Antioxidant properties of carp (Cyprinus carpio L.) protein ex vivo and in vitro hydrolysates.

The presence of specific peptides with antioxidant properties released during carp protein ex vivo and in vitro hydrolysis by human/porcine digestive enzymes, respectively, was examined. Based on the results of the in silico data analysis, antioxidant peptides were selected for subsequent identification in the digests/hydrolysates. Carp proteins were more resistant to hydrolysis by porcine enzymes than by human digestive juices.

Antioxidant properties of salmon (Salmo salar L.) protein fraction hydrolysates revealed following their ex vivo digestion and in vitro hydrolysis.

Background: Salmon (Salmo salar L.) myofibryllar protein (MP) and sarcoplasmic protein (SP) were digested with human gastric and duodenal juices and hydrolysed in vitro with commercial pepsin and Corolase PP.

Results: The digestion after duodenal juice/Corolase PP caused almost complete breakdown of peptide bonds in MP and SP.

Angiotensin I-converting enzyme (ACE) inhibitory activity and ACE inhibitory peptides of salmon (Salmo salar) protein hydrolysates obtained by human and porcine gastrointestinal enzymes.

The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE inhibitory activity of generated hydrolysates. A two-step ex vivo and in vitro model digestion was performed to simulate the human digestion process.

[Biologically active peptides derived from food proteins as the food components with cardioprotective properties].

Food proteins are the source of peptides with many biological activities. One of them is their impact on blood circulatory system. This group of peptides includes the ones with the ability to reduce the blood pressure (inhibitors of angiotensin converting enzyme--ACE), antithrombotic, and to lower the cholesterol level.

Epitopic hexapeptide sequences from Baltic cod parvalbumin beta (allergen Gad c 1) are common in the universal proteome.

The aim of this study was to analyze the distribution of hexapeptide fragments considered as epitopes of Baltic cod parvalbumin beta (allergen Gad c 1) in the universal proteome. Cod (Gadus morhua subsp. callarias) parvalbumin hexapeptides cataloged in the Immune Epitope Database were used as query sequences.