Antioxidant Activity Of Protein Hydrolysates Research Articles

Investigation of Antioxidant Activity of Protein Hydrolysates from New Zealand Commercial Low-Grade Fish Roes.

The objective of this study was to investigate the nutrient composition of low-grade New Zealand commercial fish (Gemfish and Hoki) roe and to investigate the effects of delipidation and freeze-drying processes on roe hydrolysis and antioxidant activities of their protein hydrolysates. Enzymatic hydrolysis of the Hoki and Gemfish roe homogenates was carried out using three commercial proteases: Alcalase, bacterial protease HT, and fungal protease FP-II. The protein and lipid contents of Gemfish and Hoki roes were 23.8% and 7.6%; and 17.9% and 10.1%, respectively. The lipid fraction consisted mainly of monounsaturated fatty acid (MUFA) in both Gemfish roe (41.5%) and Hoki roe (40.2%), and docosahexaenoic (DHA) was the dominant polyunsaturated fatty acid (PUFA) in Gemfish roe (21.4%) and Hoki roe (18.6%). Phosphatidylcholine was the main phospholipid in Gemfish roe (34.6%) and Hoki roe (28.7%). Alcalase achieved the most extensive hydrolysis, and its hydrolysate displayed the highest 2,2-dipheny1-1-picrylhydrazyl (DPPH)˙ and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities and ferric reducing antioxidant power (FRAP). The combination of defatting and freeze-drying treatments reduced DPPH˙ scavenging activity (by 38%), ABTS˙ scavenging activity (by 40%) and ferric (Fe3+) reducing power by18% (p < 0.05). These findings indicate that pre-processing treatments of delipidation and freeze-drying could negatively impact the effectiveness of enzymatic hydrolysis in extracting valuable compounds from low grade roe.

Preservation by ionic gelation encapsulation of the antioxidant activity of protein hydrolysate derived from Lionfish (Pterois volitans, L.) muscle proteins.

The ionic gelation for preserving the antioxidant activity of the protein hydrolysate from encapsulated lionfish (Pterois volitans, L.) muscle was evaluated. A 22 factorial design was used. The factors evaluated were sodium alginate concentration (1.75% and 3.5% w/v) and calcium chloride concentration (3% and 5% w/v). The response variables were encapsulation efficiency and preservation of antioxidant activity. The beads obtained were classified as microcapsules (2-3mm) and were mostly spherical, with a weight ranging from 12 to 38mg. Encapsulation efficiency ranged from 37 to 55.47%, while the preservation of antioxidant activity ranged from 43.3 to 64.5%. The best treatment for preserving the in vitro antioxidant activity of the protein hydrolysate was the one with 1.75% w/v sodium alginate and 3% w/v calcium chloride, which showed an encapsulation efficiency of 53.96%, preservation of antioxidant activity of 64.5%, and free radical scavenging (DPPH) of 22.73%.

The Antioxidant Protective Effect of Iris-Squid-Derived Protein Hydrolysates (&gt;10 kDa) in HSF Fibroblast Cells Induced by H2O2

One of the supporting factors behind the biomolecules recently used in anti-aging and skin nourishment is their antioxidant properties. Hydrogen peroxide (H2O2) is a well-known small molecule oxidant that induces apoptosis in human skin fibroblast (HSF) cells through the synthesis of inflammatory cytokines. Hence, this study aimed to investigate the antioxidant activities of protein hydrolysates prepared from Iris squid (Symplectoteuthis oualaniensis) (PHCSO) in vitro. Firstly, two peptides with MWs more than 10 kDa (PHCSO-1) and less than 10 kDa (PHCSO-2) were obtained through ultrafiltration and were characterized (molecular pattern amino acid composition, FTIR) before testing the antioxidant activity (DPPH radical scavenging activity and hydroxyl radical scavenging activity). Then, the effects of PHCSOs on HSF cell viability, H2O2-induced oxidative stress model of HSF cells, ROS fluorescence staining, level of cytokines (IL-1, IL-6 and TNF-α) and cellular antioxidant properties (SOD activity, CAT activity, GSH and MDA content) were investigated. The cell morphology was examined through fluorescence staining and inflammatory factors and antioxidant activity analysis showed that superior properties were observed in PHCSO-2 peptide compared to PHCSO-1 and PHCSO. Among the peptides, PHCSO-2 (5 mg/mL) had higher DPPH and hydroxyl radical scavenging activities of 58% and 57%, respectively. On the other hand, the PHCSO-2 treatment reduced the TNF-α activity by 25%, which indicated the effective protection of PHCSO-2 from oxidative stress damage in the skin. These findings proved that peptides with less than 10 kDa were more suitable for therapeutic purposes, with good antioxidant properties. Accordingly, the protein hydrolysate from S. oualaniensis proved to be an excellent marine-based antioxidant peptide, which could be applied in cosmetic, pharmaceutical and food industries.

Antibacterial and Antioxidant Activity of Protein Hydrolysate Extracted from different Indonesian Avian Egg White

White egg contains the most significant protein source that has been explored to give more benefit for health purposes. This study evaluated the potential of antibacterial and antioxidant activity of white egg protein hydrolysate extracted from Indonesian avian eggs. The avian egg materials used local Indonesian chicken eggs (kampung chicken), chicken breed eggs, duck eggs, and muscovy duck eggs. The white egg was extracted by organic solvent and produced protein extracted which was dominated by ovalbumin and ovotransferrin. The protein extracted was hydrolyzed by pepsin and then powdered using a freeze dryer. Antibacterial and antioxidant activity was evaluated by agar well diffusion technique and 2,2-Diphenyl-1-picryl hydroxyl (DPPH) radical scavenging method. All samples showed antimicrobial activity against Salmonella sp., Escherichia coli, Staphylococcus aureus, Bacillus cereus, and Bacillus subtilis with a concentration of protein hydrolysate at 40 mg/mL. The antioxidant activity between avian species was different and dose-dependent. Protein hydrolysate extracted from duck white egg exhibited the highest radical scavenging activity (65%) at 10 mg/mL concentration. However, all white egg protein hydrolysate extracted from Indonesian avian eggs can potentially help reduce oxidation and microbial deterioration.

Effect of ultrasound-assisted pretreatment in combination with heating on characteristics and antioxidant activities of protein hydrolysate from edible bird's nest co-product.

The online version contains supplementary material available at 10.1007/s13197-022-05420-5.

Evaluation of the technological functional properties and antioxidant activity of protein hydrolysate obtained from brewers' spent grain

Beer production generates a large amount of waste, called brewers' spent grain (BSG), which has a nutritional potential mainly as a protein source. Proteins can be modified by hydrolysis releasing peptides with different bioactivities, such as antioxidant activity. The aim of this study was to produce a protein hydrolysate from protein concentrate obtained from BSG, evaluating its functional properties and antioxidant activity. The BSG protein concentrate was obtained by changing the pH at the isoelectric point, established at 3.5. The concentrate was hydrolyzed with the enzyme Alcalase, after defining the enzyme: substrate ratio (2:100), and 4 h was hydrolysis time (hydrolysis degree 32%). The hydrolysate showed better results of antioxidant activity than the concentrate in all tested methods, highlighting the ABTS radical capture with activity above 90%. The foaming capacity was not significantly modified (49%–45%), while emulsion capacity was significantly improved (30%–72%) by the hydrolysis process. Practical applications The results of this work indicate that some functional properties of BSG can be upgraded by enzymatic hydrolysis. These BSG hydrolysates showing improved antioxidant and emulsifying activities can be useful ingredients in food formulations adding value to this important byproduct of the beer industry.

Effects of enzymatic hydrolysis on the antioxidant activity of protein hydrolysate derived from the larvae of black soldier fly (Hermetia illucens L.)

Effects of enzymatic hydrolysis on the antioxidant activity of protein hydrolysate derived from the larvae of black soldier fly (Hermetia illucens L.)

Antioxidant activity of protein hydrolysate from snakehead fish (Channa striata) viscera obtained by enzymatic process

Snakehead fish (Channa striata) in South Sumatra, Indonesia has been widely used as a raw material in the processing of typical Palembang food industry, namely pempek, kemplang, and kerupuk. During its processing, not all parts of the fish can be utilized. In general, only 40% of the fish is used for consumption and 60% is wasted as by-products. One of the by-product produced during processing is viscera which can still be used as value-added products. One alternative is to use viscera as raw material in the production of fish protein hydrolysate (FPH) which is well known to have functional properties such as antioxidant, antibacterial, antihypertensive, and anticancer. This research was aim to determine the antioxidant activity of FPH made from snakehead fish viscera as a source of natural antioxidants. The research was conducted by papain treatments with the concentration of enzymes used were 1%, 2% and 3%. Evaluation of the hydrolysis process was done by measure the soluble protein and DH (degree of hydrolysis) while antioxidant activity was carried out by DPPH (1,1-diphenyl-2-picrylhydrazyl) and ABTS (2,2-Azinobis 3-ethyl benzothiazoline6-sulfonic acid) assay. DH of fish protein hydrolysate was found to be 68.79%, 77.06% and 72.63%, respectively while protein solubility gave values of 5.69%, 6.15% and 6.56% respectively. The highest antioxidant activity was attained at enzyme concentration of 3% with DPPH (1,1-diphenyl-2-picrylhydrazyl) and ABTS (2,2-Azinobis 3-ethyl benzothiazoline 6-sulphonic acid) value were 37.26% and 58.58% respectively.

Investigation of antioxidant activity of protein hydrolysate derived from baby clam (Corbiculidae sp.) broth

This study is aimed to bring baby clam broth (BCB) into antioxidant proteolysate utilizing enzymatic hydrolysis. Chemical compositions of BCB were firstly analyzed, followed by investigating the effects of enzymatic hydrolysis parameters involving in enzyme type, pH, temperature, enzyme:substrate (E:S) ratio and hydrolysis time on antioxidant of BCB proteolysate. It can be seen from the result that the BCB owned the moisture content, protein content, lipid content, and ash content of 97.55±0.89%, 1.52±0.16%, 0.09±0.02%, and 0.37±0.04%, respectively. The BCB proteolysate, under the hydrolysis condition including Flavourzyme, pH 7, 50°C, E:S ratio of 5 U/g protein and hydrolysis time of 50 min, exhibited the highest 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) cation ratio (ABTS●+) scavenging activity of 770.67±28.33 µM Trolox Equivalent (µM TE) (7.1 and 2.5 times lower than those of vitamin C and butylated hydroxytoluene (BHT), in order) and ferric reducing antioxidant power (FRAP) value of 245.26±7.37 µM TE (11.6 and 4.0 folds lower than those of vitamin C and BHT, respectively). This study suggests a new use of the BCB, antioxidant proteolysate which could be applied as a functional food or natural antioxidant additive, substituting for synthetic compounds.

Chemical-free recovery of protein from cow manure digestate solid and antioxidant activity of recovered protein

Livestock manure solids have a significant content of protein which is not only underutilized, but prone to runoff and eventual breakdown to reactive nitrogen compounds, contributing to eutrophication. We have developed a novel subcritical water extraction process to extract protein from livestock manure solid without the use of any chemical. We demonstrate the versatility of our new process to control the molecular weight distribution of the extracted protein hydrolysate. The antioxidant activity of protein hydrolysate has been examined through Oxygen Radical Absorbance Capacity Assay. The results have shown that our protein hydrolysate had its antioxidant capacity against the peroxyl radical similar to that of vitamin E and exhibited almost 7 times as strong inhibition against the hydroxyl radical as vitamin E. We also evaluated the nutritional value of our PH by analyzing its amino acid composition and the MW distribution through amino acid analysis, SDS-PAGE, and MALDI-TOF mass spectroscopy.

Preparation and Characterization of Microcapsules Containing Antioxidant Fish Protein Hydrolysates: a New Use of Bycatch in Brazil.

In this study, we evaluated the effect of complexation and microencapsulation with pea protein on the antioxidant activity of protein hydrolysates from bycatch in Brazil. The zeta potential values of complexes changed from negative to positive with the increase of pea protein as a result of positively charged complexes formation. The increase in the ratio of pea protein/hydrolysates also resulted in increased turbidity in all samples. Particle size measurements indicated that the complexes tended to form larger aggregates (ranged from 61.5 ± 1.7μm to 183 ± 2.8μm). The 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity of the pea protein/fish protein hydrolysate complexes was higher than that of the protein hydrolysates alone. Moreover, increasing levels of pea protein did not affect the antioxidant activity of fish protein hydrolysates. The complexes of the Paralonchurus brasiliensis were chosen for the microencapsulation process by spray-drying. The results revealed that spray-drying did not have a significant effect (P > 0.05) on the protein hydrolysate antioxidant activity when they were complexed with pea protein. Thus, this work suggests that the complexation with pea protein and subsequent microencapsulation by spray-drying is an efficient way to protect the biological activity of protein hydrolysates obtained from bycatch. This study provides evidence for the potential use of bycatch from shrimp fisheries as functional ingredients or nutraceuticals.

Autolysis of rainbow trout (Oncorhynchus mykiss) by-products: Enzymatic activities, lipid and protein oxidation, and antioxidant activity of protein hydrolysates

Autolysis (at fixed temperatures (40, 50, 60 °C) or gradually increasing temperatures (40-60 °C) with different times) was used to produce protein hydrolysates from rainbow trout processing by-products. Total proteolytic and trypsin activities with fixed temperatures was higher than gradually increasing temperatures, decreased with increasing autolysis time and temperature with fixed temperatures (P ≤ 0.05). TCA-soluble peptides decreased with increasing autolysis times from 1 to 3 h (P ≤ 0.05). Autolysis increased peroxide value and thiobarbituric acid-reactive substances in both lipids and hydrolysates, particularly with gradually increasing temperatures (P ≤ 0.05) and was associated with oxidation of polyunsaturated fatty acids. Sulfhydryl groups decreased, while protein carbonyls and solubility were increased with fixed temperatures at higher temperatures (50 and 60 °C) or with gradually increasing temperatures at longer autolysis time (P ≤ 0.05). Free radical scavenging activity and the metal chelating ability of hydrolysates were governed by autolysis times and temperatures. Results of size exclusion chromatography-high performance liquid chromatography indicated that autolysis for 1 h at lower temperature (40 °C) was sufficient to produce autolysates rich in small peptides from rainbow trout by-products. Autolytic hydrolysis might be useful for production of such protein hydrolysates.

Antioxidant activities of peptide hydrolysates obtained from the seeds of Treculia africana Decne (African breadfruit)

Protein hydrolysates usually possess higher nutritive value than an equivalent mixture of free amino acids. This study was aimed at determining the antioxidant activities of protein hydrolysates of Treculia africana seeds. Soluble protein was isolated from Treculia africana seed flour by alkaline solubilization and acid precipitation, and further hydrolyzed with three proteases (trypsin, pancreatin and pepsin) individually and in a sequential two- and three-protease systems. Antioxidant activities (DPPH, FRAP and lipid peroxidation) of the hydrolysates were investigated. Hydrolysates from Treculia africana seed protein showed varying degree of hydrolysis, pancreatin hydrolysates had the highest (94.92%) and pancreatin-pepsin hydrolysates had the least (6.59%). Pancreatin proved to be the most efficient protease for hydrolyzing Treculia africana protein with a high protein recovery of 156.06 mg/ml. Its hydrolysates exhibited the highest DPPH scavenging activity (71.02%) and had a high radical-mediated peroxidation of oleic acid. Likewise, pancreatin hydrolysates as well as trypsin-pancreatin hydrolysates showed the highest FRAP activity (37.17 and 38.52 µg/ml BHA, respectively). Pancreatin hydrolysates showed significant higher (p < 0.05) antioxidant potentials than other hydrolysates of T. africana seed protein. These findings showed the potential use of Treculia africana hydrolysates as antioxidants in reducing food spoilage and management of oxidative stress-related metabolic disorders.

The effects of hydrolysis condition on the antioxidant activity of protein hydrolysate from Cyprinus carpio skin gelatin

The aim of the study was the selection of food grade, an inexpensive and commercially available enzyme that would allow to obtain a hydrolysate from carp (Cyprinus carpio) skin gelatin with the highest antioxidant activity. Moreover, the objective of the study was to investigate the effects of pH temperature and incubation duration of the hydrolysis on protein degradation, free amino acids and antioxidant properties of the obtained hydrolysates. Protein hydrolysates obtained from carp skin gelatin using Protamex show potent antioxidant properties, which differed depending on the hydrolysis parameters. The hydrolysis parameters significantly influenced the free amino acid profiles as well as protein depolymerization and antioxidant properties of the hydrolysates. The acquired hydrolysates showed very potent antioxidant properties (FRAP value of 5.12 μM Trolox/mg) and a high degree of the depolymerized protein (27.73%). Furthermore, there was a clear positive correlation between the pH of the hydrolysis and the metal chelating activity of the hydrolysate, with all the hydrolysates produced at pH 6 exhibiting no metal chelating activity, while hydrolysates produced at pH 8 showed metal chelating activity. The carp skin gelatin hydrolysates with the highest antioxidant properties were obtained using Protamex at pH 7 and a temperature of 50 °C for 3 h.

Bioactive stability of microalgal protein hydrolysates under food processing and storage conditions.

The stability of antioxidant protein hydrolysates from Spirulina sp. LEB 18 was evaluated under food processing conditions and after in vitro digestion. Protein hydrolysates with degrees of hydrolysis of 50.6% and 60% were obtained after 90 and 120min of reaction, respectively, with Protemax 580L. The results indicated that the antioxidant activity of protein hydrolysates was maintained following application of heat treatment (- 18°C, 63°C, and 100°C). Moreover, the ability of protein hydrolysates to inhibit the 2,2-diphenyl-1-picrylhydrazyl radical was increased by nearly 25% upon exposure to acidified media (pH 4 and pH 6). In general terms, the protein hydrolysates were bioavailable after digestion with pepsin and pancreatin. This study supports the incorporation of bioactive peptides from microalgae into functional foods by demonstrating the maintenance of their biological activities in the face of food processing conditions and gastrointestinal digestion.

장수풍뎅이 유충 단백가수분해물의 제조 및 항산화 활성

장수풍뎅이 유충 단백가수분해물의 제조 및 항산화 활성

Antimicrobial and antioxidant activities of protein hydrolysate from terrestrial snail Cryptozona bistrialis

Phytochemical screening and Antimicrobial activity of the leaves of Memecylon umbellatum burm. F.Subban Murugesan, Annamalai Pannerselvam, Arumugame Chanemougame Tangavelou

Anti-Inflammatory, Antioxidant, and Antimicrobial Effects of Underutilized Fish Protein Hydrolysate

ABSTRACTAntimicrobial, anti-inflammatory, and antioxidant activities of protein hydrolysates from Argentine croaker (Umbrina canosai) protein isolate (CPI) or Argentine croaker myofibrillar protein with different degrees of hydrolysis (DH: 10–20%) prepared using Alcalase or Protamex were determined. Results showed that an increase in the DH resulted in higher content of hydrophobic and aromatic amino acids (AAAs) and in a decrease in molecular weight (MW) distribution for all hydrolysates obtained. Furthermore, the enzyme and raw material used influenced the amino acid content and MW determined. Hydrolysates from CPI with a 20% DH by Alcalase had higher 2,2ʹ-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) radical scavenging activity, metal chelation, and ferric-reducing antioxidant power (p < 0.05). All hydrolysate samples decreased the pro-inflammatory capacity. In all the evaluated microorganisms, only seven were inhibited, most being Gram-positive. Alcalase was found to exert a considerable influence on antibacterial activity. These hydrolysates are an alternative as natural antimicrobials, anti-inflammatory, and antioxidant compounds.

Scenedesmus obliquus: Antioxidant and antiviral activity of proteins hydrolyzed by three enzymes.

PurposeTo obtain protein hydrolysates from fresh water green algae Scenedesmus obliquus by three different enzymes and evaluate its antioxidant and antiviral activity.MethodsEnzymatic hydrolysates of green algae Scenedesmus obliquus protein were prepared by treatment with: 1.2% solution of pepsin, trypsin or papain. Protein was extracted from S. obliquus by three different extraction methods. Protein extracts and hydrolysates were assessed from stained gels following SDS–PAGE of samples. Antioxidant activity of protein hydrolysates was investigated.ResultsS. obliquus cells and protein extracts were rich in Arg, Lys, Asp, Ala, and His. Protein hydrolyzed by papain (Sd1pa) and protein hydrolyzed by trypsin (Sd2Try) induced highest antioxidant activity based on 1,1-diphenyl-2-picryl-hydrazyl (DPPH) radical-scavenging (41.41% and 40.62%) respectively, and on 2,2′-azinobis 3-ethyl-benzothiazoline-6-sulphonate (ABTS) radical (87.03% and 45.12%) respectively, at 150 µg/ml. The inhibitory effect and mode of action of protein hydrolysates were evaluated against Coxsackie B3 virus (CVB3). Protein hydrolyzed by papain (Sd2pa) and protein hydrolyzed by pepsin (Sd1pep) at 100 µg/ml exhibited antiviral activity (66.2% and 57.6%, respectively), against (CVB3) from all protein hydrolysates.ConclusionS. obliquus protein hydrolysates have a potential as antioxidative neutraceutical ingredients and a potential therapeutic agent against CVB3.

Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus.

Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15min, 102.48, and 88.44min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μMTrolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstract ᅟ.