Antioxidant activity of protein hydrolysates obtained from discarded Mediterranean fish species

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.This work was supported by the Spanish National Plan I + D + i (projects CTQ2008-02978 and CTQ2011-23009) and by Santander Bank (grant for young researchers

Evaluation of Tenebrio molitor protein as a source of peptides for modulating physiological processes

The increasing world population has led to the need to search for new protein sources, such as insects, the harvesting of which can be economical and environmentally sustainable. This study explores the biological activities (angiotensin-converting enzyme (ACE) inhibition, antioxidant capacity, and dipeptidyl peptidase IV (DPP-IV) inhibition) of Tenebrio molitor hydrolysates produced by a set of food-grade pro- teases, namely subtilisin, trypsin, ficin and flavourzyme, and the degree of hydrolysis (DH), ranging from 5% to 20%. Trypsin hydrolysates exhibited the highest ACE inhibitory activity at a DH of 10% (IC50 0.27 mg mL−1) in the experimental series, which was attributed to the release of short peptides containing Arg or Lys residues in the C terminus, and described as the ACE-inhibition feature. The levels of in vitro anti- oxidant activities were comparable to those reported for insect species. Subtilisin and trypsin hydrolysates at a DH of 10% displayed optimal DPPH scavenging and ferric reducing activities, which was attributed to the presence of 5–10-residue active peptides, as reported in the literature. Iron chelating activity was significantly favoured by increasing the DH, attaining a minimal IC50 of 0.8 mg mL−1 at a DH of 20% regardless of the enzymatic treatment. Similarly, in vitro antidiabetic activity was significantly improved by extensive hydrolysis, and, more specifically, the presence of di- and tripeptides. In this regard, the combined treatment of subtilisin–flavourzyme at a DH of 20% showed maximal DPP-IV inhibition (IC50 2.62 mg mL−1). To our knowledge, this is the first study evaluating the DPP-IV activity of Tenebrio molitor hydrolysates obtained from these commercial proteases. We conclude that Tenebrio molitor hydrolysates produced with food-grade proteases are a valuable source of active peptides that can be used as functional ingredients in food and nutraceutical preparations.FEDER CTQ2017-87076-RMinisterio de Economía, Industria y Competitivida

Development of Fish Oil-Loaded Microcapsules Containing Whey Protein Hydrolysate as Film-Forming Material for Fortification of Low-Fat Mayonnaise

The authors are very grateful to Lis Berner for her skillful help with the PV and SVOP measurements of the microcapsules.The influence of the carbohydrate-based wall matrix (glucose syrup, GS, and maltodextrin, MD21) and the storage temperature (4 ◦C or 25 ◦C) on the oxidative stability of microencapsulated fish oil was studied. The microcapsules (ca. 13 wt% oil load) were produced by spray-drying emulsions stabilized with whey protein hydrolysate (WPH), achieving high encapsulation efficiencies (>97%). Both encapsulating materials showed an increase in the oxidation rate with the storage temperature. The GS-based microcapsules presented the highest oxidative stability regardless of the storage temperature with a peroxide value (PV) of 3.49 ± 0.25 meq O2/kg oil and a content of 1-penten-3-ol of 48.06 ± 9.57 ng/g oil after six weeks of storage at 4 ◦C. Moreover, low-fat mayonnaise enriched with GS-based microcapsules loaded with fish oil and containing WPH as a film-forming material (M-GS) presented higher oxidative stability after one month of storage when compared to low-fat mayonnaise enriched with either a 5 wt% fish oil-in-water emulsion stabilized with WPH or neat fish oil. This was attributed to a higher protective effect of the carbohydrate wall once the microcapsules were incorporated into the mayonnaise matrix.Spanish Ministry of Science, Innovation and Universities CTQ2017-87076-R PRE2018-08486