Article

Amino acid composition, antioxidant and functional properties of protein hydrolysates from the roe of rainbow trout (Oncorhynchus mykiss)

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Abstract

A fish roe protein hydrolysate from rainbow trout (Oncorhynchus mykiss) trout roe protein hydrolysates (TRH) was produced by pepsin and Alcalase. Proximate, amino acid compositions, protein digestibility and molecular mass distribution of the hydrolysates were determined. The degree of hydrolysis was found to be 44.08% and 27.62% (pepsin and Alcalase, respectively). The two hydrolysates contained a high amount of essential amino acids (33.53% Alcalase–29.39% pepsin). The results showed that TRH by different enzymes is a good source of the leucine and lysine amino acids. The pepsin produced a white powder with higher brightness (L* = 89.50). Alcalase hydrolysate was brownish yellow in colour (L* = 52.85, a* = 10.30, b* = 26.25). The hydrolysates represented excellent antioxidant activities in various concentrations. TRHs showed a good foaming and emulsification properties. The results thus revealed that protein hydrolysates from rainbow trout roe could be used as food additives possessing essential amino acids and antioxidant activity.

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Composition, functional properties and in vitro antioxidant and antibacterial activities of protein hydrolysates prepared with a proteolytic bacterium, Bacillus subtilis A26, through fermentation of fish proteins were investigated. Fermented fishmeat protein hydrolysates (FPHs) were prepared from sardinelle (SPH), zebra blenny (ZPH) goby (GPH) and ray (RPH). The protein content of freeze-dried FPHs ranged from 74.3% to 81%. All fermented hydrolysates had an excellent solubility and possessed interfacial properties. The antioxidant activities of FPHs were evaluated by different methods, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method, reducing power assay, β-carotene bleaching and DNA nicking assay. All hydrolysates showed dose-dependent antioxidant activities. Further, FPHs exhibited antibacterial activity and SPH was the most effective, particularly against Gram + bacteria.
Article
Roe protein concentrates prepared from Channa striatus (CRPC) and Lates calcarifer (LRPC) were investigated for physico-chemical characteristics, amino acid composition, functional properties and antioxidant activity. Channa and Lates roes yielded 20.7% and 22.5% of protein concentrates possessing 90.2% and 82.5% protein, respectively. Major differences were not observed in each of the amino acids except leucine in CRPC and LRPC. The solubility of protein was 3.93–54.6% and 1.6–55.5% over a pH range of 2–12 in CRPC and LRPC, respectively. Water absorption, oil absorption, foam capacity, stability and emulsifying capacity were found to be higher in CRPC than in LRPC. Antioxidant activity determined by the radical scavenging activity and ferric reducing power was higher in CRPC. SDS–PAGE of both roe protein concentrates showed protein bands of 170, 95 and 55 kDa. Moisture sorption isotherms of protein concentrates indicated their hygroscopic nature.
Article
A protein isolate was prepared from African locust bean (ALBPI) and the functional properties were investigated under the influence of pH, ionic strength and varying protein concentration. Protein solubility diminished as the pH increased from 2 to 4.5, after which further increase in pH increased it progressively. The oil absorption capacity of ALBPI was 1.97 ml/g protein. Water absorption capacity increased when ionic strength of the medium increased to 0.2 M but diminished with further increase in ionic strength. Gelation properties improved at pH 4. The results indicate improvement in gelation capacity as the ionic strength of protein solution increased from 0.1 to 0.2 M while further increase in ionic strength caused the gelation tendency to decline. Increase in concentration favoured emulsifying activity (EA) and stability (ES) up to 4% (w/v) concentration, while further increase from 6% to 10% (w/v) diminished emulsifying properties. Also, initial increase in ionic strength, up to 0.2 M, improved both emulsifying activity and stability while further increase in ionic strength progressively reduced emulsifying properties. Maximum emulsifying activity and stability were at pH 10 while minimum values were obtained at pH 4. Foam capacity and stability increased as the protein concentration increased. Increase in ionic strength from 0 to 0.2 M increased the foam capacity (FC) and stability (FS) but foam capacity was reduced as the ionic strength increased further. Foam capacity and stability were pH-dependent. A minimum value of 32.7% was recorded at pH 4 while further increase in pH increased the foam capacity progressively until it reached a maximum (86.8%) at pH 10. Contrarily, maximum foam stability was recorded at pH 4 while foam stability diminished as the pH of the protein solution increased.
Article
A fish protein hydrolysate (FPH) from Pacific whiting (Merluccius productus) muscle was produced by autolysis of a minced homogenate (8% protein) at pH 7.0 and 60°C, where maximum endogenous proteolytic activity was detected. FPH production was controlled by the pH stat method, yielding a 4.43% degree of hydrolysis after 1 h of autolysis. Upon autolytic processing, 28.9 ± 0.7% of the total protein was found in the soluble fraction. FPH was 100% soluble at pH 7.0 and 10.0 and was less soluble at pH 4 (82.5%, P ≤ 0.05). FPH showed better emulsifying properties than sodium caseinate (SCA) at pH 4.0 (P ≤ 0.05), but had a lower foaming capacity (P ≤ 0.05) than bovine albumin (BSA) at all evaluated pHs. FPH foaming capacity was not affected by pH, however, foam stability was equal or better than that of BSA, especially at pH 4.0 (P ≤ 0.05). These results suggest the possibility of producing FPH with similar or better functional properties than those of functional ingredients, such as SCA and BSA. Furthermore, the data presented support our hypothesis that the high proteolytic activity in Pacific whiting could be used as an advantage in fish protein hydrolysate production or as a processing aid where protein hydrolysis is required.
Article
Antioxidative activities of 28 synthetic peptides, which were designed based on an antioxidative peptide (Leu-Leu-Pro-His-His) derived from proteolytic digests of a soybean protein, against the peroxidation of linoleic acid in an aqueous system were measured by the ferric thiocyanate method. The results for the hydroperoxide levels derived from linoleic acid agreed with those obtained by reversed-phase high-performance liquid chromatography. The deletion of the C-terminal His decreased the activity, whereas the deletion of the N-terminal Leu had no effect. In the peptide sequence, His and Pro played important roles in the antioxidative activity and, among the peptides tested, Pro-His-His was the most antioxidative. The activity decreased on substitution of the second His with d-His. Introduction of Tyr to the positions of Pro or His did not increase the activities of the corresponding peptides. Antioxidative peptides showed synergistic effects with nonpeptidic antioxidants as observed in soybean protein hydrolysates. The magnitude of the effects, however, did not correlate with the antioxidative activities of the peptides. Keywords: Antioxidative peptides; antioxidant; soybean protein hydrolysate; ferric thiocyanate method; synergistic effect
Article
Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe, hydrolysed by Alcalase 2.4L (RPH) with different degrees of hydrolysis (DH) at various concentrations were examined. As DH increased, the reduction of DPPH, ABTS radicals scavenging activities and reducing power were noticeable (p<0.05). The increases in metal chelating activity and superoxide scavenging activity were attained with increasing DH (p<0.05). However, chelating activity gradually decreased at DH above 30%. All activities except superoxide anion radical scavenging activity increased as the concentration of hydrolysate increased (p<0.05). Hydrolysis using Alcalase could increase protein solubility to above 80% over a wide pH range (2-10). The highest emulsion ability index (EAI) and foam stability (FS) of hydrolysates were observed at low DH (5%) (p<0.05). Concentrations of hydrolysates determined interfacial properties differently, depending on DH. The molecular weight distribution of RPH with 5%DH (RPH5) was determined using Sephadex G-75 column. Two major peaks with the molecular weight of 57.8 and 5.5kDa were obtained. Fraction with MW of 5.5 had the strongest metal chelating activity and ABTS radical scavenging activity. The results reveal that protein hydrolysates from defatted skipjack roe could be used as food additives possessing both antioxidant activity and functional properties.
Article
The biuret method of protein estimation was compared with the Kjeldahl method. Highly significant positive correlations with Kjeldahl protein of 0.99, 0.99, 0.98, and 0.99 were obtained for ground beef, pork, chicken breast, and cod, respectively. The high correlations between the two methods and the small standard deviations for the biuret values point out the reliability and the accuracy of the biuret method. The same substances were analyzed by the Orange G dye-binding method with highly significant positive correlations with Kjeldahl protein of 0.90, 0.80, 0.94, and 0.95 for ground beef, pork, chicken breast, and cod, respectively. However, the amount of dye bound per g protein varies with the protein content of the sample, and the precision is poor. Orange G dye binding has possibilities for use in analyzing meat proteins only if the preparations and procedures are carefully standardized and the protein content does not vary more than a few percent. With Amido Black 10B, the amount of dye bound was too strongly dependent upon sample size to justify further investigation of this dye for estimation of the protein content of comminuted meats.
Article
To produce and identify bioactive peptides, two commercial enzymes, orientase (OR) and protease XXIII (PR) were used to hydrolyze tuna dark muscle by-product for up to 6 h, and the hydrolysates were evaluated for antioxidative properties. The results showed that, 60-min OR and 120-min PR hydrolysates possessed the highest antioxidative activity. Then, the protein hydrolysates were subjected to a Sephadex G-25 gel filtration chromatography, and the molecular weight of the peptide fractions which showed the highest antioxidative activity ranged from 390 to 1400 Da. The peptide fractions were further isolated using the two-step high-performance liquid chromatography (HPLC-1 and HPLC-2), and the amino acid sequences of the two antioxidative peptides from OR and PR hydrolysates were Leu–Pro–Thr–Ser–Glu–Ala–Ala–Lys–Tyr (978 Da) and Pro–Met–Asp–Tyr–Met–Val–Thr (756 Da), respectively. We thus conclude that antioxidative hydrolysates from tuna dark muscle by-product may be useful ingredients in food and nutraceutical applications.
Article
The effects of different proteolytic enzymes and different reaction durations (25, 50, 75 min) on functional and nutritional properties of red (sockeye) salmon head hydrolysates were evaluated. Degree of hydrolysis values for the 75-min digestion ranged from 6.4% to 16.7%. Oil yield (4.9% to 10.6 %) from red salmon heads was affected by the enzyme used. Protein hydrolysate powders were yellowish and contained 62.3% to 64.8% protein with high levels of essential amino acids. Increased degree of hydrolysis values were weakly correlated with increased hydrolysate solubility. Maximum emulsion stability and fat adsorption were observed for the dried hydrolysate generated in the 25-min reaction time. Water adsorption of hydrolysate powders ranged from 1.0 mL to 3.3 mL water/g dried hydrolysate.
Article
We have investigated the antioxidant activity of protein hydrolysates prepared from backbones of two commercially important fishes; seela (Sphyraena barracuda) and ribbon fish (Lepturacanthus savala). Pepsin and trypsin hydrolysates were found more potent to inhibit lipid peroxidation in case of ribbon and seela fish respectively and were further purified by using fast protein liquid chromatography on anion exchange and gel filtration chromatography. The active peaks after gel filtration chromatography of seela fish was able to scavenge 2,2-diphenyl-1-picryhydrazyl and hydroxyl radicals by 61±2.3 and 58.7±2.3% and ribbon fish hydrolysate by 60.0±2.6 and 55.6±1.8% as measured by ESR spectroscopy. And the active fractions showed presence of both essential and non-essential amino acids with high percentages of arginine (11.95 and 12.76%) and lysine (13.49 and 13.89%). KeywordsAntioxidants–ESR spectroscopy– Sphyraena barracuda – Lepturacanthus savala –Lipid peroxidation
Article
The oxidative stability of mahi mahi red muscle dipped in tilapia protein hydrolysates was evaluated. Alkali solubilised tilapia protein isolate was hydrolysed using Flavourzyme to 13% degree of hydrolysis. Whole tilapia protein hydrolysate and ultrafiltered fraction <10 kDa were used as dip solutions. Mahi mahi red muscle was dip treated either for 2 or 4 min and stored at 4 °C. Lipid hydroperoxides (PV), thiobarbituric acid reactive substances (TBARS) and a∗ value were measured at regular intervals. Results showed that dip treatments significantly decreased (p < 0.05) the formation of PV and TBARS over 90 h storage time. There was no significant (p > 0.05) difference between WH and <10 kDa fractions, and between 2 and 4 min treatments. Red colour of treated samples measured as a∗ value decreased with storage time, but was not significantly different from the control. It could be concluded that dip treatment for 2 min in whole tilapia protein hydrolysate may be used as a potential antioxidant treatment for improving oxidative stability of fish fillets.
Article
Composition, functional properties and antioxidative activity of a protein hydrolysate prepared from defatted round scad (Decapterus maruadsi) mince, using Flavourzyme, with a degree of hydrolysis (DH) of 60%, were determined. The protein hydrolysate had a high protein content (48.0%) and a high ash content (24.56%). It was brownish yellow in colour (L∗ = 58.00, a∗ = 8.38, b∗ = 28.32). The protein hydrolysate contained a high amount of essential amino acids (48.04%) and had arginine and lysine as the dominant amino acids. Na+ was the predominant mineral in the hydrolysate. The protein hydrolysate had an excellent solubility (99%) and possessed interfacial properties, which were governed by their concentrations. The emulsifying activity index of the protein hydrolysate decreased with increasing concentration (p < 0.05). Conversely, the foaming abilities increased as the hydrolysate concentrations increased (p < 0.05). During storage at 25 °C and 4 °C for 6 weeks, the antioxidative activities and the solubility of round scad protein hydrolysate slightly decreased (p < 0.05). Yellowness (b∗-value) of the protein hydrolysate became more intense as the storage time increased but the rate of increase was more pronounced at 25 °C than at 4 °C.
Article
Protein hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The protein content of Alcalase-produced hydrolysate was higher (85%) than that of papain hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased protein solubility of fish egg protein hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g hydrolysate), respectively for Alcalase and papain protein hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg protein hydrolysates could be useful in the food industry.
Article
In order to better utilize a fish by-product, the enzymatic hydrolysis of tuna liver was performed using commercially available proteases such as Flavourzyme, Alcalase, Protamex, and Neutrase. The hydrolysates were prepared as both first step hydrolysates and second step hydrolysates. The molecular weight distribution of the hydrolysates was determined by size exclusion chromatography and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry, which analyzed a representative hydrolysate type with a weight range of 1000–3000 Da. The antioxidant activities of the tuna liver hydrolysates against 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl radical, and hydrogen peroxide, along with a reducing power assay, showed that the second step hydrolysates had more potent antioxidant activity than the first step hydrolysates. However, the first step hydrolysates exhibited more effective chelating activity. Furthermore, the protection ability of the hydrolysates toward hydroxyl radical-induced oxidative DNA damage was evaluated by measuring the conversion of supercoiled pBR322 plasmid DNA to the open circular form. In addition, an angiotensin I-converting enzyme (ACE) inhibition assay revealed that all hydrolysates had similar ACE-inhibitory properties. These findings suggest that tuna liver hydrolysates may be a beneficial ingredient to use in functional foods.
Article
Antioxidative activity and functional properties of protein hydrolysates from yellow stripe trevally (Selaroides leptolepis) meat, hydrolyzed by Alcalase 2.4L (HA) and Flavourzyme 500L (HF) with different degrees of hydrolysis (DH) were investigated. As the DH increased, DPPH radical-scavenging activity and reducing power of HA decreased (p < 0.05) but no differences were observed for HF (p > 0.05). Metal chelating activity of both HA and HF increased with increasing DH (p < 0.05). HF generally had a higher (p < 0.05) chelating activity than had HA at the same DH tested. At low DH (5%), HA exhibited a better DPPH radical-scavenging activity while, at high DH (25%), HF had a higher (p < 0.05) reducing power. For the functional properties, hydrolysis by both enzymes increased protein solubility to above 85% over a wide pH range (2–12). When the DH increased, the interfacial activities (emulsion activity index, emulsion stability index, foaming capacity, foam stability) of hydrolysates decreased (p < 0.05), possibly caused by the shorter peptide chain length. At the same DH, the functionalities of protein hydrolysate depended on the enzyme used. The results reveal that antioxidative activity and functionalities of protein hydrolysates from yellow stripe trevally meat were determined by the DH and by the enzyme type employed.
Article
This work is mainly concerned with the effect of γ-irradiation on amino acids content of a manufactured baby food that was irradiated with a gamma cell (Co-60) at dose levels of 0.5, 1.5, 6, 10, 30, 50 kGy at room temperature and in the presence of air. The samples were analyzed immediately after irradiation. The methods for hydrolysis of proteins, the derivatization of amino acids with phenylisothiocyanate, the separation and quantitation of the resulting phenylthiocarbamyl derivatives by reverse phase high performance liquid chromatography are described. The destruction pattern of amino acids in this formulated food (whose ingredients were: wheat starch, skim milk powder, sugar, vegetable oils, vitamins, minerals, essences) was not very different from whole foods.
Article
Considerable amounts of fish processing byproducts are discarded each year. By developing enzyme technologies for protein recovery and modification, production of a broad spectrum of food ingredients and industrial products may be possible. Hydrolyzed vegetable and milk proteins are widely used food ingredients. There are few hydrolyzed fish protein foods with the exception of East Asian condiments and sauces. This review describes various manufacturing techniques for fish protein hydrolysates using acid, base, endogenous enzymes, and added bacterial or digestive proteases. The chemical and biochemical characteristics of hydrolyzed fish proteins are discussed. In addition, functional properties of fish protein hydrolysates are described, including solubility, water-holding capacity, emulsification, and foam-forming ability. Possible applications of fish protein hydrolysates in food systems are provided, and comparison with other food protein hydrolysates where pertinent.
Salt and water temperature curing effect on rainbow trout fish eggs qualitative changes (Oncorhyncus mykiss) during cold storage
  • Mirsadghi
Salt and water temperature curing effect on rainbow trout fish eggs qualitative changes (Oncorhyncus mykiss) during cold storage
  • H Mirsadghi
  • A Alishahi
  • B Shabanpuor
  • R Safari
Mirsadghi, H., Alishahi, A., Shabanpuor, B. & Safari, R.. (2015). Salt and water temperature curing effect on rainbow trout fish eggs qualitative changes (Oncorhyncus mykiss) during cold storage. Journal of Fisheries Science and Technology, 4, 93-104.
The State of World Fisheries and Aquaculture. Contributing to food security and nutrition for all
  • Fao
FAO. (2016). The State of World Fisheries and Aquaculture. Contributing to food security and nutrition for all. PP. 200. Rome: FAO.