Antioxidant activity of protein hydrolysates obtained from discarded Mediterranean fish species

被引:102
|
作者
Garcia-Moreno, Pedro J. [1 ]
Batista, Irineu [2 ]
Pires, Carla [2 ]
Bandarra, Narcisa M. [2 ]
Espejo-Carpio, F. Javier [1 ]
Guadix, Antonio [1 ]
Guadix, Emilia M. [1 ]
机构
[1] Univ Granada, Dept Chem Engn, Granada 18071, Spain
[2] IPMA, DivAv, P-1449006 Lisbon, Portugal
关键词
Discards; Fish protein hydrolysates; Antioxidant activity; DPPH; Fe2+ chelating activity; Reducing power; RADICAL-SCAVENGING ACTIVITIES; MORHUA BY-PRODUCTS; FUNCTIONAL-PROPERTIES; ENZYMATIC-HYDROLYSIS; GASTROINTESTINAL PROTEASES; OXIDATIVE STABILITY; FRAME PROTEIN; MUSCLE; PEPTIDES; PURIFICATION;
D O I
10.1016/j.foodres.2014.03.061
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
In this study, five discarded species in the Mediterranean Sea, namely sardine, horse mackerel, axillary seabream, bogue and small-spotted catshark, were evaluated as raw material for obtaining fish protein hydrolysates exhibiting antioxidant activity. The DH of the hydrolysates ranged from 13.2 to 21.0%, with a protein content varying from 60.7 to 89.5%. The peptide profile of all hydrolysates was very similar, except for the hydrolysate of small-spotted catshark. Their lipid content was found to be between 4.6 and 25.3%. The highest DPPH scavenging activity was found for the hydrolysates of sardine and horse mackerel with EC50 values varying from 0.91 to 1.78 mg protein/mL Sardine and small-spotted catshark hydrolysates exhibited the highest ferrous chelating activity with an EC50 value of 0.32 mg protein/mL Moreover, sardine and bogue hydrolysates presented the highest reducing power. Finally, a total of six antioxidant peptides were theoretically identified within the structure of myosin and actin proteins from sardine and small-spotted catshark. The potential antioxidant activity exhibited by the hydrolysates suggests that it is feasible to obtain added-value products such as natural antioxidants from these discarded species. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:469 / 476
页数:8
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