جستجوی مقالات مرتبط با کلیدواژه « پپتیدهای زیست فعال » در نشریات گروه « صنایع غذایی »

 Free radicals originate from oxidation reactions decrease 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. Food-derived bioactive peptides, can play an important role in the oxidative systems. Ultrasound, as a cheap and green technology, is widely used to extract proteins and antioxidant compounds. Ultrasound pretreatment before enzymatic hydrolysis can open the protein structure and increase the intensity of proteolysis by increasing the exposure of peptide bonds prone to enzymatic hydrolysis; which increases the production efficiency of bioactive peptides. Ultrasound treatment changes the three-dimensional structure of proteins. Therefore, a combination of pretreatment with ultrasound and sequential enzymatic hydrolysis can be a promising way to modify the function of proteins.

 In this research the effect of hydrolysis time and ultrasonic pretreatment on enzymatic hydrolysis of edible mushroom protein by pancreatic enzyme to produce peptides with high antioxidant capacity was evaluated. First edible mushroom was turned into powder and then, in order to optimize the production of hydrolyzed proteins with maximum antioxidant activity, the hydrolysis was performed 30, 60, 90, 120, 150, 180 and 210 minutes with a ratio of enzyme to substrate of 1% (based on the result of previous research) and at 40°C in four conditions (1- without ultrasound pre-treatment, 2- with ultrasound pre-treatment with 40% power, 3- with ultrasound pre-treatment with 70% power and 4- with ultrasound pre-treatment with 100% power) by ultrasound probe in 5 minutes before adding the enzyme. In the next step, the antioxidant capacity of hydrolyzed proteins was measured at different times by DPPH free radical scavenging activity, iron ion reduction power, iron ion chelation and total antioxidant capacity.

 The results showed that the highest DPPH free radical scavenging activity in untreated and treated samples with 40, 70 and 100% ultrasound power were 69.1, 77.45, 79.07 and 80.27, respectively. In most of the hydrolysis times, DPPH free radical scavenging activity in ultrasound treatment with 100% power was higher than the samples treated with 40 and 70% power. The highest total antioxidant capacity in untreated and treated samples with 40, 70 and 100% ultrasound power were 0.871, 1.025, 1.05 and 1.2 (absorption at 695 nm), respectively. In most of the hydrolysis times, the total antioxidant capacity in the samples treated with ultrasound with 100% power was higher than the samples treated with 40 and 70% power. The results showed that the highest reducing power of Fe3+ in untreated and treated samples with 40, 70 and 100% ultrasound power were 2.03, 2.40, 2.44 and 2.51(absorption at 700 nm), respectively. The highest iron ion chelation power in untreated and treated samples with 40, 70 and 100% ultrasound power were 25.22, 30.40, 26.52 and 41.10%, respectively. By increasing the ultrasound power in most of the hydrolysis times, the chelating power of iron ions in the ultrasound treatment with 100% power was higher than the samples pretreated with 40 and 70% power. The results showed that samples pretreated with 100% power ultrasound have the highest antioxidant properties compared to samples without pretreatment and pretreated with 40% and 70% ultrasound power. Based on the results, using ultrasound treatment with 100% power and during hydrolysis time of 60 minutes, a product with high antioxidant capacity was obtained and selected as a suitable treatment.

 The ultrasonic mechanism is attributed to its thermal effects, cavitation and mechanical efficiency, so that it can increase the mass transfer and increase the contact between the substrate and the enzyme or change the spatial structure of the substrate. The results showed that samples pretreated with ultrasound with 100% power have the highest antioxidant properties compared to samples without pretreatment and pretreated with 40 and 70% power. Therefore, the use of high-power ultrasonic pretreatment shortens the hydrolysis time to achieve peptides with higher antioxidant capacity and thus increases the efficiency of enzymatic hydrolysis.

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.

Given the concerns regarding the use of synthetic antioxidants in the food industry, it seems necessary to identify and use substances containing natural antioxidants. Protein-containing wastes are one of these substances from which antioxidant compounds can be extracted in various ways. The aim of this study was to compare and comprehensively evaluate the antioxidant activity of bioactive peptides produced from three sources of waste including fish (FPH), poultry (PPH) and shrimp (SPH) with flavourzyme enzyme. Therefore, post-production bioactive peptides from these three sources were compared in term of all common and uncommon antioxidant tests in the food industry. The results showed that the peptides produced from these three sources (with the same enzyme and degree of hydrolysis) were different in terms of antioxidant activity. In free radical scavenging activity tests of DPPH and ABTS, linoleic acid peroxidation inhibition and metal chelating power, SPH was significantly higher than the other two proteins (p<0.05). The values of these four indices in SPH were measured 87.45±1.38%, 79.26±0.59%, 94.56±1.62%, and 71.49±0.37 %, respectively. There was no significant difference between SPH and FPH regarding ferric ion reducing power and hydroxyl free radical scavenging activity (p>0.05). Also, FPH and PPH did not show significant differences in terms of ABTS free radical scavenging activity index (69.15±0.85% and 68.44±1.93% respectively). In general, based on the results of the tests, in the present study, bioactive peptides produced from shrimp wastes (SPH) had the highest antioxidant activity. Peptides from fish wastes hydrolysis (FPH) was ranked second. In almost all tests, the lowest antioxidant activity was related to poultry wastes peptides (PPH).

The aim of this study was to investigate the effect of probiotic bacteria and trypsin enzyme on the physicochemical, microbial and sensory properties of dough. For this purpose, bioactive peptides of 1.5 and 3 mg /100 ml were added to the probiotic dough formulation, which were inoculated separately with 108 cfu / ml of Lactobacillus acidophilus and Lactobacillus helveticus. PH tests, mold and yeast counts, coliform counting, probiotic bacterial survival, antioxidant activity evaluation, gamma amino butyric acid measurement and sensory evaluation were performed on dough. The results showed that the use of probiotic bacteria with trypsin enzyme and increasing its concentration was maintained viability increase, probiotic bacteria, antioxidant properties, GABA production rate, and sensory evaluation score after 60 days. It also reduced pH, mold and coliforms in dough. Using Lactobacillus acidophilus and the enzyme trypsin 3 mg / 100 ml can produce high-yielding dough containing GABA with lower microbial load and higher antioxidant and sensory properties.

Food is considered not only as a source of energy and essential ingredients for growth and health but also as a source of bioactive compounds that can have beneficial effects in humans. Bioactive peptides are considered to be functional compounds that have been recognized in foods recently. An enzymatic hydrolysis has been used to improve the functional properties of plant proteins. One of the features of the protein hydrolysates is their antioxidant activity, which makes it possible to use them as antioxidant agents in food models. In this study, the effect of using different enzymes and their combination in production of protein hydrolysates with high functional and antioxidant properties was investigated.

Faba bean protein isolate was enzymatically hydrolyzed by trypsin and alcalase alone, and in a successive way with trypsin and alcalase at concentrations of 1.5 and 3%, and optimum temperature of 37 and 50 °C and pH of 7 and 8.5 respectively all at the reaction time of 3h. The solubility parameters at pH 2-12, foaming and foam stability at the pH level of 4, 6, 8 and 10, DPPH radical scavenging activity, and iron chelating activity of protein hydrolysates were investigated.

The results showed that enzymatic hydrolysis increased the solubility, especially in acidic pH range. At pH 3, the protein hydrolysates derived from alcalase and the combination of trypsin and alcalase enzymes at the concentration of 3% had the highest solubility (64.51% and 60.95% respectively). Foaming capacity increased with increasing of pH from 4 to 8. The highest foaming capacity was observed at pH level of 8, but at pH level of 10, in all samples, foaming capacity decreased. Protein isolate at pH level of 4 created no foam after 60 minutes. The highest foam stability was observed at pH level of 8 in all samples. The results also showed that hydrolysis of faba bean protein significantly increased the foaming stability (p < 0.05). At pH level of 8, samples that hydrolyzed with trypsin and combination of trypsin-alcalase enzymes at the concentration of 3% had the highest foam stability. The enzymatic hydrolysis significantly increased the DPPH radical scavenging activity (p < 0.05). Maximum DPPH radical scavenging activity was observed in the alcalase treated hydrolysates (75.71%), which had a significant difference with other protein hydrolysates (p < 0.05). There was no significant difference in the DPPH radical scavenging activity of trypsin treated protein hydrolysates, and trypsin-alcalase combinations with concentrations of 1.5 and 3% which were 72.54, 73.66 and 73.62% respectively (P>0.05). The enzymatic hydrolysis significantly increased the iron chelating activity compared to the faba bean protein isolate (P <0.05).

The results showed that different enzymes under constant hydrolysis conditions have different effects on a single substrate. Enzymatic modification of proteins creates a natural antioxidant source in food models, which can increase the shelf life of products.

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.

Proteins are being hydrolyzed to generate various properties such as antioxidant activity and nutritional values. Enzymatic hydrolysis is carried out in milder condition and is more controllable. The produced protein hydrolysates’ properties are dependent to the hydrolysis condition. So by optimizing the hydrolysis conditions, proteins with higher antioxidant abilities are achieved. Response surface method is a statistical way to optimize and model the process more efficiently. The aim of present study was to optimize and model the hydrolysis condition to produce and antioxidant protein hydrolysate with high nutritional value   from Cajanus cajan by pepsin.

First, Cajanus cajan’s proteins solubility was measured. After reaching the pHs with the most and least solubility, protein extraction was carries out by using NaOH and HCl. Enzyme concentration (1, 2, 3%), temperature (30, 35, 40 °C) and time (2, 3.5, 5 h) as independent variables were given to the Design Expert software and protein hydrolysis was done in a shaker incubator according to the 20 treatments suggested by the software. 1, 1- diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, hydroxyl radical scavenging activity, Reducing power and total antioxidant activity were measured as dependent variables. Antioxidant assays were modeled by the software and the optimum condition was evaluated. The obtained optimum condition was validated by repeating the antioxidant assays for the protein hydrolysate produced in the optimum condition. The amino acid profile of the protein hydrolysate was measured using HPLC-MS and chemical score was measures. Then, the molecular weight distribution of the protein concentrate and protein hydrolysate was evaluated by FPLC. Chemical composition of the samples was also measured.

The optimum condition for achieving antioxidant protein hydrolysate was enzyme concentration 2.15%, temperature 39.99 °C and time 4.52 h. Model validation results for this point were including DPPH scavenging activity 58.49%, reducing power 0.31 nm, hydroxyl radical scavenging activity 38.2% and total antioxidant capacity 0.63 nm. The protein concentrate consisted of 215.84 mg/g hydrophobic and 57.04 mg/g of them were aromatic amino acids. These amino acids are responsible for antioxidant activity of the protein hydrolysates. Chemical scores for essential amino acids were good. Most of the peptides in the protein hydrolysate had molecular weights below 10 kD that is considered to have antioxidant activities. Hydrolysis also increased the protein and ash content while fat and water content decreased compared to the Cajanus cajan’s flour and protein concentrate. Results showed that Cajanus cajan’s protein hydrolysate can be a good source of antioxidants and play a positive role in human nutrition.

Bioactive peptides are organic substances composed of amino acids, which are linked by covalent bonds, are known as peptide bonds or amide bonds. Although some of these peptides are free in natural products, but many of them are encrypted in the primary protein structures that are released through enzymatic processes. The aim of this study was to evaluate the physicochemical and functional properties of hydrolyzed protein derived from cottonseed meal by alcalase enzyme. The enzyme hydrolysis was investigated with alcalase enzyme at constant pH equal to 8, different time interval (2, 3.5 and 5 hours), temperature (45, 50 and 55 °C) and enzyme/ substrate ratio (0.5, 1.5 and 2 %). Optimization of enzyme hydrolysis was performed by surface response method. In optimal conditions, some of the hydrolyzed protein features including antioxidant activity of hydrolyzed proteins derived from cottonseed meal, including free radical DPPH inhibiting, iron ion fermentation strength, capacity total antioxidants and regenerative effects were investigated. The results of this study show that with a degree of hydrolysis 32%. The optimal hydrolysis conditions for cottonseed meal protein were 5 hours, 55 °C and the ratio of enzyme to the substrate 1.7%, In these conditions, the optimum amount of free radical inhibitory activity DPPH was 62.69%, total antioxidant capacity was 2.1 mmol α-tocopherol/mL, regenerative capacity equaled 0.078%, and chelating capacity was 80.20%. The bioactive peptides derived from cottonseed meal have physicochemical and functional properties. The response surface method was also used as an easy, reliable and available method to optimize protein hydrolysis and was effective in achieving desirable health features. Therefore, the use of cottonseed hydrolyzed proteins is recommended in some of food and medicinal formulations.

Bee pollen, commonly referred as the ‘‘life-giving dust’’, results from the agglutination of flower pollens with nectar using salivary substances of the honeybees (Almeida-Muradian et al., 2005). Pollen contains 10 to 40% protein, 1 to 13% lipid, 13 to 55% carbohydrates and 2 to 6% minerals. Royal Jelly is produced by enzymatic digesting of bee pollen by proteases and other natural enzymes. Based on dry weight, it contains 27-41% protein, 30% carbohydrates, 8-19% lipids, minerals, trace elements and some vitamins (Sabatini et al., 2009; Wytrychowski et al., 2013). The antioxidant properties of royal jelly and bee pollen, are related to main proteins and phenolic compounds and flavonoids (Nagai and Inue, 2004). The antioxidant activity of peptides can be evaluated using DPPH, radicals scavenging activity, Ferric reducing, Ferrous chelating activity (Khantaphant et al., 2011). Antioxidant and ACE inhibitory activity of pollen, royal jelly and peptides were investigated by different researchers (Bogdanov, 2014; Morais et al., 2011; Salampessy et al., 2015; Marinova and Tchorbanov, 2010; Wiriyaphan et al., 2012). The objective of present research was optimization of enzymatic hydrolysis of bee pollen protein by Alcalase according to its antioxidant and ACE inhibitory activity compared to royal jelly.
The preparation of the bee pollen extract was performed by mixing the bee pollen with water (1:10) (w/v). The macerates were filtered and centrifuged at 12000 g. The obtained supernatant was lyophilized. The royal jelly extract were prepared using method described by Liu et al., 2008. The total phenolic content of the extracts was recorded using the Folin–Ciocalteu method (Moreira et al., 2008). DPPH radical-scavenging activity was determined as described by Bersuder, Hole, and Smith (1998). The ability of the hydrolysate to reduce iron (III) was determined according to the method of Bougatef et al. (2008). Bee pollen was added and homogenized with 5 volumes of distilled water. pH and temperature of the solution were adjusted to pH=8 and 50◦C. Alcalase in the concentration range of 1 to 2% w/w were added to the pollen protein solution. Enzymatic hydrolysis performed during different times 2 to 5 hours. Hydrolysis was stopped by heating at 80˚C for 10 min. The hydrolysats were centrifuged at 4000x g for 30 min to remove the residue. The supernatants were pooled and then lyophilized (Matsuoka et al., 2012). DPPH radical scavenging ability and reducing power of pollen hydrolysates of pollen hydrolysates were measured. Also ACE-inhibitory activity of pollen hydrolysates was measured was assayed by method reported by Nakamura et al. (1995). Statistical analysis of results before hydrolysis was done by SPSS. Optimization of enzymatic hydrolysis was done by Response Surface Methodology (RSM) in Design Expert software.
Total phenol value measured for pollen ranged between 48.15 to 174 mg Gallic acid/g for royal jelly ranged from 9.24 to 87.261 mg Gallic acid/g. Considering that royal jelly is obtained by direct digestion of pollen, the amounts of their phenolic compounds were comparable (Bogdanov, 2014). Phenolic compounds increased by increasing concentration royal jelly and pollen extract in dose dependent manner. Increasing concentrations of royal jelly in range of 300 to 1000 mg/l was more effective than pollen (p

In this study antioxidant activity, protection of mice sperm’s DNA from oxidative damage resulting from hydroxyl radicals and anti-hyperglycemic capacity of Iranian traditional fermented fish sauce made from sardine (mahyaveh) was determined. The traditional fish sauce exhibited high antioxidant activity in scavenging ABTS and hydroxyl free radical with IC50 values of 179 and 147 µg/mL as well as ferric reducing antioxidant power (FRAP). The traditional product effectively inhibited mice sperm’s DNA from oxidation induced by hydroxyl radicals as evidenced by lowering the formation of single stranded DNA with the coincidental higher viability in sperm cells (P

Bee pollen, results from the agglutination of flower pollens with nectar and salivary substances of the honeybees. Honey bees save the pollen in the pollen bag at the third clause of their legs. At the entrance to the hive, pollen is trapped in pollen trap and beekeeper collects it. One of the functional properties of bee pollen is antioxidant activity due to its proteins and phenolic compounds. In this study, effect of enzymatic hydrolysis of bee pollen’s proteins on its anti-oxidative activity and optimization of hydrolysis conditions was evaluated. In this regard, phenolic compounds, DPPH free radical scavenging activity, ferric ion reducing power and ferrous ion chelating properties of pollen were measured (respectively 4.1 µg/ 100 g, 31.86%, 1.89, 4.9). Bee pollens hydrolyzed by Alcalase at 2 to 5 hours and concentration of 1to 2%. Treatments determined by RSM. Anti-oxidative factors of hydrolyzed pollen were evaluated. Results showed that maximum amount of reducing power of hydrolyzed pollen received at 2 hours by enzyme concentration of 2%. Maximum amount chelating activity was 31.71% received at 1.38 hours of hydrolysis; effect of enzyme concentration on chelating activity was insignificant. Maximum amount of DPPH free radical scavenging activity received at 2-3.5 hours and enzyme concentration of 1-1.5%. Chelating and DPPH free radical scavenging activities of bee pollen increased to respectively 26% and 23.65% after hydrolyzing.

Despite all the progresses made in the field of pest control, bug is yet the hazardous pest in Iran. This insect injects a salivary proteinase into immature wheat kernels resulting in poor rheological properties, which leads to having bread with low volume and unacceptable texture. On the other hand, protein hydrolysis of gluten can improve the functional properties and also body physiological mechanisms according to producing bioactive peptides. In this study wheat samples with variable proportion of bug-infested grains (25, 50, 75 and 100%) were initially prepared and then qualitative, functional and bioactive tests were performed to evaluate the effect of suni-bug damage. Results showed that Zeleny sedimentation value decreased by increasing bug damage in samples indicating low quality in gluten for bread making. On the other hand, by increasing proportion of bug damage, degree of hydrolysis increased and functional properties of wheat samples such as solubility and emulsifying capacity were improved. By increasing the degree of hydrolysis, protein solubility also increased and the highest emulsifying capacity was observed in 25% suni-bug wheat sample. The results of evaluating bioactive properties in wheat samples indicated that by increasing the degree of bug attack, producing short peptides with ACE inhibitory and antioxidant activity increased, therefore the highest percentage of ACE inhibition and antioxidant ability is observed in 100% suni-bug damaged sample whereas the lowest was evidenced in the sound wheat sample.