Antioxidant Properties Of Protein Hydrolysates Research Articles

Research of the properties of protein hydrolysates obtained from the broiler chicken gizzards as a potential component of bioactive film coatings

Protein hydrolysates are a promising active component in the production of bioactive film coatings for food products. Some biopolymers can exert the biological activity. More often, however, it is necessary to select biologically active substances to impart these properties to films. On the other hand, not all components allow forming films with the required properties, and therefore there is a need to study the individual technological characteristics of the components used. The purpose of the research is to establish the antioxidant and technological properties of protein hydrolysates obtained by microbial fermenta- tion of poultry by-products in whey with bifidobacteria, propionic acid bacteria and acidophilic bacteria as a potential basis for bioactive film coatings of food products. The hydrolysate obtained by fermentation without the addition of the specified bacterial species was used as a control sample. The functional properties of protein hydrolysates were assessed: antioxidant capacity by coulometric titration on an Expert-006 coulometer using ascorbic acid as a standard, antiradical activity by the DPPH method on a Jenway 6405 UV/Vis spectrophotometer with determination of the IC50 value. The technological proper- ties, solubility, water-holding, fat-holding and fat-emulsifying capacities were also determined by the gravimetric method. In addition, the average hydrodynamic diameter of particles in protein hydrolysates was determined using a Microtrac FLEX particle size analyzer. The results of studies of the antioxidant properties showed that the DPPH antiradical activity was 14.7% higher in the experimental samples of hydrolysates obtained by fermentation with bifidobacteria compared to the control; samples of hydrolysates obtained by fermentation with propionic acid bacteria showed an antioxidant capacity 29.6% higher than that of the control sample. The IC50 value turned out to be the highest in the control hydrolysate sample (2.994 mg/ml), which was 45.5–53.3% higher than that in the experimental hydrolysate samples. The results of determining the technologi- cal properties showed that they differ significantly for protein hydrolysates obtained by fermentation with different types of bacteria. For example, the highest values of fat-holding and fat-emulsifying capacities were found in the hydrolysate obtained by fermentation with bifidobacteria (351.1% and 61%, respectively), which shows its potential for incorporation into the bio- composite in the form of a protein-oil emulsion. The high solubility of the experimental samples of hydrolysates (from 90.1 to 91.4%) suggests their uniform distribution in the aqueous phase when composing the biocomposite of the film. Thus, the research results have shown the prospects of using protein hydrolysates from the gizzards of broiler chickens in whey as an active component of bioactive film coatings. The antioxidant properties of protein hydrolysates allow slowing down oxidative processes in the main food nutrients, which will contribute to an increase in the shelf life of food products packaged in bioac- tive films with this component.

Protein hydrolysates from Mytilus edulis L. mussel: Physicochemical and antioxidant properties

Meat of marine molluscs is a promising protein-containing raw material for obtaining protein hydrolysate and biologically active peptides. The purpose of this research was to study the physicochemical properties and antioxidant properties of protein hydrolysate obtained from the mussel Mytilus edulis L. The hydrolysates were obtained by acidic hydrolysis and enzymatic hydrolysis using protozyme as an enzyme. Gel permeation chromatography was used as experimental method in this study to characterise the molecular weight distribution of the protein hydrolysates. Chemical analysis was used for determine the composition and antioxidant activity of hydrolysates. It is shown that the content of low-molecular fractions - biologically active peptides with a molecular weight of less than 5 kDa is almost three times higher in the enzymatic hydrolysate compared to the acidic one. Accordingly, the enzymatic hydrolysate demonstrates high antioxidant activity, which determines its prospects as a component for functional food products and biomedical drugs.

Effects of peptide fractions and amino acids on antioxidant properties of autolyzed tuna viscera protein hydrolysate

Tuna viscera as a common waste product from the tuna processing industry contributes to environmental pollution. The effects were determined of peptide fractions and amino acids on the antioxidant properties of protein hydrolysate from tuna viscera. We converted this waste into protein hydrolysate, a high added-value product, using autolysis. Tuna protein hydrolysate was fractionated by ultrafiltration into four fractions (>10 kDa, 5–10 kDa, 1–5 kDa and <1 kDa) and each was examined for its antioxidant properties (DPPH, ABTS, FRAP and metal chelating) and amino acids composition. The MW and amino acids of the tuna protein hydrolysate peptide fractions were not directly correlated with DPPH radical scavenging activity and metal chelating. The ABTS radical scavenging activity and ferric reducing antioxidant power (FRAP) of the 1–5 kDa fraction were higher than for the other fractions. The tuna protein hydrolysate peptide fractions contributed to antioxidant activity and should be used to their full advantage by the nutritional and food industries

Impact of Enzymatic Hydrolysis Using Two Proteases on Functional, Structural, and Antioxidant Properties of Protein Hydrolysates Derived from Fresh and Microwave-dried Substrates of Bighead Carp (Hypophthalmichthys Nobilis)

Impact of Enzymatic Hydrolysis Using Two Proteases on Functional, Structural, and Antioxidant Properties of Protein Hydrolysates Derived from Fresh and Microwave-dried Substrates of Bighead Carp (Hypophthalmichthys Nobilis)

Ultrasound-Assisted Extraction of Artocarpus heterophyllus L. Leaf Protein Concentrate: Solubility, Foaming, Emulsifying, and Antioxidant Properties of Protein Hydrolysates

The impact of ultrasound-assisted extraction (UAE) was evaluated on the functionality of jackfruit leaf protein hydrolysates. Leaf protein concentrate was obtained by ultrasound (LPCU) and conventional extractions by maceration (LPCM). LPCM and LPCU were hydrolyzed with pancreatin (180 min), and hydrolysates by maceration (HM) and ultrasound (HU) were obtained. The composition of amino acids, techno-functional (solubility, foaming, and emulsifying properties), and antioxidant properties of the hydrolysates were evaluated. A higher amount of essential amino acids was found in HU, while HM showed a higher content of hydrophobic amino acids. LPCs exhibited low solubility (0.97–2.89%). However, HM (67.8 ± 0.98) and HU (77.39 ± 0.43) reached maximum solubility at pH 6.0. The foaming and emulsifying properties of the hydrolysates were improved when LPC was obtained by UAE. The IC50 of LPCs could not be quantified. However, HU (0.29 ± 0.01 mg/mL) showed lower IC50 than HM (0.32 ± 0.01 mg/mL). The results reflect that the extraction method had a significant (p < 0.05) effect on the functionality of protein hydrolysates. The UAE is a suitable method for enhancing of quality, techno-functionality, and antioxidant properties of LPC.

Influence of Degree of Hydrolysis on Chemical Composition, Functional Properties, and Antioxidant Activities of Chinese Sturgeon (Acipenser sinensis) Hydrolysates Obtained by Using Alcalase 2.4L

ABSTRACTProtein hydrolysates from Chinese sturgeon were prepared using Alcalase 2.4L enzyme. Under the optimum conditions (enzyme–substrate ratio of 3.5%, pH of 8.5, and temperature of 55°C), the degree of hydrolysis (DH) was 13.8%, 16.7%, and 19.1% after 1, 3, and 6 h, respectively. The contents of crude protein and amino acid increased at DH of 19.1% to 86.97% and 78.29%, respectively. There was an obvious increase in the low-molecular-weight peptides, which could enhance the hydrolysate’s functional properties such as solubility, representing more than 90% at different pH levels. The obtained protein hydrolysates revealed good emulsification properties and high oil absorption. Furthermore, good antioxidant activities such as 1, 1-diphenyl-2-picrylhydrazyl (DPPH) inhibition, ferric reducing power, and ferrous ion (Fe2+) chelating ability were attained depending on the solution concentration. The findings indicate that the functional and antioxidant properties of protein hydrolysates could be useful in many applications of the food industry.

Functional and antioxidant properties of protein hydrolysates obtained from white shrimp (Litopenaeus vannamei).

Protein hydrolysates from white shrimp (Litopenaeus vannamei) with different degrees of hydrolysis (DH-10 and 20%) were prepared using the enzymes Alcalase 2.4L and Protamex. The hydrolysates were evaluated for amino acid composition, solubility, foaming properties, emulsifying and antioxidant activity. All the hydrolysates showed high concentrations of Glutamic Acid, Aspartic acid, Arginine, Glycine, Lysine, Proline. It was found that the increase in the production of negatively charged amino acids was related to increase in DH. The hydrophobic amino acids were higher for hydrolysates obtained with Alcalase (10% DH) and Protamex (20% DH). The results indicated that higher degree of hydrolysis showed positive relation with the protein solubility of the hydrolysates, while negatively influenced foam and emulsification properties. The antioxidant properties presented by the white shrimp protein hydrolysates were influenced by the composition and peptides size. Hydrolysates with higher peptide chain showed the highest antioxidant power for the 2,2-Diphenyl-1-picrylhydrazyl radical scavenging and reducing power, while hydrolysates with lower peptide chain showed higher antioxidant power for 2,2'-azinobis (3-ethylbenzothiazoline sulfonic acid) radical scavenging. All hydrolysates showed dose-dependent antioxidant activities. Therefore, the results of the present study suggest that white shrimp is a potential source of protein hydrolysates as bioactive ingredients for the use in the formulation of functional foods as well as natural antioxidants in lipid food systems.

Antioxidant properties of protein hydrolysate from Douchi by membrane ultrafiltration

ABSTRACTProtein extracted from Douchi was hydrolyzed by alcalase based on a single-factor experiment and response surface methodology was employed to optimize hydrolysis conditions. The optimum conditions were determined to be: 63℃ extraction temperature, 1.4% quantities of enzyme and substrate, and 1.7 h extraction time. The optimal protein hydrolysate was subsequently subjected to ultrafiltration, and the fraction of molecular weight 10–50 kDa was identified as the most potent contributor to antioxidant activity. Amino acid analysis indicated that acidic amino acids were the most abundant in all fractions of the protein hydrolysate. Infrared spectroscopy showed there were no significant differences in secondary structure between fractions.

Compositions and antioxidant properties of protein hydrolysates from the skins of four carp species

SummaryCompositions and antioxidant properties of protein hydrolysates prepared from four carp skins: black carp, grass carp, silver carp and bighead carp, using pepsin, with a degree of hydrolysis (DH) of 6–15%, were investigated. The yield of freeze‐dried hydrolysates was in the range of 54–62 g/100 g (dry skin). The content of protein and ash in four freeze‐dried hydrolysates was 72–81% and 8–17%, respectively. All hydrolysates contained high amount of hydrophobic amino acid residues (389–480 residues/1000 residues). Meanwhile, their antioxidant properties were evaluated by in vitro assays. The results revealed that all hydrolysates possessed potent antioxidant activities and showed dose dependency as the activity increased with sample concentration, capable of scavenging 72–88% of DPPH and 61–69% of hydroxyl radicals, respectively, at the highest tested concentration. The hydrolysates exhibited high reducing power and β‐carotene–linoleic acid oxidation inhibition. Among the four hydrolysates, the hydrolysate derived from bighead carp skin was superior to others in terms of yield, DH and antioxidant activities.

Protease fromAspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

This study reports the biochemical characterization of a protease fromAspergillus oryzaeLBA 01 and the study of the antioxidant properties of protein hydrolysates produced with this protease. The biochemical characterization showed that the enzyme was most active over the pH range 5.0–5.5 and was stable from pH 4.5 to 5.5. The optimum temperature range for activity was 55–60°C, and the enzyme was stable at temperatures below 45°C. The activation energy (Ea) for azocasein hydrolysis and temperature quotient (Q10) were found to be 37.98 kJ mol−1and 1.64–1.53 at temperature range from 30 to 55°C, respectively. The enzyme exhibitedt1/2of 97.63 min and aDvalue of 324.31 at the optimum temperature for activity (57.2°C). Protease fromA. oryzaeLBA 01 was shown as a potentially useful biocatalyst for protein hydrolysis, increasing the antioxidant activities of soy protein isolate, bovine whey protein, and egg white protein from 2.0- to 10.0-fold.

Antioxidant Properties of Protein Hydrolysate Obtained from Oyster Saccostrea cucullata (Born, 1778)

The antioxidant activities of enzymatically hydrolyzed (protease from Bacillus cereus SU12) oyster (Saccostrea cucullata) protein were studied. The hydrolysate exhibited a strong antioxidant potential in 1, 1-diphenyl-2-picrylhydrazyl (DPPH, 85.7 ± 0.37%), followed by hydrogen peroxide radical scavenging activity (81.6 ± 0.3%), hydroxyl radical scavenging activity (79.32 ± 0.6%), and reducing power assay (2.63 ± 0.2 OD at 700 nm) at a concentration of 1 mg/mL. Due to the high antioxidant potential, the hydrolysate was purified in Sephadex G-25 gel filtration chromatography. The active peptide fraction was identified by DPPH and reducing power assay. The amino acid content of the purified active peptide fraction was analyzed by high performance liquid chromatography. The active fraction contained a good quantity of both essential and nonessential amino acids. The present study revealed that oyster (S. cucullata) protein hydrolysate is a potential source for natural antioxidants.

Fermentative recovery of lipids and proteins from freshwater fish head waste with reference to antimicrobial and antioxidant properties of protein hydrolysate.

Effectiveness of fermentation using lactic acid bacteria (LAB) for recovering lipids and proteins simultaneously from freshwater fish head (FWH) was evaluated. Three different proteolytic LAB (Pediococcus acidilactici NCIM5368, Enterococcus faecium NCIM5335 and Pediococcus acidilactici FD3) isolated from fish processing wastes were employed in the fermentation process. The fermentation conditions involved 10% (w/w) glucose, 2% (w/w) NaCl and 10% (v/w) LAB cultures at 37°C. The process resulted in 38.4% of degree of hydrolysis (in case proteins) and a recovery of 63.6% of the oil present in the material. The fermentation process did not affect the fatty acid profile of lipids. The hydrolyzed protein rich fermentation liquor exhibited DPPH radical scavenging activity (EC50 - 5.1mg protein) as well as antagonistic properties towards several bacterial and fungal pathogens. The minimum inhibitory concentrations (MIC) of fermentated liquor (with E. faecium NCIM5335 as starter) were 10 and 12mg/ml for Listeria monocytogenes and Salmonella itridicus, respectively. A higher MIC (60 and 96mg/ml for Aspergillus ochraceus and Penicillium chrysogenum, respectively) was observed in case of fungal pathogens. Both the oil and protein hydrolysate rich liquor from fish head can be used as biofunctional ingredients in both human food as well as livestock feed formulations.

Nutritional composition and antioxidant properties of protein hydrolysates prepared from echinoderm byproducts

SummaryProtein hydrolysates were prepared from echinoderm byproducts, including viscera (SCV) of Atlantic sea cucumber (Cucumaria frondosa) and digestive tract (UDT) and non‐commercial grade gonads (UGN) of green sea urchin (Strongylocentrotus droebachiensis). Enzymatic hydrolysis was performed on defatted materials using Alcalase® 2.4L (0.75% w/w) and reaction was carried out overnight (∼16 h, 55 °C, pH 8.0). Freeze‐dried hydrolysates were analysed for their nutritional composition, nitrogen solubility index and antioxidant activity. Degree of hydrolysis was low, with values of 5.6%, 4.6% and 7.0% for SCV, UDT and UGN, respectively. Hydrolysates showed high protein content (∼55%), high proportion of essential amino acids (∼35% of total amino acids) and good solubility (nitrogen solubility index ≈ 68%). They contained variable concentrations of major and trace elements with a predominance of Na and K. Hydrolysates showed apparent antioxidant activities in both ORAC assay (267–421 μmol TE g−1) and inhibition of lipid oxidation test (54–57%). Antioxidant activities were thought to be associated with the presence of antioxidant peptides in hydrolysates. Our results showed that hydrolysates from Atlantic sea cucumber and green sea urchin byproducts might serve as alternative sources of dietary proteins, with good nutritional composition, high solubility and interesting protection against oxidative stress.