جستجوی مقالات مرتبط با کلیدواژه « هیدرولیز آنزیمی » در نشریات گروه « صنایع غذایی »

Peptides obtained from protein hydrolysis have many bioactive properties and have strong antioxidant activity against free radicals and prevent oxidation processes that cause damage to biological macromolecules and degradation and loss of food quality. Due to the large amount of rice production in the world, a large amount of rice bran is produced and available. As a suitable and cheap protein source, rice bran can be used for the production of plant-derived peptides. Optimizing conditions of enzymatic hydrolysis of rice bran protein by alcalase enzyme was done with the aim of achieving maximum antioxidant properties. In order to check the antioxidant activity of the obtained peptides, iron 3 reduction power tests and DPPH free radical inhibitory activity and total antioxidant activity were used. In order to optimize the process, Design Expert software and response surface method were used with three independent variables: enzyme concentration to substrate 1-3%, temperature 40-55 degrees Celsius and hydrolysis time 30-210 minutes. The optimal treatment was obtained under the determined conditions including temperature of 51.5 degrees Celsius, time of 131.5 minutes and concentration of enzyme to substrate of 3%, which has maximum DPPH free radical inhibition of 37.172%, total antioxidant activity of 1.109% and reductiveness of 2.084%. The obtained results showed that the hydrolysis process of rice bran protein by alkalase enzyme has led to the production of peptides with high and significant antioxidant properties that can be used in the production of useful foods and pharmaceutical industries and can also replace synthetic antioxidants.

In recent years, researchers have identified and extracted bioactive peptides with acceptable antioxidant properties from different protein sources. Flaxseed meal, which is the main by-product of the linseed oil extraction process, contains a large amount of protein, which can be obtained by enzymatic hydrolysis to peptides with antioxidant properties. In this research, the effect of hydrolysis conditions (enzyme concentration 2.7-1% and time 30-183.64 minutes), type of protease (pancreatin and alcalase) and ultrasound pretreatment on the degree of hydrolysis and antioxidant properties (DPPH free radical inhibition, Total antioxidant activity, and iron ion chelation) of hydrolyzed protein obtained from flaxseed meal were evaluated using the response surface method. The optimal conditions for the production of hydrolyzed protein with the most antioxidant properties with alcalase enzyme with and without pretreatment and pancreatin enzyme with and without pretreatment, respectively, were hydrolysis time 79, 146.79, 111.77 and 97.21 minutes and enzyme concentration 2.29%, 1.46%, 2.26% and 1.38%; According to the obtained results, by examining the degree of hydrolysis and antioxidant properties of the hydrolyzed proteins of flaxseed meal, hydrolyzed protein with pancreatin enzyme was suggested as the optimal treatment. Hydrolyzed protein with pancreatin enzyme with ultrasound pretreatment was reported to have 75.66% DPPH free radical inhibition, 70.39% iron ion chelating activity, total antioxidant activity with absorbance of 0.86 nm and 80.69% hydrolysis degree. Therefore, it can be stated that the hydrolyzed protein of flax seed meal with strong antioxidant capacity is a bioactive compound for use in food formulations and the production of beneficial products.

Bioactive peptides are actually specific protein parts that, in addition to nutritional value, have positive effects on body function and conditions that lead to health effects. The combined use of pretreatment and enzymatic hydrolysis causes changes in the physical and chemical properties of hydrolyzed proteins. Microwave pretreatment is a well-known strategy to increase the accessibility of hydrolysis-sensitive bonds, facilitating enzyme cleavage sites and exposure to proteases. The aim of this research was to investigate the effect of hydrolysis time and also the effect of microwave pretreatment on enzymatic hydrolysis of edible mushroom (Agaricus bisporus) protein by trypsin enzyme to produce antioxidant peptides. To conduct this research, first, edible mushrooms were turned into powder after purchase from the market and conducting related processes. In this research, hydrolyzed edible mushroom was produced using trypsin enzyme without pretreatment and with microwave pretreatment at different powers of 120, 200, and 280W and time intervals of 30, 60, 90, 120, 150, 180 and 210 minutes. The antioxidant properties of the hydrolysed samples (DPPH radical scavenging activity, iron chelating power, iron ion reduction power and total antioxidant activity) were evaluated and compared. The results showed that in most of the experiments, pretreatment with microwaves decreased the time of obtaining and increased the antioxidant capacity of the samples, so that the samples pretreated with microwave power of 120W showed higher antioxidant power compared to the other treated samples. In all antioxidant tests, the sample pre-treated with microwave with power 120W and hydrolysed at 90minutes showed higher antioxidant performance, and therefore it is considered as suitable treatment.

Due to the length of the time required for protein hydrolysis, ultrasound, as a cheap technology, can be used as a pre-treatment in protein hydrolysis to shorten the time. The aim of this study was to investigate the effect of hydrolysis time and ultrasonic pretreatment on enzymatic hydrolysis of edible mushroom proteins by pancreatin enzyme to produce short chain peptides with high antioxidant capacity. In this research first edible mushrooms were turned into powder then hydrolysed during 30-210 min with enzyme to substrate ratio of 1% and at temperature of 40 °C without pretreatment, and with pretreatment by 80 and 40% ultrasound power. Increasing the power of ultrasonic treatment increased the 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical scavenging activity and total antioxidant capacity at shorter hydrolysis time. The highest DPPH free radical scavenging activity in untreated and treated samples with 40 and 80% ultrasound power were 39.96, 42.91 and 47.76, respectively. The highest total antioxidant capacity for untreated and treated samples with 40 and 80% ultrasound power was 1.64, 1.73 and 1.98 (absorption at 695 nm), respectively. The results showed that the highest reducing power of Fe3+ in untreated and treated samples with 40 and 80% ultrasound power were 2.61, 2.84 and 2.90 (absorption at 700 nm), respectively. These results showed that pre-treated samples with 80% ultrasound compared to samples without pretreatment and pre-treated with 40% ultrasound had the highest antioxidant properties. Therefore, the use of high power ultrasonic pretreatment shortens the hydrolysis time to achieve peptides with higher antioxidant capacity.

In recent years, due to concerns about the safety and health of synthetic antioxidants, there has been widespread attention to the use of natural antioxidants. Bioactive peptides are one of these types of natural antioxidants. Turkmen melon seeds are a rich source of protein. The purpose of this study, was to perform enzymatic hydrolysis of Turkmen melon seed protein with pancreatin and alcalase enzymes in the ratio of enzyme to substrate of 1% and at intervals of 20-200 minutes. The degree of hydrolysis and antioxidant properties (DPPH radical scavengingactivity, Fe3+ reducing power, and total antioxidant activity) of the obtained hydrolysates were investigated. Based on the results obtained from the effect of time on hydrolysis for alcalase-derived hydrolysates, the treatment was 20 to 120 minutes longer than pancreatin, while the treatment of pancreatin-derived hydrolysates for 140 to 200 minutes was higher than that of alcalase. The results showed that there was no significant difference between most of the hydrolysates from pancreatin and alcalase at 180 minutes compared to 200 minutes (about the free radical scavenging activity of DPPH hydrolyzes from alcalase, 160 minutes was determined as the best treatment). The highest scavenging activity of DPPH was total antioxidant by pancreatin enzyme after 160 minutes and 180 minutes of hydrolysis and respectively 72.49% and 1.27 (absorption at 659 nm). The results showed that the produced hydrolysates have a high ability to prevent food oxidation or be used as a medicinal compound.

 High levels of free radicals can damage biomolecules and eventually cause oxidative stress. Bioactive peptides produced during enzymatic hydrolysis keep high health properties, such as antioxidant properties. The production of antioxidant peptides has received much attention as a new generation of natural antioxidants. Plants are one of the most abundant sources of biopolymers, especially protein. As long as the protein structure is intact, its amino acid sequence is inactive; however, during proteolysis, fermentation, and gastrointestinal digestion, these amino acids are released as oligopeptides ordinally with less than 20 amino acids and below 10 kDa in molecular weight. These peptides are more digestible and can exhibit specific bioactive properties such antioxidant properties. In this regard, the use of food waste containing protein to produce bioactive peptides and increase their value has received increasing attention. Enzymatic hydrolysis can increase their functional properties by converting proteins into peptides without affecting their nutritional value. Pomegranate seed protein is a by-product of the pomegranate seed oil industry and can be a good source of bioactive peptides with antioxidant properties. According to our knowledge, there isn’t any data about the enzymatic hydrolysis of pomegranate seed protein for antioxidant peptides production. In this study, the optimal conditions for enzymatic hydrolysis of pomegranate seed protein with trypsin using the responses surface method and the effect of hydrolysis on protein structure were investigated.

 In this study, the protein was extracted from pomegranate seed, and using trypsin the optimization of enzymatic hydrolysis conditions of protein was determined by Face-Centered Central Composite design, which is one of the responses surface design methods. The effect of independent variables including temperature (30 to 45 °C), time (30 to 180 minutes), and enzyme to substrate ratio (1 to 3 w/w) on DPPH free radical scavenging activity and Fe+3 reducing power as responses, was evaluated. Validation tests were performed for confirmation of the proposed values by software and the degree of hydrolysis of the samples was determined. In the next step, the unhydrolyzed and hydrolyzed protein was evaluated for molecular weight distribution and their surface hydrophobicity was compared. Finally, scanning electron microscopy images were used to confirm the hydrolysis process.

 Under optimal conditions obtained from the response surface method (temperature: 37.6 °C, time: 136.55 minutes, and enzyme to substrate ratio: 2.2%), trypsin-derived hydrolyzate, showed DPPH free radical scavenging power: 87±0.89% and Fe+3 reduction power: 0.293±0.44. Under these conditions, the degree of hydrolysis was equal to 30.1±1%. The optimum conditions of hydrolysis were validated by RSM. The increase in the surface hydrophobicity of the protein after the hydrolysis process indicated the unfolding of the pomegranate seed protein chain and the exposure of its structure during the reaction. The electrophoretic profile of denatured pomegranate seed protein showed smaller peptide bands and lower band intensity, along with losing some of the peptide fractions after hydrolysis. so the efficacy of trypsin at cleaving the protein was confirmed. Evaluation of images obtained by scanning electron microscopy showed that unhydrolyzed protein had complex structures comprised of random sheets of different sizes and shapes and the protein degraded into small fragments and looser structure with many folds after enzyme hydrolysis, resulting in smaller particles compared with untreated samples with the same SEM parameters

Considering the consumer’s tendency toward functional foods and present concerns about the application of synthetic additives and according to the results, the hydrolyzed pomegranate seed protein prepared by trypsin shows good antioxidant capacity. In addition, there will be a reduction in waste generated by the pomegranate processing industry. Further studies will need for the isolation and identification of the specific peptides and amino acid sequences and the evaluation of their possible incorporation in food matrices.

In this study, Indian mackerel (Rastrelliger kanagurta ) waste protein hydrolysate was produced using two enzymes, alcalase and flavourzyme, at different times of hydrolysis (10, 20 and 30 minutes) and then its antimicrobial properties against Gram-positive Escherichia coli and Gram-negative Staphylococcus aurous were examined. The results showed that the highest values of nitrogen recovery (89.88%) and degree of hydrolysis (38.70%) were observed by alcalase enzyme during 30 minutes of hydrolysis (P <0.05). The composition of amino acids also showed that the proteins hydrolyzed with both enzymes have a relatively similar composition. The highest levels of essential amino acids for alcalase and flavourzyme were lysine 7.99%, 7.19% and arginine 7.55% and 8.21%, respectively. The highest levels of non- essential amino acids were glutamic acid 12.55%, 11.79% and then aspartic amino acid were 7.99% and 6.98%, respectively. The chemical index showed that both hydrolyzed proteins could well meet an adult human need for most amino acids. The highest antimicrobial activity was observed in the hydrolyzed protein produced by alcalase (P <0.05). Staphylococcus aureus had lower resistance to Escherichia coli. Overall, it seems that Indian mackerel waste protein hydrolysate can be used as protein supplements in food and in diet formulas as a natural antimicrobial.

Enzymatic hydrolysis of protein sources is a common method in food processing. Hydrolyzed protein is a mixture of peptides and amino acids that have many health properties including anti-hypertensive, anti-cholesterol and antioxidant. Turkmen melon seed is one of the fruit by-product which can be a cost-effective source for the production of bioactive peptides. In this study, enzymatic hydrolysis of Turkmen melon seed protein with pancreatin and trypsin enzymes in enzyme to substrate ratio of 1% and time intervals of 20-200 minutes was performed. The degree of hydrolysis and antioxidant properties (DPPH radical scavenging activity, Fe3+ reducing power, total antioxidant activity and hydroxyl radical scavenging activity) of the obtained hydrolysates were investigated. The results showed that with increasing the hydrolysis time up to 180 minutes, the degree of hydrolysis increased significantly and after that no significant differences was observed in this factor. The maximum DPPH scavenging activity, Fe3+ reducing power and hydroxyl radical scavenging activity were obtained by hydrolysis with pancreatin enzyme and after 180 minutes of hydrolysis and were 72.49%, 0.55 (adsorption at 700 nm) and 59%, respectively. The maximum total antioxidant activity of pancreatin and trypsin hydrolysates was obtained after hydrolysis at 180 minutes and there was no significant difference between them. According to the results, compared to trypsin, pancreatin enzyme showed a better performance in the production of protein hydrolysate with maximum antioxidant properties. As a result, the resulting hydrolysates, can be used in food formulation as a natural preservative and the production of functional products.

Free radicals and hydroperoxides originate from oxidation reactions could reduce food quality and also promote incidence of various diseases such as cancer. In this regard, the use of natural compounds with antioxidant properties, such as bioactive peptides, is of interest to many researchers. Demand for natural and safe antioxidants such as bioactive peptides has increased dramatically due to concerns about the safety and long-term health implications of synthetic antioxidants such as BHT and BHA. Bioactive peptides are defined as hydrolyzed proteins that, after entering the body, show potential ability to stimulate desirable and health promoting activities.

The aim of this study was to optimize the hydrolysis conditions of edible mushroom (Agaricus bisporus) powder protein with alcalase enzyme in order to produce hydrolyzed protein with potential antioxidant properties. To conduct this research, first, edible mushrooms were turned into powder after purchase from the market and conducting related processes. Then, in order to optimize the production of hydrolyzed proteins with maximum antioxidant activity using response surface methodology, the independent variables selected as time, temperature and ratio of enzyme to substrate and dependent variables was selected as the antioxidant capacity of the hydrolyzed sample (using DPPH free radical scavenging methods, iron ion reduction power and total antioxidant capacity). The temperatures used were in the range of 40-55 °C, the hydrolysis time between 30 to 210 minutes and the enzyme to substrate ratio 1 to 3%, which was optimized by the surface response methodology. In this research, Design Expert statistical software was used to apply the response level of statistical design. The statistical design was prepared with a central composite design with 20 experimental treatments that included a central point with six replications.

The obtained results showed that all the studied parameters (enzyme concentration, temperature and time of hydrolysis) had a significant effect on the antioxidant activity of the hydrolyzed product. The results showed that for the production of hydrolyzed protein of edible mushroom with high antioxidant activity (DPPH free radical scavenging methods, reducing power of Fe3+ and total antioxidant capacity) by the alcalase enzyme, the optimal conditions include temperature of 47.5 ° C, the hydrolysis time of 197 minutes and the enzyme-to-substrate ratio 2.1%, which with desirability of 100% was equal to DPPH free radical scavenging of 10.661%, reducing power of Fe3+ equal to 2.45 (absorption at 700 nm) and the total antioxidant capacity of 1.224 (absorption at 695 nm).

The results showed that by hydrolysis of protein of edible mushroom under optimal conditions a product with suitable antioxidant capacity can be obtained, which can be used as natural and functional additives in food formulations.

The present work aimed to study the effect of enzymatic hydrolysis of sarcoplastic and myofibrillar proteins from pangasius sutchi fish on the chemical compositions, the solubility, degree of hydrolysis (DH), peptide content and amino acid compositions was evaluated and their molecular weight recorded. The fish sarcoplasmic protein hydrolysates (SPHs) and myofibrillar protein hydrolysates (MPHs) were produced using three types of proteases: papain, alcalase and flavourzyme. Physicochemical properties of proteins and molecular weight were investigated. Results indicated that type of protease affected the degree of hydrolysis (DH), where all of the enzymes showed high rate of hydrolysis during the first hour, and then gradually decreased. The type of enzyme and the extent of the DH greatly influenced the amino acid residue composition and the molecular weight of the protein hydrolysates. Different amino acid composition of proteins and their hydrolysates was observed. The soluble protein and peptide content of hydrolysates significantly increased by the increase in time of incubation. The high amount of hydrophobic and aromatic amino acids in the SPH and MPH can enhance the biological activities of the peptides. Results suggest that the protein hydrolysates derived from patin may be used in functional food and supplements.

Today, special attention is paid to the use of bioactive peptides in the production of functional foods and drugs. In the present study, isolation and evaluation of bioactive properties of peptides derived from enzymatic hydrolysis of soy whey were investigated. For enzymatic hydrolysis of soy whey protein, two types of enzymes, ficin and trypsin, were used at temperatures of 37 °C and 45 °C and at times of 2 and 4 hours. Then, the obtained protein hydrolysates were separated by reverse phase- high performance liquid chromatography and the obtained fractions were collected for biological activity. Statistical analysis of hydrolysis degree results was conducted by factorial method. One-way analysis of variance was used to analyze the results of the bioactive properties of peptides. The means were compared by Duncan's multiple range test at 5% probability level. Based on the results, peptide fractions had good antioxidant activity and also showed antimicrobial effect against Escherichia coli and Staphylococcus aureus. The T4F7 fraction (the seventh fraction obtained from trypsin-prepared protein hydrolyzate at 45 °C for 4 hours) had the highest antioxidant and antimicrobial properties. Therefore, this fraction was considered as the superior fraction. Electrophoregram of separation of peptide components in the selected bioactive peptide fraction (T4F7) showd that the presence of peptides with a molecular mass often of about 5 to 10 kDa and Less than 50 kDa is the main cause of desirable antioxidant properties in this treatment. Therefore, soy whey peptide can be used as a functional ingredient and natural preservative in food products.

In this study, the effect of enzyme type (alcalase and pepsin) and process time (50-300 minutes) on the degree of hydrolysis and antioxidant indices including free radical scavenging of DPPH, ABTS, hydroxyl, reducing power, and chelating activity of Iron and copper ions were evaluated for navy bean protein (Phaseolus vulgari L.). Also, the composition of amino acids (hydrophobic and antioxidants types) and structural properties (FTIR) of primary protein and hydrolysates were investigated. The results showed that enzymatic hydrolysis improves antioxidant properties. Also, the composition of amino acids has a significant effect on antioxidant activities. On the other hand, the type of enzyme and the time of the hydrolysis process affected the degree of hydrolysis and the antioxidant activity of the hydrolysates. Thus, the highest percentage of free radicals scavenging of DPPH (82.4%), ABTS (58.3%), reducing power (0.97), hydroxyl radical scavenging (57.5%), and chelation of Fe (53.7%) and Cu ions (12.1%) were affected by the type of enzyme and process time. Among different treatments, the highest value of these indices (except copper ion chelating) was related to hydrolysates with alcalase. Structural properties of white bean protein were evaluated and enzymatic hydrolysis caused changes in the amide regions (I and II) as well as exposure to some hydrophobic-buried groups. The results of this study indicated the positive effect of enzymatic hydrolysis on the production of antioxidant hydrolysates that can be used in the food industry.

Among the beneficial compounds, bioactive peptides from enzymatic hydrolysis of proteins have many properties such as low allergenicity, lowering blood pressure, antidiabetic, anti-cancer role, natural and efficient source of antioxidants with chelating activity of metal ions and many other health benefits. Cannabis, scientifically known as Cannabis sativa L., has long played an important role in the production of dietary formulations, drugs and fiber. In this study, protein was extracted from the pulp of hemp oil. Then, the effect of time of enzymatic hydrolysis process with alkalase (60-300 min) on the degree of hydrolysis, inhibition of free radical DPPH, ABTS, inhibition of hydroxyl radical and regenerative power of hydrolyzates were investigated. Statistical evaluation of the results was performed using factorial design and comparison of means in 3 replications with one-way analysis of variance (ANOVA). The results of enzymatic hydrolysis showed an increase in the degree of hydrolysis with increasing time of enzymatic hydrolysis process. Free radical scavenging activity of DPPH, ABTS, hydroxyl and cannabis protein reducing power after enzymatic hydrolysis from 7.85 to 52.04, from 47.13 to 80.03, from 30.13 to 72.96 and from 55, respectively. Increased to 0.79%. In general, enzymatic hydrolysis of crude protein for up to 240 minutes showed a positive effect of the hydrolysis process on increasing the antioxidant properties and inhibition of free radicals.

In the present study, Antioxidant and antimicrobial activities of protein hydrolysates from viscera of Liza abu by products were investigated. Hydrolysis was performed at three different times (10, 20 and 30 min), using commercial enzyme alcalase and flaverzyme and an enzyme to substrate ratio of 1% meat protein at 50°C. The results indicated that, Protein recovery and degree of hydrolysis increased with increasing incubation time (P<0.05) and the protein hydrolysate from alcalase had the highest protein recovery and degree of hydrolysis (P<0.05). The highest antioxidant activity (DPPH radical scavenging activity, ferric reducing antioxidant power and ABTS radical scavenging activity) and the highest antimicrobial activity of protein hydrolyzed against Escherichia coli and Staphylococcus aureus were observed in protein hydrolysates with alcalase after 30 min (P<0.05). The results revealed that Liza abu by product hydrolysates have high antioxidant and antimicrobial activity, which may be useful ingredients in food and formulated diets applications.

In this study, cantaloupe seed protein (Cucumis melo var cantalupensis) were used to obtain bioactive peptides with maximum antioxidant power (DPPH radical scavenging activity and reducing power for alkalase treatment,. For this purpose, in this study, the surface response methodology and central composite design with different levels of independent variables of enzyme to substrate ratio (E / S) 0.25%-3.25% , hydrolysis time 30-210 min, temperature 30C°-55 °C  for alkalase enzyme. Optimal condition treatment obtained as enzyme to substrate ratio (E / S) 0.86, hydrolysis time 173.51 min and temperature 49.93 °C  and adjasted- R2 for DPPH radical scavenging activity were 0.80 and 0.58, respectively, and for Fe2+ reducing power were 0.96 and 0.91 (alkalase treatment), respectively. respectively, indicating that the fitted model had a relatively good description of the data distribution.  Antioxidant tests were performed using different concentrations of 50-200 ppm of the optimal treatment, and the results showed a positive effect of concentration on antioxidant properties. In all samples, hydrolyzed protein with alkalase showed higher antioxidant properties compared to, but was lower than  the antioxidant activity of ascorbic acid as a positive control. The antioxidant properties of bioactive peptides make it possible to use them as a natural alternative to common antioxidant compounds in the food industry.

In the present study, the white fish (Rutilus kutum) viscera protein was hydrolyzed by the application of different concentrations of 0.5, 1, 1.5% Alcalase and Trypsin. Chemical composition, functional properties and antioxidant activities of fish hydrolysate was then analyzed. Results of this research indicated that the fish protein hydrolysates (FPH) contain high protein content. The maximum amount of soluble protein and protein recovery was seen in hydrolyzed protein produced by 0.5 % Alcalase (76.87, 46.87%). According to the results, highest degree of hydrolysis (33.1%) was observed for 1.5 % Alcalase. The maximum rate of water holding capacity was seen in the FPH produced by 1.5% Alcalase (84.83%) and increased significantly with increasing enzyme concentration (P < 0.05). The FPHs at different concentrations showed good antioxidant properties. The highest antioxidant properties and reduction capacity were obtained by using 0.5% Alcalase (76.9, 0.8%). Good foaming and emulsifying properties were observed for fish protein hydrolysates. The current research suggested that the hydrolyzed protein from Caspian white fish viscera can be a good source of protein with high antioxidant and functional activity, that can perform acceptable emulsifying and foaming properties in food formulations.

Considering that humanity is currently facing major problems such as cardiovascular diseases, researchers have found that there is a tight relationship between nutrition and health. Thus, there are extensive studies conducted on enriching food products and beverages with a variety of salutary compounds (such as nutraceutical food) and producing functional food. The present study aimed at investigating the effect of enzymatic hydrolysis process time with alcalase and pancreatin on the functional properties of bioactive peptides derived from enzymatic hydrolysis of defatted Bunium persicum Bioss. pressed cake. The hydrolysis process was performed using alcalase and pancreatin enzymes in the ratio of enzyme to substrate (2% w/w) at different times (40-240 min). The solubility of hydrolyzed proteins derived from defatted Bunium persicum Bioss. pressed cake under acidic conditions (pH = 4- 5) was increased from about 20% to more than 60% following just hydrolysis for 40 min. Generally, by increasing the time and degree of hydrolysis, the solubility of the hydrolysates in both enzymes was significantly increased (p<0.05) at the isoelectric point of the protein. Thus, as the degree of hydrolysis was increased, the sensitivity to pH was decreased and the solubility was maintained in a wide range of pH. The emulsion activity index (ESI) and its stability were reached their maximum values following the enzymatic hydrolysis of the defatted Bunium persicum Bioss. pressed cake with pancreatin and alcalase peaked for 40 minutes under acidic pH. Considering the evaluated functional properties such as protein emulsion and foaming, the results indicated that hydrolyzed proteins for 40 minutes with alcalase have better functional properties than other treatments with pancreatin or other times.

Enzymetic modification of proteins in order to break down specific peptide bonds and protein modification is widely used in the food industry. In this research, protein of faba bean seeds was hydrolyzed using alcalase and trypsin enzymes at three concentrations (1, 2 and 3%) and reaction times of 1-6 h at optimal temperature and pH of enzymes (50 and 37 °C, pH 8.5 and 7, respectively). Hydrolysis degree, 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, and iron chelating activity of hydrolyzed proteins were investigated. The results showed that the degree of hydrolysis increased with increasing reaction time and concentration of alcalase and trypsin enzymes. The time of hydrolysis and type of enzyme has a significant effect on the degree of hydrolysis, the antioxidant and chelating activity of the faba bean protein hydrolysates (P<0.05). The proteins hydrolyzed by alcalase at concentration of 3% and reaction time of 3 h had the highest antioxidant (75.41%) and metal chelating activity (55.95%). At the 1 and 2% concentration of trypsin, the highest DPPH radical scavenging activity was observed at 4 h which was 42.38 and 53.7 %, respectively. The most metal chelating activity in trypsin hydrolyzed treatments was observed in a reaction time of 2 h, after which the activity decreased. DPPH radical scavenging and metal chelating activity increased with increasing enzyme concentration. The results showed that alcalase have more efficiency in the production of anti-oxidant peptides compared to the trypsin.