENTIFICATION;
D O I:
10.1016/j.foodchem.2013.12.074
中图分类号:
O69 [应用化学];
学科分类号:
070301 [无机化学];
摘要:
Muscle protein from round scad (Decapterus maruadsi) was hydrolyzed with five commercial proteases, namely, Alcalase, neutral protease, papain, pepsin, and trypsin. Round scad hydrolysate (RSH) prepared with Alcalase demonstrated high antioxidative activity. After ultrafiltration, RSH-III fraction (M-w < 5 kDa) exhibited the strongest activity. Then, RSH-III was purified by gel filtration chromatography (Sephadex G-15) and separated into four fractions (A, B, C, and D), of which fraction B showed the highest antioxidative activity and was further purified using reverse-phase high-performance liquid chromatography twice. The purified peptides were identified as His-Asp-His-Pro-Val-Cys (706.8 Da) and His-Glu-Lys-Val-Cys (614.7 Da) by matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry. Subsequently, the identified peptides were synthesized, and their antioxidative activities were verified. Results indicated that the two novel peptides isolated from round scad muscle protein can be developed into antioxidative ingredients in functional foods. (C) 2013 Elsevier Ltd. All rights reserved.
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页码:158 / 163
页数:6
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