Extraction and Characterization of Protein Concentrates from Limpets () and Peptide Release Following Gastrointestinal Digestion.

This study investigated the characterization of proteins from the Irish limpet () and assessed the biological activities of hydrolysates obtained following gastrointestinal digestion (INFOGEST) of a limpet protein concentrate (LPC). The physicochemical properties and the digestibility of the LPC were investigated, along with the angiotensin-converting enzyme (ACE) inhibition and antioxidant activities of the LPC-digested samples. All the digested samples examined outperformed the LPC in terms of activity.

Structure and in vitro bioactive properties of O/W emulsions generated with fava bean protein hydrolysates.

The use of plant-derived proteins in the generation of food products is gaining popularity as an alternative to proteins of animal origin. This study described the emulsifying and bioactive properties of fava bean protein hydrolysates (FBH) generated at low and high degree of hydrolysis (DH), i.e.

dipeptidyl peptidase IV inhibitory activity and insulinotropic activity of milk and egg white protein digests.

Dietary proteins are involved in the regulation of glucose homeostasis by different mechanisms. Food protein digestion products are reported to inhibit dipeptidyl peptidase IV (DPP-IV), induce incretin secretion or directly exert an insulinotropic effect in pancreatic β-cells. This study illustrates the DPP-IV inhibitory activity of gastric and intestinal digests of casein, whey and egg white proteins determined , using Gly-Pro-AMC, and using non-differentiated Caco-2 cells.

Enzyme-Assisted Release of Antioxidant Peptides from Conchocelis.

The conchocelis life cycle stage of represents an unexplored source of bioactive compounds. The aim of this study was to generate and characterise, for the first time, hydrolysates of conchocelis using a specific combination of proteases (Prolyve and Flavourzyme). Hydrolysate molecular mass distribution and free amino acid contents were assessed, and the antioxidant activity was determined using a range of in vitro assays.

Effect of in vitro simulated gastrointestinal digestion on the antioxidant activity of the red seaweed Porphyra dioica.

Porphyra sp. is one of the most cultivated and commercially valuable species, recognized for its high protein content (up to 47% dry weight) and complete amino acids profile. Based on these characteristics, P.

Influence of Hydrolysis on the Bioactive Properties and Stability of Chickpea-Protein-Based O/W Emulsions.

This study evaluated the effect of enzymatic hydrolysis on the emulsion microstructure and bioactive properties of oil-in-water emulsions generated using chickpea protein concentrate (CP) and its 10 and 210 min Alcalase CP hydrolysates (CPH and CPH, respectively) at three pH values (2.5, 5.0, and 7.

Current knowledge on the extraction, purification, identification, and validation of bioactive peptides from seaweed.

Seaweed (macroalgae) is considered as a sustainable bioresource rich in high-quality nutrients such as protein. Seaweed protein can be used as an alternative to other protein sources. Furthermore, these proteins are natural reservoirs of bioactive peptides (BAPs) associated with various health benefits such as antioxidant, antihypertensive, and antidiabetic activities.

Enzymatic Modification of -Derived Proteins to Improve their Antioxidant Potential.

Enzymatic hydrolysis has been employed to modify protein functional properties and discover new sources of antioxidants. In this study, the effect of different enzymatic treatments on antioxidant activity of (blades and protein isolate (PI)) was investigated. Protein nitrogen content of blades and PI were 23 and 50% (dry weight), respectively.

Peptide identification from a Porphyra dioica protein hydrolysate with antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activities.

A Porphyra dioica protein extract was enzymatically hydrolysed and then fractionated using semi-preparative reverse-phase high performance chromatography. The hydrolysate and its fractions were tested for their oxygen radical absorbance capacity (ORAC) along with their angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. The most potent fraction was analysed by liquid chromatography mass spectrometry.

Characterisation of the bioactive properties and microstructure of chickpea protein-based oil in water emulsions.

Legumes, such as chickpea, represent a good source of high quality proteins for which there is an increasing global consumer demand. A chickpea protein concentrate (CP) was generated by isoelectric precipitation. Protein determination, electrophoretic and gel permeation chromatographic analysis revealed that the order of CP solubility was pH 7.

Characterisation of the in vitro bioactive properties of alkaline and enzyme extracted brewers' spent grain protein hydrolysates.

Brewer's spent grain (BSG) is a co-product of the brewing industry that has been shown to contain a range of bioactive peptides encrypted within its protein sequences. Two methods were evaluated herein to generate bioactive peptides; (i) an alkaline extracted BSG protein rich fraction (BSG-PI) was hydrolysed using different combinations of proteolytic enzymes and (ii) BSG was pre-treated with carbohydrases followed by direct hydrolysis using proteolytic enzymes (BSG-DH). BSG-DH with Alcalase/Flavourzyme resulted in significantly higher (p < .