Enzymatic Hydrolysis Of Food Proteins Research Articles

Proteolytic Activity of Silkworm Thorn (Cudrania tricuspidata) Fruit for Enzymatic Hydrolysis of Food Proteins.

This study aimed to isolate the proteolytic fraction from the silkworm thorn fruit (Cudrania tricuspidata) through ethanol precipitation at different ratios, and to determine its proteolytic activity and optimal activity conditions. Furthermore, the hydrolysis characteristics and antioxidant activity of soy protein isolate (SPI) and whey protein concentrate (WPC) hydrolyzates obtained through the enzymatic hydrolysis of freeze-dried silkworm thorn fruit powder (SF) were evaluated. For isolation and partial purification of proteolytic fraction, the water-solubilized fraction of the silkworm thorn fruit was purified through ethanol precipitation at four different ratios of 1:1, 1:2, 1:4, and 1:6 (v/v). The protein recovery rate, caseinolytic activity, protein pattern, and optimal activity (pH, temperature, and inhibitors) of fractional ethanol precipitate obtained from the silkworm thorn fruit (ESF) were evaluated. The proteolytic fraction obtained from silkworm thorn fruit exhibited a major protein band around 65-70 kDa and showed the highest proteolytic activity at a 1:4 ratio of ethanol precipitation (p < 0.05). The optimal activity of the measured enzyme fraction was determined to be at pH 9.0 and 50 °C, and the proteolytic activity of ESF was almost inhibited by phenyl methyl sulphonyl fluoride (PMSF, 2 mM), a serine protease inhibitor. Compared to Alcalase and papain, extensively used as commercial enzymes, the silkworm thorn fruit powder was less effective in hydrolyzing SPI and WPC. Nevertheless, SPI and WPC hydrolyzates mediated with silkworm thorn fruit powder showed even better antioxidant activities than those mediated with Alcalase and papain. Thus, our results show the potential application of silkworm thorn fruit as a novel source of plant protease for producing human-grade protein hydrolyzates.

Fermented food products for gastrointestinal health and related diseases

The incidence of lifestyle diseases such as inflammatory bowel diseases is increasing due to unhealthy eating habits and modern lifestyles, resulting in a growing demand for fermented foods worldwide due to their scientifically proven functional and nutritional attributes. Fermented foods are obtained by controlled microbial growth and enzymatic degradation of food constituents. These foods have a good amount of probiotic bacteria and bioactive peptides that benefit human health. Bioactive peptides are formed by either fermentation or enzymatic hydrolysis of food proteins. Fermented foods and beverages i.e., dahi, yogurt, kefir, kimchi, sourdough bread, pickles play a significant role in gut microbiota balance and mental health. Starter culture used in the fermentation of food products provide various health-promoting activities to fermented foods like anti-oxidant activity, anti-hypertensive activity, probiotic activity and improves protein digestibility. Several groups of lactic acid bacteria (LAB) strains produce Exopolysaccharides (EPS) such as  and - glucans, galactans, fructans, and gluco- and fructo-oligosaccharides. EPS produced by LAB has a positive impact on gut health. In addition, probiotic bacteria have proven to be a beneficial ingredient for any gut disorder (inside or outside the GI tract). They regulate the level of immunoglobulins (IgA) and inflammatory cytokines and improve gut barrier activity. Symbiotic yogurt (made with bacterial strains of Lactobacillus acidophilus and Bifidobacterium longum) helps raise high-density lipoprotein (HDL) cholesterol and also changes the ratio of low-density lipoprotein (LDL) to HDL. Consumption of kefir inhibits the pathogen's action by the production of acids and bacteriocins. Isolation and pharmaceutical applications of health-promoting bioactive peptides from fermented foods have been emerging in dairy and food research areas.

Agro-industrial by-products as substrates for the production of bacterial protease and antioxidant hydrolysates

Feather meal (FM), sweet whey (LW), lyophilized whey (WL), and cassava bagasse (CB) were investigated as substrates to obtain extracellular proteases and bioactive hydrolysates during cultivations with Bacillus sp. CL33A. Initial evaluations indicated that FM (10 g/L), as single substrate, resulted in higher protease production, and higher soluble protein contents and antioxidant activities in culture supernatants, in comparison to LW, WL (5, 10, 15 g/L) or CB (5, 10, 15 g/L plus 1 g/L (NH4)2SO4)). Increasing FM to 30 g/L enhanced protease production 6-fold, which peaked after 4 days of cultivation. Protease production was paralleled by increases in soluble protein content in supernatants, which demonstrated radical-scavenging, Fe3+-reducing, and Fe2+-chelating activities. Supplementation of 30 g/L FM with 5 g/L WL increased protease yields (1.8-fold) after 4 days; enzyme production peaked after 6 days of cultivation, corresponding to a 3-fold increase in comparison to FM-only medium at day 4. Adding CB (5 and 10 g/L) to 30 g/L FM increased protease production by 110–130% after 4 days of cultivation. LW-supplemented FM medium showed decreased protease production, postponing soluble protein release and increases on antioxidant activities. No marked influences of supplemental WL or CB were observed on the antioxidant activities of obtained protein hydrolysates. FM is a low-cost substrate to simultaneously obtain bioproducts. The use of WL or CB as co-substrates might be interesting to manage and add value to these by-products. The obtained protease might find applications in the enzymatic hydrolysis of food proteins, and antioxidant hydrolysates deserve investigations as animal feed.

Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins

Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 ± 23 µm) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 ± 103 nm and 394 ± 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 ± 4 mg g−1 on the carrier and the highest immobilized alcalase activity of 2716.1 IU g−1 in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.

Principal Component Analysis from Mass Spectrometry Data Combined to a Sensory Evaluation as a Suitable Method for Assessing Bitterness of Enzymatic Hydrolysates Produced from Micellar Casein Proteins.

Enzymatic hydrolysis of food proteins generally changes the techno-functional, nutritional, and organoleptic properties of hydrolyzed proteins. As a result, protein hydrolysates have an important interest in the food industries. However, they tend to be characterized by a bitter taste and some off-flavors, which limit their use in the food industry. These tastes and aromas come from peptides, amino acids, and volatile compounds generated during hydrolysis. In this article, sixteen more or less bitter enzymatic hydrolysates produced from a milk protein liquid fraction enriched in micellar caseins using commercially available, food-grade proteases were subjected to a sensory analysis using a trained and validated sensory panel combined to a peptidomics approach based on the peptide characterization by reverse-phase high-performance liquid chromatography, high-resolution mass spectrometry, and bioinformatics software. The comparison between the sensory characteristics and the principal components of the principal component analysis (PCA) of mass spectrometry data reveals that peptidomics constitutes a convenient, valuable, fast, and economic intermediate method to evaluating the bitterness of enzymatic hydrolysates, as a trained sensory panel can do it.

Antidiabetic Food-Derived Peptides for Functional Feeding: Production, Functionality and In Vivo Evidences.

Bioactive peptides released from the enzymatic hydrolysis of food proteins are currently a trending topic in the scientific community. Their potential as antidiabetic agents, by regulating the glycemic index, and thus to be employed in food formulation, is one of the most important functions of these peptides. In this review, we aimed to summarize the whole process that must be considered when talking about including these molecules as a bioactive ingredient. In this regard, at first, the production, purification and identification of bioactive peptides is summed up. The detailed metabolic pathways described included carbohydrate hydrolases (glucosidase and amylase) and dipeptidyl-peptidase IV inhibition, due to their importance in the food-derived peptides research field. Then, their characterization, concerning bioavailability in vitro and in situ, stability and functionality in food matrices, and ultimately, the in vivo evidence (from invertebrate animals to humans), was described. The future applicability that these molecules have due to their biological potential as functional ingredients makes them an important field of research, which could help the world population avoid suffering from several diseases, such as diabetes.

Current genetic engineering strategies for the production of antihypertensive ACEI peptides.

Hypertension is a major and highly prevalent risk factor for various diseases. Among the most frequently prescribed antihypertensive first-line drugs are synthetic angiotensin I-converting enzyme inhibitors (ACEI). However, since their use in hypertension therapy has been linked to various side effects, interest in the application of food-derived ACEI peptides (ACEIp) as antihypertensive agents is rapidly growing. Although promising, the industrial production of ACEIp through conventional methods such as chemical synthesis or enzymatic hydrolysis of food proteins has beenproven troublesome. We here provide an overview ofcurrent antihypertensive therapeutics, focusing on ACEI, and illustrate how biotechnology and bioengineering can overcome the limitations ofACEIp large-scale production. Latest advances in ACEIp research and current genetic engineering-based strategies for heterologous production of ACEIp (and precursors) are also presented. Cloning approaches include tandem repeats of single ACEIp, ACEIp fusion to proteins/polypeptides, joining multivariate ACEIp into bioactive polypeptides, and producing ACEIp-containing modified plant storage proteins. Although bacteria have been privileged ACEIp heterologous hosts, particularly when testing for new genetic engineering strategies, plants and microalgae-based platforms are now emerging. Besides being generally safer, cost-effective and scalable, these "pharming" platforms can perform therelevant posttranslational modifications and produce (and eventually deliver) biologically active protein/peptide-based antihypertensive medicines.

Antioxidant and antihypertensive protein hydrolysates in fish products - a review

Fish proteins are a good source of bioactive peptides (BAPs). Such BAPs are derived through enzymatic hydrolysis of food proteins and can potentially by applied as health-promoting factors against chronic non-communicable diseases (NCDs), including arterial hypertension, cardiovascular disease and obesity. Antihypertensive and antioxidant BAPs derived from fish could represent a good alternative to synthetic drugs. This article reviews the literature on BAPs derived from fish and fish products, with an emphasis on antihypertensive and antioxidant properties and the impact of technological processes on the activity of BAPs. The review shows that BAPs isolated from fish exhibit quite good stability when applied under moderate physical conditions and after simulated in vitro digestion. Processing can increase the susceptibility of peptides to digestion in the digestive tract as well as improving absorption and immune system responses. Therefore, it is important to determine the optimal conditions under which proteins (and peptides) can be processed in order to maintain their bioactivity. Future research efforts on BAPs should be directed towards an elucidation of their activity after technological processes.

Experimental evaluation of hypolipidemic properties of soy and rice proteins and their enzyme hydrolysates. A brief review

Metabolic syndrome (MS) is characterized with high prevalence, constant increase of people suffering from this disease and high rate of cardiovascular complications. The key factors, leading to the development of metabolism disorders during MS, are visceral fat mass growth and decrease in sensitivity of peripheral tissues to insulin, which are associated with disorders of carbohydrate, lipid, purine metabolism and arterial hypertension. The main results of in vivo studies of hypolipidemic properties of soy protein, rice bran protein and their enzymatic hydrolysates using laboratory rats and mice with experimentally induced or genetically associated dyslipidemia are presented in this review. The analysis of reviewed publications shows that consumption of soy protein provides body weight loss, normalizes lipid metabolism, reduces insulin resistance. The consumption of rice protein by laboratory animals, as well as soy protein, leads to decrease of serum cholesterol level and also provides steroid excretion, such as cholesterol and bile acids, with feces. Enzymatic hydrolysis of food proteins allows obtaining peptide mixtures with high biological value and improved functional properties, especially water solubility and intestinal absorption. In their turn, hypolipidemic peptides of hydrolysates can play a key role in endogenous cholesterol homeostasis by means of disturbing its micellar solubility, intestinal absorption, changing bile acids entherohepatic circulation, and also lowering the expression of some genes of proteins - mediators of lipid transport. It has been concluded, that hypolipidemic properties of obtained enzymatic hydrolysates of food proteins determine the prospects of their use in specialized food products for prevention of metabolic disorders.

Features of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from dietary proteins.

Dipeptidyl peptidase IV (DPP-IV) is involved in incretin hormone processing and therefore plays a key role in glycemic regulation. This review summarizes the latest developments in food protein-derived DPP-IV inhibitory peptides. The in silico approaches currently used to develop targeted strategies for the enzymatic release of DPP-IV inhibitory peptides from food proteins are outlined. The features within the primary sequences of potent DPP-IV inhibitory di-, tri-, and larger peptides, having half maximal inhibitory activity (IC50 ) < 100 µM, were evaluated and the outcomes are presented herein. It is proposed that detailed analysis of those food derived peptides identified in humans following ingestion may constitute a practical strategy for the targeted identification of novel bioavailable DPP-IV inhibitory peptides. Human intervention studies are required as the specific role of food protein-derived DPP-IV inhibitory peptides in the regulation of glycaemia in humans remains to be fully elucidated. PRACTICAL APPLICATIONS: This review provides recent information on dipeptidyl peptidase IV (DPP-IV) inhibitory peptides arising from food protein hydrolysates. Small animal studies have demonstrated that food protein hydrolysates with in vitro DPP-IV inhibitory properties also display antidiabetic activity. DPP-IV inhibitory peptides may be used as food ingredients to improve glycemic regulation in Type 2 diabetics. Therefore, the development of potent DPP-IV inhibitory hydrolysates containing bioavailable peptides in humans is of significant interest. This may help in the formulation of foods containing physiologically relevant doses of bioactive hydrolysates/peptides. Acquisition of detailed knowledge of DPP-IV inhibitory peptide features via the utilization of in silico tools may help to optimize the release of potent DPP-IV inhibitory peptides during enzymatic hydrolysis of food proteins. This review provides information on features within the primary sequences of potent DPP-IV inhibitory peptides and current in silico strategies which may be used to inform on the targeted enzymatic hydrolysis of food proteins.

Characterization of commercially available peptidases in respect of the production of protein hydrolysates with defined compositions using a three-step methodology

Enzymatic hydrolysis of food proteins is an effective way to implement a desired functionality into protein containing foods. Since these functionalities are highly dependent on the degree of hydrolysis (DH) of the hydrolysates, the enzymatic hydrolysis process must be carefully controlled. Hydrolysates with both free amino acids and long-chain peptides are usually not desirable which leads to strict requirements for the commercial peptidases used. In the study presented, we characterized ten commercially available peptidase preparations in respect of the production of protein hydrolysates with defined compositions. Therefore, we utilized a three-step methodology to investigate the composition of the commercial peptidase preparations and to characterize the obtained protein hydrolysates applying a HPLC-based system for automated small-scale enzymatic reaction and analysis. With the presented methodology we identified two suitable preparations for the production of hydrolysates with high DH and high amounts of free amino acids, and six suitable preparations for the production of hydrolysates with low DH and negligible release of amino acids.

Analysis of the operational strategies for the enzymatic hydrolysis of food proteins in batch reactor

The aim of this work was to validate a mathematical model and evaluate hydrolysis of salmon muscle proteins by Alcalase in batch reactor. The inhibition constants were correlated with conversion and temperature thus improving dramatically the agreement between model predictions and experimental hydrolysis time courses. The standard operation in batch reactor consisting in pre-heating, isothermal stage and inactivation of enzyme was evaluated through simulation of different operational strategies based on increasing temperature gradients. Operational conditions were 7.5%(w/w) protein, 1 g/l Alcalase and different temperatures from 50 °C to 73 °C. The optimal temperature for the standard process was 68 °C with a processing time of 41 min. Different operational strategies, included temperature profiles, resulted in longer operation times. The standard process was the best reactor performance due to the maximization of the enzyme efficiency.

Influence of Degree of Hydrolysis on the Functional Properties of Cowpea Protein Hydrolysates

The effects of limited enzymatic hydrolysis with pepsin on the functional properties and molecular characteristics of cowpea protein concentrate (CPC) were investigated. Hydrolysates were prepared at degrees of hydrolysis (DH) 5–30%. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis demonstrated that globulin was the major protein component of CPC, and enzymatic breakdown of polypeptides was selective. As a result, significant changes in the functional properties of hydrolysates were noticed as compared to the protein concentrate. Then, cowpea protein hydrolysates (CPHs) showed good water solubility index at pH 7 (>95%) and pH 4.5 (>55%), at DH 20 and 30%, respectively. Oil-holding capacity, emulsifying activity and foaming capacity were also improved by the enzymatic hydrolysis, while proteolysis was detrimental to foam stability and did not improve emulsion stability at DH 10–30%. Therefore, CPHs showed good potential for utilization in food formulations. Practical Applications Cowpea is a good nutritional value and available protein source, which could be used for a large-scale production of protein hydrolysates. Enzymatic hydrolysis of food proteins is mostly used to produce ingredients or supplements in food and beverages. In this regard, functional properties of protein hydrolysates are largely dependent on the degree of hydrolysis (DH), which needs to be controlled to avoid excessive proteolysis that can impair functionality and cause unfavorable effects. Then, functional properties of cowpea protein concentrate hydrolyzed by pepsin at DH 5–30% were investigated. The results showed that solubility and oil-holding capacity were higher at DH 20–30%. Emulsifying activity and foaming capacity were also improved following hydrolysis, while de-decreasing molecular weight of protein was detrimental to foam stability of hydrolysates. In summary, cowpea protein hydrolysates showed adequate functional properties for utilization as food ingredient and the peptides produced could turn out to present some biological activities.

Industrial Applications of SelectedJFSArticles

Industrial Applications of Selected<i>JFS</i>Articles

"Potential health benefits of lunasin: a multifaceted soy-derived bioactive peptide".

Bioactive peptides are small protein fragments derived from enzymatic hydrolysis of food proteins, fermentation with proteolytic starter cultures, and gastrointestinal digestion. These peptides have positive impacts on a number of physiological functions in living beings. Lunasin, a soy-derived bioactive peptide, is one of the most promising among them. Lunasin encoded within 2S albumin (GM2S-1) gene, identified as a novel peptide extracted from soybean seed. It is composed of 43 amino acid residues with a molecular weight of 5.5 kDa. Extensive scientific studies have shown that lunasin possesses inherent antioxidative, anti-inflammatory, anticancerous properties and could also play a vital role in regulating of cholesterol biosynthesis in the body. Its high bioavailability and heat stable nature allow its potential use as dietary supplement. The present review summarizes some of the potential health and therapeutic benefits of lunasin reported hitherto.

Antioxidant activity of Vigna unguiculata L. walp and hard-to-cook Phaseolus vulgaris L. protein hydrolysates

Recent research, using model systems, has shown that enzymatic hydrolysis of food proteins can make them act as direct scavengers of diverse free radicals. This study aimed at the characterization of protein hydrolysates with antioxidant properties from Vigna unguiculata L. walp and hard-to-cook Phaseolus vulgaris L. protein concentrates. The maximum values obtained for all the assays were 15.1 mM/mg of protein for Trolox-equivalent-antioxidative capacity, 98.2% for percentage of 2,2-diphenyl-1-picrylhydrazyl (DPPH) discoloration, 70.1% and 71.4% for iron and copper chelating activities, respectively. The reducing power of hydrolysates was higher than butylated hydroxytoluene (BHT) (control). The antioxidant activity of the hydrolysates may be a result of enzymatic hydrolysis generating peptides that exhibit this type of activity. The hydrolysates showed an increase of amino acids that have been associated with the biological activity of peptides with antioxidant activity, such as hydrophobic residues: Ala, Phe and Ile; hydrophilic: Lys and neutral: Ser and Gly.

Food Protein‐Derived Bioactive Peptides: Production, Processing, and Potential Health Benefits

Bioactive peptides (BAPs), derived through enzymatic hydrolysis of food proteins, have demonstrated potential for application as health-promoting agents against numerous human health and disease conditions, including cardiovascular disease, inflammation, and cancer. The feasibility of pharmacological application of these peptides depends on absorption and bioavailability in intact forms in target tissues, which in turn depends on structure of the peptides. Therefore, production and processing of peptides based on important structure-function parameters can lead to the production of potent peptides. This article reviews the literature on BAPs with emphasis on strategic production and processing methods as well as antihypertensive, anticancer, anticalmodulin, hypocholesterolemic, and multifunctional properties of the food protein-derived peptides. It is recommended that future research efforts on BAP should be directed toward elucidation of their in vivo molecular mechanisms of action, safety at various doses, and pharmacological activity in maintaining homeostasis during aberrant health conditions in human subjects.

EFFECTS OF pH, TEMPERATURE AND ENZYME TO SUBSTRATE RATIO ON THE ANTIOXIDANT ACTIVITY OF PORCINE HEMOGLOBIN HYDROLYSATE PREPARED WITH PEPSIN

ABSTRACT The effects of pepsin-assisted hydrolysis conditions on the antioxidant activity (AA) of porcine hemoglobin hydrolysate (PHH) were investigated in this study. Effects of temperature, pH and enzyme to substrate ratio on the AA were evaluated and compared using response surface methodology. Temperature and pH were the major factors affecting the AA. Enzyme to substrate ratio influenced AA to a lesser extent. The model for the AA of PHH was established and it showed a good fit with the experimental data. The PHH (1 mg/mL) showed the strongest AA (65.43%) at 40.4C, pH 1.6, enzyme to substrate ratio = 1.6% (w/w). The degree of hydrolysis (DH) and AA of pepsin-assisted hydrolyzed PHH were significant higher (P < 0.05) than chemical hydrolyzed PHH whatever the hydrolysis time. There was no correlation between DH and AA. PRACTICAL APPLICATIONS Blood protein is a by-product of the meat industry with high nutritional and functional value but high pollution power. The proportion of hemoglobin in blood protein is 60–70%. Enzymatic hydrolysis of food proteins generally results in profound changes in the bioactivities of proteins treated. The porcine hemoglobin hydrolysate prepared with pepsin at the optimal hydrolysis conditions was a potent natural free radical scavenger, which would be expected to protect against oxidative damage in living systems and might be potential anti-oxidant for application in food, cosmetic and medicine industries.

OPTIMIZATION OF THE PRODUCTION OF HYDROLYSATES FROM GRASS CARP (CTENOPHARYNGODON IDELLA) SKIN USING ALCALASE

ABSTRACT Protein hydrolysate was produced from grass carp skin using Alcalase. Hydrolysis conditions were optimized by using a response surface methodology (RSM). A model equation was proposed with regard to effects of temperature (T), pH, enzyme/substrate (E/S) ratio (%v/w of minced skin) and time (t) on degree of hydrolysis (%DH). The optimum values for T, pH, E/S ratio and t were found to be 59.74C, 8.25, 1.70% and 83.83 min, respectively. Regression coefficients indicated that all linear forms T, pH, t and E/S ratio plus one quadratic form t2 and one cross-product interaction T · t were significant (α = 0.05). The model showed a good fit in experimental data because 90.7% of the variability within the range of values studied could be explained by it. The freeze-dried hydrolysate contained high protein content (90.8%). The hydrolysate produced was highly water-soluble with good water-holding, oil-binding and emulsifying properties. Thus, the production of a hydrolysate with desired functional properties is possible from grass carp skin using Alcalase. PRACTICAL APPLICATIONS Considerable amounts of protein-rich by-products from seafood processing plants are discarded without any attempt to carry out recovery. The preference in many Western countries for bone-free fillets necessitates the removal of flesh from fish, and a substantial amount of original weight is considered a waste, of which the skin is inclusive. It would be of great interest to put these by-products that are high in protein to use in human foods instead of in fish meals for animal feed. Enzymatic hydrolysis of food proteins generally results in profound changes in the functional properties of proteins treated. The choice of substrate, the protease enzyme employed and the degree of hydrolysis can greatly affect the physicochemical properties of the resultant hydrolysate. Through the control of the process parameters such as pH, time and enzyme/substrate ratio, it is possible to produce hydrolysates whose components may present some interesting properties. Fish protein hydrolysates have numerous applications, particularly in the food and pharmaceutical industries.

The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin

Enzymatic hydrolysis of food proteins can release peptides able to exert different biological activities. Among the bioactive peptides known so far, those with angiotensin converting enzyme (ACE)-inhibitory properties are receiving special attention due to their potential beneficial effects in the treatment of hypertension. In a previous work, we identified active peptide sequences that derived from proteolysis of ovalbumin. We have now explored the possibility of using high hydrostatic pressure to promote the release of bioactive peptides. Treatment of ovalbumin under high pressures, up to 400 MPa, with chymotrypsin, trypsin and pepsin, enhanced its hydrolysis and changed the proteolytic pattern. However, under the conditions assayed, the in vitro ACE inhibitory activity of the hydrolysates did not improve as compared with those obtained at atmospheric pressure. Nevertheless, proteolysis under pressures of 200–400 MPa accelerated the release of the peptides YAEERYPIL, FRADHPFL and RADHPFL, with demonstrated antihypertensive effects in vivo.