We have investigated the antioxidant activity of hydrolysates from whey proteins bovine alpha-lactalbumin (alpha-La) and beta-lactoglobulin A (beta-Lg A) by commercial proteases (pepsin, trypsin, chymotrypsin, thermolysin, and Corolase PP). Corolase PP was the most appropriate enzyme to obtain antioxidant hydrolysates from alpha-La and beta-Lg A (ORAC-FL values of 2.315 and 2.151 micromol of Trolox equivalent/mg of protein, respectively). A total of 42 peptide fragments were identified by HPLC-MS/MS in the beta-Lg A hydrolysate by Corolase PP. One of the sequences (Trp-Tyr-Ser-Leu-Ala-Met-Ala-Ala-Ser-Asp-Ile) possessed radical scavenging (ORAC-FL value of 2.621 micromol of Trolox equivalent/micromol of peptide) higher than that of butylated hydroxyanisole (BHA). Our results suggest that whey protein hydrolysates could be suitable as natural ingredients in enhancing antioxidant properties of functional foods and in preventing oxidation reaction in food processing.

The angiotensin-converting enzyme (ACE)-inhibitory activity and antioxidant properties of a commercial fermented milk from Europe were evaluated. This dairy product showed moderate ACEinhibitory activity and ABTS • + radical-scavenging capacity. The peptides from most active fractions collected by reverse phase high-performance liquid chromatography (RP-HPLC) were sequenced by RP-HPLC-tandem mass spectrometry. This technique allowed rapid identification of peptides included in the most active fractions, and various potentially active peptides were recognised according to previous studies of structure-activity relationship. Three of the identified sequences had previously been described as potent ACE inhibitors. The structure of some sequences substantiated the presence of peptides with ACE-inhibitory, antioxidant and immunomodulatory activities.

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The angiotensin converting enzyme (ACE)-inhibitory activity of several commercial fermented milks was evaluated. Most of these products showed moderate inhibitory activity, but a few exceptions were detected. The high ACE-inhibitory activity found in some cases could be related to the origin of the milk. Two of these products were subjected to an enzymatic hydrolysis process, which simulates physiological digestion, to study the influence of digestion on ACE-inhibitory activity. The activity did not significantly change or increase during simulated gastrointestinal digestion. The peptides generated from one selected product during simulated digestion were sequenced by tandem spectrometry. Most peptides found at the end of the simulated digestion were released after 30 min of incubation with the pancreatic extract. This suggests that physiological digestion promotes the formation of active peptides from the proteins present in these fermented products. The potential ACE-inhibitory activity of the identified peptides is discussed with regard to their amino acid sequences.

Germinated brown rice (GBR) is considered a healthy alternative to white rice in the fight against chronic diseases. As the functional quality of GBR depends on genotype and germination conditions, the objectives were to identify suitable Ecuadorian brown rice cultivars and optimal germination time and temperature to maximise γ-aminobutyric acid (GABA), total phenolics compounds (TPC) and antioxidant activity of GBR. Regression models for the prediction of phytochemical composition and antioxidant activity in GBR were also obtained. Germination improved GABA, TPC and antioxidant activity in all cultivars. Maximum GABA and antioxidant activity were attained at 34 °C for 96 h, while the highest TPC was found at 28 °C for 96 h in all cultivars. GBR cv. GO displayed the highest antioxidant activity and cv. 15 was the most effective at accumulating GABA and TPC in the optimal germination conditions. Therefore, Ecuadorian GBR could be used for the preparation of functional foods serving as preventative strategies in combating chronic diseases.

In this study, a potent angiotensin-converting enzyme (ACE)-inhibitory activity was found in a commercial kefir made from caprine milk. The low molecular mass peptides released from caseins during fermentation were mainly responsible for this activity. Sixteen peptides were identified by HPLC-tandem mass spectrometry. Two of these peptides, with sequences PYVRYL and LVYPFTGPIPN, showed potent ACE-inhibitory properties. The impact of gastrointestinal digestion on ACE-inhibitory activity of kefir peptides was also evaluated. Some of these peptides were resistant to the incubation with pepsin followed by hydrolysis with Corolase PP. The ACE-inhibitory activity after simulated digestion was similar to or slightly lower than unhydrolyzed peptides, except for peptide beta-casein f(47-52) (DKIHPF), which exhibited an activity 8 times greater after hydrolysis.

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