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Amino acid composition, antioxidant and functional properties of protein hydrolysates from the roe of rainbow trout (Oncorhynchus mykiss)
International Journal of Food Science & Technology
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.
... The linear polymer alginate is an In Asian countries, much of the fish roe is not consumed and is thrown away. Fish roe containing 11% albumin, 75% ovoglobulin and 13% collagen are good sources for the production of bioactive peptides by enzymatic hydrolysis [29,43]. In addition, seafood products and wastes have been shown to be good sources of antioxidant peptides (Ovissipour et al. 2013, [35]. ...
... After hydrolysis, the samples were heated at 95-85 °C for 15 min to inactivate the enzymes and then centrifuged at 13,000 × g (30 min, 4 °C). The obtained substrate was stored under the sublimation dryer and the PH fish roe was stored in closed containers at − 20 °C [10,43]. ...
... In the present study, the moisture content of the samples was lower than 10 and was consistent with previous studies. In most studies in this field on hydrolyzed fish protein, the moisture content has been reported to be less than 10 [37,43,55]. The low moisture content of this powder is due to the use of methods such as spray drying or lyophilization. ...
Using alcalase and pepsin enzymes, rainbow trout roe protein hydrolysate (RPH) was prepared and its effect along with alginate–chia seed composite coating (CC) was investigated in order to increase the shelf life of meat fillets during refrigeration. As a result of RPH tests, alcalase enzyme produced a RPH with a higher degree of hydrolysis, antioxidant activity, and essential amino acid content. As a result, it was used for further experiments. Afterward, five meat fillet treatments were prepared, T1: control, T2: CC, T3: CC + RPH 1%, T4: CC + RPH 1.5% and T5: CC + BHA, and periodically evaluated for physicochemical (peroxide value, thiobarbituric acid, total volatile nitrogen bases, texture hardness, chewability, and water-holding capacity) and microbiological (total bacterial count, psychrotrophic bacteria). The results showed that CC has antioxidant and antimicrobial properties and the addition of RPH increased the proposed properties, and by increasing the concentration, the better results were observed. Thus, T4 delayed significantly the process of microbial spoilage and oxidation and increased the shelf life of the meat. In most cases, it was more effective than T5 (P < 0.05). All in all, the addition of RPH to CC can meet the demand of consumers for meat products free of chemicals.
Graphical abstract
... The emulsifying activity index (EAI) and the emulsion stability index (ESI) were measured by modifying the method of Rajabzadeh, Pourashouri, Shabanpour, and Alishahi (2018). ...
... Enzyme hydrolysis improves thermal stability. that is, small peptides can easily migrate into the air-water interface (Rajabzadeh et al., 2018). However, our results showed that gelatine with a low DH (1.61%) had a high FC, which could be attributed to F I G U R E 4 DSC curves of deer antler base gelatine and its hydrolysate. ...
... As increasing the DH has been reported to enhance emulsion stability (Chalamaiah, Jyothirmayi, Prakash, & Dinesh Kumar, 2015), the increase in the gelatine hydrolysate ESI may have resulted from the higher DH of the gelatine hydrolysate than that of the gelatine. The results for the emulsifying properties found in this study are consistent with those for protein hydrolysates from the roe of rainbow trout reported by Rajabzadeh et al. (2018). ...
Gelatine was extracted from deer antler base by the hot water method and hydrolyzed with trypsin. A comparison of the properties of gelatine before and after enzymatic hydrolysis showed a decline in the surface hydrophobicity, enhanced thermal stability, broadening of the particle size distribution, a zeta potential shift to a lower pH, reduced foaming and emulsifying properties, and enhanced antioxidant activity. Hydrolysis increased the gelatine antioxidant activity in DPPH and FRAP assays. These results indicate that the functional properties of deer antler base gelatine may be affected by trypsin modification. The properties of deer antler base gelatin were compared before and after hydrolysis. The surface hydrophobicity declined after hydrolysis. The emulsifying stability of the hydrolysate increased. The antioxidant activity of DPPH and FRAP was enhanced after hydrolysis.
... Chemical composition of salmonids wastes in terms of moisture (Mo), organic matter (OM), and ashes (Ash). Total lipids (Lip), proteins (Pr-tN, as total nitrogen × 6. 25), and proteins after degreasing samples (Pr-tN *) were determined using dried substrates. Error bars showed the intervals of confidence for n = 3-4 (samples from independent batch) and α = 0.05. ...
... In addition, these numerical values of parameters were similar to those obtained in 100 mL-reactor and reported in Table 3 and Figures 1 and 2. In all reports about the production of salmonid FPHs, the mathematical modeling of proteolytic kinetics was unexplored. Taking into account the published data of H (%) at the end of Alcalase treatment, our values of H m (Table 3) were always higher or slightly higher than those obtained for hydrolysates of salmon head (17%), salmon frames (27%), and trout roe (28%) [9,24,25]. Using soluble proteins extracted by CaCl 2 -citric treatment of a mixture of RT by-products (heads, frames, and viscera) as substrate, the value of H was of 42% for a 3-h Alcalase hydrolysate [26]. In addition to the type of starting material, the concentration of enzyme in that work was 50 times higher than that used in the present experiments. ...
... In all cases, the essential amino acid content was higher (value of TEAA/TAA as percentage) than recommended for human adults and infants [30,31]. Similar percentages to our outcomes were observed for enzymatic hydrolysates of rainbow trout frames and roes generated by Alcalase [14,25], and salmon frames catalyzed with Protamex [3] but inferior when Papain was applied to identical salmon wastes [9]. Nevertheless, the data of TEAA/TAA for salmon viscera hydrolysates [32] were higher than here reported for other by-products of salmonids (46% vs. 33-37%). ...
In the present manuscript, various by-products (heads, trimmings, and frames) generated from salmonids (rainbow trout and salmon) processing were evaluated as substrates for the production of fish protein hydrolysates (FPHs), potentially adequate as protein ingredients of aquaculture feeds. Initially, enzymatic conditions of hydrolysis were optimized using second order rotatable designs and multivariable statistical analysis. The optimal conditions for the Alcalase hydrolysis of heads were 0.1% (v/w) of enzyme concentration, pH 8.27, 56.2°C, ratio (Solid:Liquid = 1:1), 3 h of hydrolysis, and agitation of 200 rpm for rainbow trout and 0.2% (v/w) of enzyme, pH 8.98, 64.2 °C, 200 rpm, 3 h of hydrolysis, and S:L = 1:1 for salmon. These conditions obtained at 100 mL-reactor scale were then validated at 5L-reactor scale. The hydrolytic capacity of Alcalase and the protein quality of FPHs were excellent in terms of digestion of wastes (Vdig > 84%), high degrees of hydrolysis (Hm > 30%), high concentration of soluble protein (Prs > 48 g/L), good balance of amino acids, and almost full in vitro digestibility (Dig > 93%). Fish oils were recovered from wastes jointly with FPHs and bioactive properties of hydrolysates (antioxidant and antihypertensive) were also determined. The salmon FPHs from trimmings + frames (TF) showed the higher protein content in comparison to the rest of FPHs from salmonids. Average molecular weights of salmonid-FPHs ranged from 1.4 to 2.0 kDa and the peptide sizes distribution indicated that hydrolysates of rainbow trout heads and salmon TF led to the highest percentages of small peptides (0–500 Da).
... In vitro enzymatic hydrolysis has been extensively used to generate bioactive peptides from high-protein foods and enhance their functional properties while preserving their nutritional values. Specifically, hydrolysis using proteolytic enzymes such as Alcalase, pepsin, trypsin, neutrase, and papain has shown a promise in producing bioactive protein hydrolysates from fish roe [5,6]. Common carp (Cyprinus carpio) roe is often treated as waste or animal feed due to its low-value and sensory appeal [7]. ...
... Furthermore, the ferric-reducing power of Alcalase and HT hydrolysates was significantly higher than FP-II (p < 0.05), but the ferric-reducing power of Alcalase and FP-II hydrolysates was not different (p > 0.05) in both roe species samples. Rajabzadeh et al. [6] compared Alcalase and pepsin abilities in hydrolyzing rainbow trout protein and found higher antioxidant activity in Alcalase-treated samples. Furthermore, Ahmmed et al. [13] demonstrated that Alcalase produced the highest antioxidant activity and DH when used to hydrolyze Hoki roe protein, compared to HT and FP-II. ...
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.
... The alc-FPH, pro-FPH, and pan-FPH were rich in containing aspartic acid, glutamic acid, and proline. These results were similar to those obtained by Rajabzadeh et al. (2018) for obtaining protein hydrolysates from the roe of rainbow trout Protein hydrolysates produced from rainbow trout roe by Alcalase and Pepsin contained 33.25 and 29.33 (g/100 g protein) of essential amino acids which were lower than their content in FPHs produced in the present study (Rajabzadeh et al., 2018). Moreover, the content of essential amino acids of saithe (Pollachius virens) head and backbone protein hydrolysates was lower than the present results (Hjellnes et al., 2021). ...
... The alc-FPH, pro-FPH, and pan-FPH were rich in containing aspartic acid, glutamic acid, and proline. These results were similar to those obtained by Rajabzadeh et al. (2018) for obtaining protein hydrolysates from the roe of rainbow trout Protein hydrolysates produced from rainbow trout roe by Alcalase and Pepsin contained 33.25 and 29.33 (g/100 g protein) of essential amino acids which were lower than their content in FPHs produced in the present study (Rajabzadeh et al., 2018). Moreover, the content of essential amino acids of saithe (Pollachius virens) head and backbone protein hydrolysates was lower than the present results (Hjellnes et al., 2021). ...
A new process for parallel extraction of sulfated polysaccharides (SPs) and fish protein hydrolysate (FPH) from tuna head was developed. The effect of type of enzymes (Alcalase, Protamex, and Pancreatin) on the structural, functional, and bioactivity of both SPs and FPHs was also investigated. Initially, SPs were extracted, then the remaining ethanol from polysaccharide precipitation was used to obtain hydrolyzed proteins. Protamex produced SPs with the highest carbohydrate content (50.17%) while Alcalase prompted the highest content of uronic acid/sulfate. The degree of hydrolysis of the FPHs varied by the used enzyme but their amino acid composition fulfilled human requirements. Both SPs and FPHs had antioxidant activity but their efficiency was governed by the type of enzyme and oxidation mechanism. SPs had good metal chelation while FPHs showed good radical scavenging. Recovered FPHs had substantially higher antibacterial activity than the SPs and showed the highest inhibition against E. coli in concentration of 1 mg/mL. Altogether, parallel extraction of SPs and FPHs could be a promising biorefinery approach for more efficient utilization of tuna head.
... Color is an important quality indicator in food industry, sometimes it reflects the changes in product quality (Verma et al., 2018a) and involves the sense of the product (Rafieian et al., 2015). This result consists with Rajabzadeh et al. (2018), who showed pepsin hydrolysate had higher brightness. There were some researchers showed that the Maillard reaction is responsible for yellowness of hydrolysates (Thiansilakul et al., 2007). ...
... There were some researchers showed that the Maillard reaction is responsible for yellowness of hydrolysates (Thiansilakul et al., 2007). In this work the reaction temperature of DBH-A was highest at 50 o C, this result consists with Chalamaiah et al. (2010) and Rajabzadeh et al. (2018). Table 4 showed the amino acids composition of deer blood and its hydrolysates. ...
... In this study experimental value (17.4%) was higher than predicted value (12.9%) which suggested that RSM model was effective and potential tool for the optimization of enzymatic hydrolysis. Earlier published literature reports that optimum temperature, pH, time and enzyme concentration for hydrolysis of fish byproduct by using Alcalase was in the range 55-65 °C; pH 6-8.5, 120-180 min and 0.5-3% added enzyme [35][36][37]. ...
... Rights reserved. and glutamate play important role in growth and regulation of immune systems [36]. The amino acid compositions and size of peptides are responsible for flavor development in food. ...
During surimi processing, large amount of the head & viscera is generated as by-product, which is either discarded or used for production of low value products such as fish feed. This study presents technology for sustainable utilization of by-products as high value-added products which indirectly reduces environmental pollution. Response Surface Methodology was used to define the optimal conditions for protein hydrolysates production. Different temperature (25–70 °C), time (20–120 min), and enzyme concentrations (0.05–0.2%) were optimized to obtain the maximum yield of Pink Perch Head & Viscera Protein Hydrolysate (PHVPH). The analysis of PHVPH revealed high amount of essential amino acids (35%) with 15% degree of hydrolysis, good functional properties, and moderate antioxidant properties (24.8%). The PHVPH was further microencapsulated using combination of wall material (maltodextrin, sodium alginate, gum Arabic and carboxyl methyl cellulose) to reduce the bitterness, fishy odor and hygroscopicity of PHVPH. Efficiency of microencapsulation process of PHVPH was assess by physiochemical properties, antioxidant activity, chemical bond (FTIR), microstructure (SEM) and sensory acceptability. The presence of PHVPH in the structure of microcapsule was proved by FTIR spectrometry. In addition, sensory evaluation of PHVPH and microencapsulated protein hydrolysate suggested that the microencapsulation process has been effective method in reducing the bitterness and odor of PHVPH powder and enhance its value in food formulation.
Graphical Abstract
... No comparison can be made with literature results since this is the first report dealing with the production of FPHs from turbot from the aquaculture industry. Regarding other fish by-products, our outcomes of H m are in range (similar or slightly lower) with the values observed for hydrolysates from whole fish discards as megrim, blue whiting, red scorpionfish, and grenadier [30], but higher than those obtained for FPHs of boardfish, and pouting and by-products from salmon and trout [6,13,32,33]. In the last decade, Alcalase has shown an excellent capacity to hydrolyze several fish wastes such as salmon by-products [25], yellowfin tuna heads [26], and Atlantic cod, having being also applied to cattle viscera [12,27]. ...
... No comparison can be made with literature results since this is the first report dealing with the production of FPHs from turbot from the aquaculture industry. Regarding other fish by-products, our outcomes of Hm are in range (similar or slightly lower) with the values observed for hydrolysates from whole fish discards as megrim, blue whiting, red scorpionfish, and grenadier [30], but higher than those obtained for FPHs of boardfish, and pouting and by-products from salmon and trout [6,13,32,33]. Figure S2 (supplementary material) shows different pictures related to the production of FPHs and the concomitant bones and oil recovered using the scheme reported in Figure 1. The amount of Figure 1. ...
The valorization of wastes generated in the processing of farmed fish is currently an issue of extreme relevance for the industry, aiming to accomplish the objectives of circular bioeconomy. In the present report, turbot (Scophthalmus maximus) by-products were subjected to Alcalase hydrolysis under the optimal conditions initially defined by response surface methodology. All the fish protein hydrolysates (FPHs) showed a high yield of digestion (>83%), very remarkable degrees of hydrolysis (30–37%), high content of soluble protein (>62 g/L), an excellent profile of amino acids, and almost total in vitro digestibility (higher than 92%). Antioxidant and antihypertensive activities were analyzed in all cases, viscera hydrolysates being the most active. The range of average molecular weights (Mw) of turbot hydrolysates varied from 1200 to 1669 Da, and peptide size distribution showed that the hydrolysate of viscera had the highest content of peptides above 1000 Da and below 200 Da.
... Accordingly, Naghdi et al. (2023b) suggest in a solution of lowmolecular-weight peptides that more air can be incorporated and, hence, the capacity to maintain a durable foam lowers. However, different results can be found in the literature about the relation between DH and foaming properties, and higher foaming properties have also been related to higher foaming properties in sardinella (Ben Khaled et al., 2014) or rainbow trout roe (Rajabzadeh et al., 2018) protein hydrolysates. Moreover, Liu et al. (2014) observed that the hydrolysates with DH 20% and 30% prepared by Alcalase exhibited superior foam properties to those of the samples with the same DH prepared by Protamex TM . ...
... The usage of alcalase is more indicated due to a much higher degree of hydrolysis of 30.9% compared to 6.5% for papain and a lower cost of this enzyme. Another comparison of the functionality of enzymatic hydrolysis with 2% alcalase and 2% pepsin was conducted on a rainbow trout (Oncorhynchus mykiss) [108]. It was shown that the degree of hydrolysis was 16.46% higher in the case of pepsin, but the amino acid content in the alcalase-based hydrolyzate was higher by 4.14%. ...
This paper reviews the scientific literature on the latest technologies for treating waste by chemical hydrolysis, enzymatic hydrolysis and supporting processes. Particular attention is focused on wastes of biological origin, especially high-protein materials and those containing fats and sugars, as valuable components can be extracted from these recyclables to produce plant growth-stimulating compounds and animal feed, chemicals, biofuels or biopolymers. The wastes with the greatest potential were identified and the legislative regulations related to their processing were discussed. Chemical and enzymatic hydrolysis were compared and their main applications directions and important process parameters were indicated, as well as the need to optimize them in order to increase the efficiency of extraction of valuable components.
... than others. Different antioxidant activities could be due to the different amino acid compositions that affected by the type of enzyme (Rajabzadeh, et al., 2018). The size and amino acid composition of peptides were influenced by the DH, which could affect their biological activities (Hajfathalian et al., 2018). ...
Abstract Excessive reactive oxygen species (ROS) can induce oxidative damage to cell membranes and biomolecules, leading to various chronic diseases. Therefore, the exploration of effective natural antioxidants that can replace traditional synthetic antioxidants to reduce excess free radicals without side effects is important. Herein, the antioxidant peptide (Lateolabrax japonicus protein hydrolysates; LPH) was obtained from bass (L. japonicus) by an optimal enzymatic hydrolysis process. The protective effect of LPH on the Caco‐2 cell oxidative stress model and the potential antioxidant signaling pathways were explored. The results showed that LPH was rich in hydrophobic amino acids, and the IC50 for 2,2‐diphenyl‐1‐picrylhydrazyl radical scavenging activity was 0.9667 mg/mL. Furthermore, the LPH treatment reduced cellular ROS levels and lipid peroxidation while increasing antioxidant enzyme activity in a dose‐dependent manner (p
... Some rainbow trout proteins and byproducts have already been shown to produce hydrolysate with antioxidant [12][13][14][15], anticancer [16] and antibacterial activities [17]. In literature, different enzymes, i.e., Alcalase [18,19] alkaline protease, papain [20], neutral protease, Flavourzyme, or trypsin [21], and conditions have been evaluated to produce protein hydrolysate from rainbow trout with different degrees of hydrolysis, characteristics and peptide generation. The fish protein hydrolysate (FPH) was obtained from minced rainbow trout raw material treated with two commercial enzymes, namely papain and bromelain (0.05% w/w each) [22]. ...
The present study aimed at characterizing the possible biological activities of the multifunctional low molecular weight fractions (<3 kDa) peptides isolated from rainbow trout (Oncorhynchus mykiss) obtained by enzymatic hydrolysis. The fish protein hydrolysate (FPH) was tested for its antioxidant property along with its angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. In particular, the 2,2-diphenyl-1-picrylhydrazyl (DPPH), the ferric reducing antioxidant power (FRAP), the oxygen radical absorbance capacity (ORAC) assay and the 2,2′-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assays were carried out for the evaluation of the in vitro antioxidant activity. The cell-free ACE and DPP-IV inhibitory activity assays were also estimated, showing a dose-dependent inhibition. These biological properties were additionally quantified at the cellular level using human intestinal Caco-2 cells. Namely, the antioxidant activity was determined by evaluating the capability of the hydrolysate to reduce the H2O2-induced reactive oxygen species (ROS) and lipid peroxidation levels, and the DPP-IV activity assays show a reduction of enzyme activity of up to 27.57 ± 3.7% at 5 mg/mL. The results indicate that Oncorhynchus mykiss-derived peptides may have potential employment as health-promoting ingredients.
... Najafian and Babji (2012) [5] stated that roe protein hydrolysates from defatted fish possesses functional and antioxidant properties with health-promoting benefits, such as anti-inflammatory and antibacterial effects. Fish roe hydrolysate was able to slow lipid oxidation [6] and showed good foaming and emulsification properties [7] in food model systems. In addition, fish roe polypeptide exerted hypoglycemic effects by regulating insulin secretion, which is mediated by Nrf2/ERK signaling [8]. ...
Currently, the use of skipjack tuna (Katsuwonus pelamis) roe to produce hydrolysate is limited, although it is a potentially valuable resource. This study aimed to investigate the physical and chemical characteristics of protein hydrolysates from tuna roe using autoclave and enzymes (alcalase and trypsin at 0.5 and 1.0% w/v). Bioinformatics was also applied to analyze the identified peptides. The hydrolysates were determined for amino acid composition, peptide profile patterns, antioxidant activity, solubility and foaming properties. The proteins were separated by SDS-PAGE before tryptic digestion and peptide identification by nano LC-ESI-MS/MS. The putative bioactivities of the identified peptides were predicted using bioinformatics prediction tools. The main amino acids found in all hydrolysates were cysteine, glycine and arginine (16.26-20.65, 10.67-13.61 and 10.87-12.08 g/100 g protein, respectively). The hydrolysates obtained from autoclaving showed lower molecular weights than those by the enzymatic method. The 0.1 g/mL concentration of hydrolysates provided higher antioxidant activities compared to the others. All hydrolysates had high solubility and exhibited foaming capacity and foam stability. Putative anti-hypertensive, anti-virus and anti-parasite activities were highly abundant within the obtained peptides. Moreover, predicted muti-bioactivity was indicated for seven novel peptides. In the future work, these peptides should be experimentally validated for further applications.
... Enzymatic hydrolysis is an effective method to convert lowconsumption proteins into high-value products and to improve their biological activity and nutritional value (Rajabzadeh et al., 2018). pH, temperature, enzyme/substrate ratio, hydrolysis time, enzyme type and substrate are important factors in the enzymatic hydrolysis process (Bozkurt et al., 2021). ...
Abstract
Fish skin is one of the most common resources of gelatin, which can be hydrolyzed bioactive peptides. In this study, gelatin
from sea bass skin (SBS) was hydrolyzed with flavourzyme to obtain peptide fractions with different molecular weights and
determined their bioactive and functional properties. All peptide fractions obtained showed antioxidant activity (DPPH and
FRAP). The bass gelatin peptide fraction 1 (BF1) (≤5 kDa) showed the highest DPPH (44.9%) and FRAP (42.04 mmol Fe+2 /g and
22.98 mmol trolox/g) activities. Besides, the BF1 (≤5 kDa) peptide fraction showed the highest in vitro cytotoxic effect (16.58%)
at 20 mg/mL concentration compared to the other peptide fractions. The highest emulsifying capacity (389.5 m2
/g), emulsifying
stability (53.2 min), foaming capacity (30.47%), and foaming stability (10.40%) were obtained from the control gelatin sample.
Moreover, the BF3 (≥10 kDa) peptide fraction showed an excellent fat binding capacity (9.39 mL/g). Enzymatic hydrolysis
decreased emulsifying and foaming capacity of gelatin while increasing its fat binding capacity. In particular, antioxidant and
anticancer activities of peptide fractions with low molecular weight were found to be high. The results demonstrated that gelatin
and hydrolysates from the SBS offer an important alternative as a functional food ingredient for food technology.
Keywords: sea bass skin; gelatin peptide fractions; bioactive peptides; in-vitro cytotoxic activity; functional properties.
Practical Application: Bioconservation of fish skin waste into valuable product has highly potential to reduce pollution and
industrial cost and thus, to provide economic development. Peptides with different molecular weights are produced from fish
waste by enzymatic hydrolysis and can be concentrated with ultrafiltration membrane. The low molecular weight peptides
obtained can be used as function
... Furthermore, the presence of specific amino acids and their distribution and special orientation contribute to the overall antioxidative activity. This covers inclusion of aromatic AAs such as Tyr, Trp, and Phe [47,69,70], hydrophobic AAs including Val, Leu, and Ala [47,[69][70][71][72] sulphur-containing AAs, i.e., Met and Cys [47,69,70], acidic AAs, i.e., Glu and Asp [71,73], alkaline AAs, i.e., His, Lys and Arg [47,70,74,75], as well as Pro [8], which all may dramatically influence the antioxidative activity of peptides. Furthermore, high content of N-terminal Leu, Ala and Val has also been reported to positively affect antioxidant activity [8,76]. ...
Protein hydrolysates show great promise as bioactive food and feed ingredients and for valorization of side-streams from e.g., the fish processing industry. We present a novel approach for hydrolysate characterization that utilizes proteomics data for calculation of weighted mean peptide properties (length, molecular weight, and charge) and peptide-level abundance estimation. Using a novel bioinformatic approach for subsequent prediction of biofunctional properties of identified peptides, we are able to provide an unprecedented, in-depth characterization. The study further characterizes bulk emulsifying, foaming, and in vitro antioxidative properties of enzymatic hydrolysates derived from cod frame by application of Alcalase and Neutrase, individually and sequentially, as well as the influence of heat pre-treatment. All hydrolysates displayed comparable or higher emulsifying activity and stability than sodium caseinate. Heat-treatment significantly increased stability but showed a negative effect on the activity and degree of hydrolysis. Lower degrees of hydrolysis resulted in significantly higher chelating activity, while the opposite was observed for radical scavenging activity. Combining peptide abundance with bioinformatic prediction, we identified several peptides that are likely linked to the observed differences in bulk emulsifying properties. The study highlights the prospects of applying proteomics and bioinformatics for hydrolysate characterization and in food protein science.
... The interfacial (emulsion stability index, emulsion activity index) and the surface (foaming stability and capacity) properties decreased when the degree of hydrolysis increased [709]. Rainbow trout roe protein hydrolysates were obtained via pepsin or Alcalase hydrolysis presented essential amino acids in a very interesting proportion [710]. In another paper, hydrolysates from the livers of Oncorhynchus keta and Oncorhynchus gorbuscha were produced using different proteases and Alcalase was the most efficient one [711]. ...
This review aims to cover the uses of the commercially available protease Alcalase in the production of biologically active peptides since 2010. Immobilization of Alcalase has also been reviewed, as immobilization of the enzyme may improve the final reaction design enabling the use of more drastic conditions and the reuse of the biocatalyst. That way, this review presents the production, via Alcalase hydrolysis of different proteins, of peptides with antioxidant, angiotensin I–converting enzyme inhibitory, metal binding, antidiabetic, anti-inflammatory and antimicrobial activities (among other bioactivities) and peptides that improve the functional, sensory and nutritional properties of foods. Alcalase has proved to be among the most efficient proteases for this goal, using different protein sources, being especially interesting the use of the protein residues from food industry as feedstock, as this also solves nature pollution problems. Very interestingly, the bioactivities of the protein hydrolysates further improved when Alcalase is used in a combined way with other proteases both in a sequential way or in a simultaneous hydrolysis (something that could be related to the concept of combi-enzymes), as the combination of proteases with different selectivities and specificities enable the production of a larger amount of peptides and of a smaller size.
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... The values of in vitro antioxidants of monkfish hydrolysates were less active and valuable than compared with the data of the hydrolysates from herring, hoki, and trout [38][39][40], but showed similar values of DPPH (around 50%) than those recently reported for the head of L. vomerinus [23]. The present bioactivities are also in line with the results reported in FPH generated from discarded fish and turbot by-products [14,[41][42][43]. ...
The aim of this work was the recovery of protein substrates from monkfish waste (heads and viscera) generated in the on-board processing of this species. Initially, the effect of pH, temperature, and protease concentration was studied on mixtures of a 1:1 ratio (w/v) of monkfish heads/water. The optimal conditions of proteolytic digestion were established at 57.4 °C, pH 8.31, [Alcalase] = 0.05% (v/w) for 3 h of hydrolysis. Later on, a set of hydrolysis at 5L-pH-stat reactor were run under the aforementioned conditions, confirming the validity of the optimization studies for the head and viscera of monkfish. Regarding the chemical properties of the fish protein hydrolysates (FPH), the yield of digestion was higher than 90% in both cases and the degrees of hydrolysis and the soluble protein content were not especially large (<20% and <45 g/L, respectively). In vitro digestibility was higher than 90% and the percentage of essential amino acids ranged from 40 to 42%. Antioxidant activities were higher in viscera FPH, and antihypertensive ability was superior in head FPH. The values of number average molecular weights (Mn) of monkfish hydrolysates were 600 Da in the viscera and 947 Da in the head. The peptide size distribution, obtained by size-exclusion chromatography, indicated that the largest presence of peptides below 1000 Da and 200 Da was observed in the viscera FPH.
... Further research using chickpea seed protein showed better antioxidative activity after hydrolyzation to protein hydrolysates by pepsin. The similar enzymatic hydrolyzation also produced protein hydrolysates with stronger antioxidative activity from rainbow trout (Mahsa, Parastoo, & Bahare, 2018), Rapana venosa meat (Fenglei, Ronge, & Xueqin, 2018), and crab shell (Wei, Shiwei, & Shijie, 2017). Some of these antioxidative hydrolysates have been purified and sequenced. ...
A two‐step process of enzymatic hydrolyzation followed by Maillard reaction was used to produce oyster meat hydrolysate Maillard reaction products (MRPs). The flavor of oyster meat hydrolysate MRPs was significantly improved through an optimized orthogonal experimental design. Comparisons between the antioxidative activities of oyster meat hydrolysates and their MRPs were made using lipid peroxidation inhabitation, hydroxyl radical scavenging radical activity, and radical scavenging activity of 2,2 diphenyl‐1‐picrylhydrazyl (DPPH). These methods indicated that an improvement of Maillard reaction on the oyster meat hydrolysates antioxidative activity. Gas chromatography‐mass spectrometry illustrated that the increase was due to the newly formed antioxidative compounds after Maillard reaction, mainly of acids from 22.45% to 37.77% and phenols from 0% to 9.88%. Optimized process for oyster meat Maillard reaction products with the best sensory. Increased antioxidative activity of oyster meat Maillard reaction products. Increased antioxidative (phenolic and acids) compounds after Maillard reaction.
... of physically stable emulsion like pea, soy, and lupine (Benjamin, Silcock, Beauchamp, Buettner, & Everett, 2014;Chalamaiah, Jyothirmayi, Diwan, & Dinesh Kumar, 2015;Embiriekah, Bulatović, Borić, Zarić, & Rakin, 2018;Rajabzadeh, Pourashouri, Shabanpour, & Alishahi, 2018). In addition, the protein from animal is another promising possibility applied in the emulsion, which are easily accepted by the consumer for its high nutrition value. ...
The emulsifying and antioxidant properties of chicken protein hydrolysates for the physical and oxidative stabilization of chicken oil‐in‐water emulsion were investigated. The chicken protein pepsin hydrolysates obtained at reaction temperature of 33℃, 1.8% enzyme addition, liquid–solid ratio of 5:1, and reaction time of 4h, showed the DPPH radical scavenging rate of 92.12% and emulsion stability index of 0.07. The hydrolysate exerted significantly improved antioxidant activity and emulsion ability compared to the native chicken protein. The amino acid composition analysis indicated that the contents of hydrophobic amino acids including tyrosine, phenylalanine, and tryptophan were increased after hydrolysis, which contributed to the higher hydrophobicity and antioxidant activity of chicken hydrolysates. The results suggested that the chicken protein hydrolysates could be used as an alternative protein emulsifier for the production of oxidatively stable chicken oil‐in‐water emulsion. The chicken hydrolysates exhibited good antioxidant activity and emulsion ability, which can be used to protect chicken oil from oxidation.
... In the present study, we detected 5.7% aromatic amino acids (AAAs), 22.4% negatively charged amino acids (NCAAs), and 48.1% hydrophobic amino acids (HAAs) in the EHPs (Table 1). In general, EHPs contain all essential amino acids and are rich in glutamate, which significantly affected the antioxidant properties [16]. ...
In this study, the antioxidant components in co-culture of Chlorella pyrenoidosa and Yarrowia lipolytica (3:1 ratio) were confirmed as trypsin-hydrolyzed peptides (EHPs). The EHPs were composed of 836 different peptides with molecular weights ranging from 639 to 3531 Da and were mainly composed of hydrophobic amino acids (48.1%). These peptides showed remarkable protective effects against oxidative stress in HepG2, which may be attributed to their structures. Furthermore, the mRNA and protein levels of nuclear factor erythroid 2-related factor 2 (Nrf2) were significantly lower in the peptide-treated group than in the control group, suggesting that the antioxidant enzyme-coding genes were not activated. The EC50 value of three peptides in the EHPs were in the order of AGYSPIGFVR (0.04 ± 0.002 mg/mL) > VLDELTLAR (0.09 ± 0.001 mg/mL) > LFDPVYLFDQG (0.41 ± 0.03 mg/mL); these results agreed with the prediction of the model (R2 > 0.9, Q2 > 0.5). Thus, EHPs show potential as potent new antioxidant agents.
An expanding list of marine species has been identified and evaluated for their potential bioactivity and nutritional values. Most attention is directed toward utilising protein‐rich by‐products of fish processing for their bioactive functionalities, which can aid in minimising waste and add value to underutilised resources. Milt and roe, the reproductive constituents of fish, are known to contain a high concentration of nutritional content. Bioactive peptides derived from these constituents have shown several biological activities including antihypertensive, antibacterial, anticoagulant, anti‐inflammatory, anti‐obesity, anti‐cancer, and antioxidant activities. These peptides are commonly extracted by enzymatic hydrolysis and purified by different chromatographic methods according to their mass, molecular size, and composition. This review discusses the approaches to produce, purify, and characterise the protein hydrolysates from fish milt and roe and delves into the compositions of the nutraceutical compounds derived from milt and roe. The review also highlights the bioactive properties of the milt and roe‐derived peptides that can have potential applications in the food, nutraceutical, pharmaceutical, and cosmeceutical industries.
This study aims to assess the physicochemical and mechanical properties of O/W emulsion gels formulated with quinoa protein partial hydrolysates (QPH). The effect of varying QPH concentrations (0.5%, 1%, and 2%) on these attributes was also investigated. The QPH were obtained from quinoa protein concentrate (QPC) after treatment with alcalase. Surface hydrophobicity (S0) and emulsifying properties of QPH suspensions were determined. Microstructure, color, water holding capacity (WHC), thermal stability, as well as textural properties of the formulated emulsion gels, were also evaluated. After the hydrolysis treatment, S0 exhibited a significant increase (p = 0.006). The emulsifying activity of QPH also increased (p = 0.002), while the emulsion stability decreased (p < 0.000) as QPH concentrations increased. Confocal laser scanning microscopy images showed that in QPH-based emulsion gels, oil droplets seemed to be more associated with each other forming a three-dimensional network that was less bound to the matrix, in comparison with QPC-based emulsion gels. In addition, hydrolysis produced a significant reduction in WHC of emulsion gels (p = 0.000); however, in all samples evaluated the WHC was around 70%. Furthermore, after heat treatment, there was a decrease in this parameter (p < 0.000). The evaluation of textural properties showed that hardness was significantly lower for emulsion gels formulated with QPH (p < 0.000); whereas no differences between emulsion gels with 0.5% QPC and those with 0.5, 1, and 2% QPH were obtained. Therefore, hydrolysates have the potential to be used in emulsion gel formulation and could be applied to the development of soft-solid food products.
Increased oceanic temperature due to climatic change is gradually decreasing the production rates of Pyropia yezoensis in South Korea, which accounts for 50 % of the global supply. This study demonstrates the antioxidant property of a newly developed edible marine red algae, heat-resistant P. yezoensis (HrP). The water extract of HrP displayed a notably higher reactive oxygen species (ROS) scavenging effect on DPPH, alkyl, hydroxyl radicals, and H2O2 than the commercial P. yezoensis water extract. To increase the radical scavenging ability of HrP, it was enzymatically hydrolyzed using seven enzymes (Alcalase, Celluclast, Flavourzyme, Neutrase, Protamex, Ultraflo, and Viscozyme). These enzymes-assisted HrP hydrolysates (EHrPs) were evaluated for their free radical scavenging activity. Among them, Neutrase-assisted HrP hydrolysate (NHrP), containing the highest protein content, showed a significant protective effect against H2O2-induced cytotoxicity in Vero cells. The 10 kDa molecular weight cut-off fractionation of NHrP revealed that the filtered fraction (10B; ≤10 kDa) was superior to the unfiltered fraction (10A; >10 kDa) in antioxidant activity. The characterization of the three fractions indicated that the high radical scavenging function mainly depends on the level of proteins. Moreover, 10B treatment ameliorated H2O2-induced oxidative stress in Vero cells and zebrafish embryos (increased survival percentage, and decreased cell death and ROS formation). These data suggest that HrP might be a potential antioxidant for nutraceutical industries.
In this study, hydrolysates of large yellow croaker (Pseudosciaena crocea) roe were prepared by trypsin (Try‐pcRHs) and papain (Pap‐pcRHs). The degree of hydrolysis (DH), molecular weight distribution and iron chelating capacity of hydrolysates were investigated. Moreover, the chelation mechanism of iron‐hydrolysates complex also was investigated by amino acid composition analysis, fourier transform infrared spectrophotometer, fluorescence spectrophotometer and ultraviolet‐visible spectroscopy. These results showed that Try‐pcRHs exhibited higher iron chelating ability with the EC50 value of 0.14 mg/mL than Pap‐pcRHs, which may be due to the higher DH and content of peptide less than 1 KDa. Furthermore, the Asp, Glu, Ser, Pro, Ile, Phe and His in Try‐pcRHs might contribute to the chelation reaction, and the groups of ‐COOH, C=O, N‐H and C‐O were involved in chealtiong of Try‐pcRHs with iron. Therefore, Try‐pcRHs have the potential to be used as iron supplements in food industries.
Fish roe is considered as a highly valuable flavor food in international and domestic markets. Several types of roes from different fish species have been processed into shelf-stable products. Processed fish roe products are available in different forms, including refrigerated or frozen caviar from sturgeon, lightly salted roe (popular as black caviar) from beluga, osetra, and imperial. Physicochemical characteristics such as size, color, proximate composition, fatty acids, antioxidants (vitamins and carotenoids), as well as microbiological profiles of fish roe and its processed products are important since these factors will influence the quality and consumer perceptions of the products. Consumer demand for natural and nutritious processed fish products is gaining more attention, which drives opportunities to add commercial value and improve the functionality of unprocessed roe. Therefore the development of technologies to characterize compounds, including physicochemical properties and other microbiology attributes from fish processing by-products is relevant and brings great value. This chapter will contribute to building a current frame of the scientific knowledge on the roe processing and compositional changes, helping to support future developments in this important by-product of the fish processing industry.
In many of the Asian countries, fish roe products are considered important condiments and are consumed not only as a source of dense nutrients but also as a sign of strong cultural customs from the time immemorial. Fish roes are consumed and enjoyed in fresh or processed forms (e.g., salted, fermented, canned, or smoked). The main principles of fish roe processing are the reduction of moisture content and the use of curing agents and spices to enhance shelf life, nutritional value and sensory attributes. Fish roe is rich in protein, contains all essential and nonessential amino acids and has tremendous bioactivities such as anticancer, antiinflammatory, antihypertensive, and immunomodulatory activities. The lipid fraction of fish roe contains a substantial amount of the health-beneficial long-chain ω-3 polyunsaturated fatty acids, for example, eicosapentaenoic acid (EPA, C20:5n3) and docosahexaenoic acid (DHA, C22:6n3). These essential fatty acids are effective in preventing atherosclerosis, maintaining favorable blood lipid profile, aiding in brain maturity, exerting antiinflammatory activity, and relieving rheumatoid arthritis. Also, there are some health-beneficial fatty acids such as linoleic acid, linolenic acid, arachidonic acid, palmitoleic acid, and oleic acid available in fish roe. Additionally, fish roe contains a substantial amount of essential trace elements, that is, K, S, P, Na, Mg, and Zn, which contribute to crucial biological functions and health benefits. However, fish roe and roe products are associated with several biological, chemical, and physical hazards if they are not handled and processed properly, which makes them unsafe for consumption. Therefore guidelines and processing recommendations have been streamlined to ensure that the roe and roe products are safe for public health.
Two experiments were conducted to assess the potential of replacing complex weanling pig diets with simple corn-soybean meal (SBM) diets by supplementation with a feed additive. The effort was made to determine the optimum inclusion rate of fish peptides in experiment 1 (Exp. 1), whereas the possibility of replacing complex diets with simply corn-SBM diets was investigated in Exp. 2. Ninety six (7.9 ± 0.7 kg) and 48 (7.8 ± 0.8 kg) pigs were used in Exp. 1 and 2, respectively, and pigs were assigned randomly to 6 (Exp. 1) and 3 (Exp. 2) dietary treatments with 4 pens per treatment and 2 gilts and 2 castrated males per pen in both experiments. The phase 1 (d 0 to 14) and 2 (d 14 to 28) complex, positive control diets (POS) were formulated in both experiments. Two simple corn-SBM, negative control (NEG) diets were formulated to be iso-lysinic to the POS diets in Exp. 1, and the NEG diets were supplemented with 0.5, 1.0, 1.5, or 2.0% fish peptides. Similarly, the phase 1 and 2 simple corn-SBM, NEG diets were formulated to be iso-lysinic to the POS diets in Exp. 2. However, the NEG diets contained 1.5% fish peptides, and those diets were supplemented with multienzyme complexes (ALL). During the wk 4, blood sample was collected and analyzed for serum metabolites and cytokines in Exp. 1 and metabolites in Exp. 2. During the last 2 wk of Exp. 1, the intake of feed, Lys, and digestible energy (DE) increased (cubic, P < 0.026) as fish peptides increased from 0 to 2%. Dietary treatments had no effect on gain to feed (G:F), gain to Lys (G:Lys), or gain to DE (G:DE) intake. Although there were some differences in serum total protein, urea N, and triglycerides, dietary treatments seemed to have no clear effect on serum metabolites or cytokines. Pigs seemed to respond to the diets containing 1.5% fish peptides, and it was used as the basis for the dietary treatments in Exp. 2. From wk 0 to 2 in Exp. 2, pigs fed the NEG and ALL diets had greater G:F, G:Lys intake, and G:DE intake (P < 0.004) than those fed the POS diet. In addition, G:F and G:Lys intake tended to be greater (P = 0.095) and G:DE intake was greater (P = 0.009) in pigs fed the ALL diet than those fed the NEG diet. Dietary treatments had no clear effect on the growth performance during the phase 2 or overall. Serum total protein and globulin were greater (P < 0.007) in pigs fed the NEG and ALL diets than those fed the POS diets because of the greater values in pigs fed the ALL diets, but those metabolites were not different between pigs fed the NEG and ALL diets. The results indicated that a complex diets can be replaced with a simple corn-SBM diet by supplementing the weanling pig diet with fish peptides and multienzyme complexes during the phase 1 (d 0 to 14).
In this study, to improve the quality and shelf life of hamburgers, sesame meal protein hydrolysates (SPH) were produced using two enzymes of alcalase and flavourzyme and then four hamburger treatments: T1: control (10% soybean), T2: 1% SPH + soybean 9%, T3: 2% SPH + soybean 8%, and T4: 3% SPH + soybean 7% were prepared. Physicochemical properties were analyzed at the beginning of the storage period; microbial and chemical quality was evaluated at intervals of 0, 4, 8, 12, and 16 days. The results of SPH showed that alcalase enzyme can produce a SPH with a higher antioxidant properties (DPPH, FRAP, and beta‐carotene‐linoleic acid) (P < 0.05); therefore, this SPH was used for hamburger properties. According to the results, with the addition of SPH, moisture, fat, texture firmness decreased, protein, and brightness increased (P < 0.05), and all treatments had the allowable range. SPH replacement with soybean slowed down the increasing trend of oxidation and microbial spoilage (P < 0.05). In general, better results were observed in T3 and T4, which had a permissible range chemical and microbial index until the end of the storage period, as well as these treatments inhibited the growth of Staphylococcus aureus and Escherichia coli. Only T3 was approved by the evaluators.
Mayonnaise is a semi-solid oil-in-water emulsion that in addition to eggs other stabilizers and thickeners are used as emulsifiers for better stability. Although eggs are an important ingredient in the production of mayonnaise, the health problems associated with the use of eggs is increasing due to their high cholesterol content. The aim of this study was to evaluate the feasibility of clover sprout protein hydrolysates (CSPH) to replace eggs for the production mayonnaise. First, CSPH was produced using alcalase and flavourzyme enzyme, and in order to find the best enzyme, the degree of hydrolysis (DH) and protein recovery (PR) were determined. Then four mayonnaise treatments included, T1: control (egg 9%), T2: egg 6%+ CSPH 3%, T3: egg 3%+ CSPH 6%, T4: egg 0%+ CSPH 9% was prepared and the stability, viscosity, physicochemical, textural, and sensory properties of mayonnaise was investigated. The samples containing CSPH showed that CSPH had high essential amino acids, CSPH from alcalase enzyme had higher amounts of protein, DH, PR, and increasing hydrolysis time had a positive effect on these parameters (p < .05); therefore, CSPH from alcalase enzyme was used for the production mayonnaise. The stability, viscosity, firmness, adhesion of texture, and pH increased with increasing CSPH, while the brightness, acidity, and sensory score of the samples decreased (p < .05). In general, T3 had an acceptable quality in terms of the studied characteristics, but sensory score in T4 could not be confirmed. Hence, by replacing eggs with CSPH up to 6%, mayonnaise with appropriate physicochemical and sensory properties can be produced. Therefore, the formulation egg 3%+ CSPH 6% is an appropriate choice to produce mayonnaise for consumers who are on a restricted diet to eat foods containing eggs.
Fish protein hydrolysates (FPH) obtained from industrial processing residues are sources of bioactive peptides. The enzymatic hydrolysis process is essential in obtaining specific bioactivities such as inhibition of the enzyme acetylcholinesterase (AChE). In this study the effect of different hydrolysis conditions on the properties of FPH to inhibit the enzyme acetylcholinesterase. A chemometric evaluation, based on a central composite rotatable design and principal component analysis, was applied to select hydrolysis conditions with best yield, degree of hydrolysis and acetylcholinesterase inhibition. Experimental design results for AChE inhibition were between 10.51 and 40.45% (20, 30 and 50 mg.mL-1 of FPH), and three hydrolysis conditions were selected based on PCA evaluation. The amino acids profile, FTIR and AChE inhibition kinetics were evaluated. Results showed a mixed type of inhibition behavior and, the docking molecular analyzes suggest that the inhibition AChE occurred due to the basic amino acids, mainly by arginine.
The article studies the effect of using complete compound feeds with different energy levels on the morphological composition of the body and the amino acid composition of trout meat proteins. The experiment aimed to establish the influence of different levels of energy nutrition of commercial rainbow trout on the morphological composition of their body and the amino acid composition of meat proteins. For this purpose, five experimental groups were formed using the analog method. The study lasted 210 days and was divided into two periods: comparative (10 days) and main (200 days). During the comparative period, the study fish consumed compound feed of the control group. During the main period, the energy level in experimental compound feeds for different experimental trout groups ranged from 16 to 20 mJ per 1 kg. It was found that with an increase in the mass of two-year-old trout, the mass of muscle tissue and the yield of edible parts probably increases. Feeding fish with an increased amount of metabolic energy (20 mJ.kg-1) resulted in a significant change in the weight of internal organs, including the heart, liver, and kidneys. Increasing the metabolic energy in the compound feeds of fish from 18 mJ.kg-1 to 19 – 20 mJ.kg-1 leads to a significant increase in bowel mass by 13.3 – 5.0%. An increase in the level of metabolic energy in rainbow trout diets from 18 mJ.kg-1 to 19 – 20 mJ.kg-1 contributed to a likely increase in the methionine content in meat. A similar pattern was observed for the tryptophan content. It was found that the content of most essential amino acids in the protein of rainbow trout meat exceeds the corresponding values in the "ideal" protein, except for the content of isoleucine and leucine, which refers them to limiting amino acids.
Defatted Sacha inchi seed is an important source of protein (up to 59.1% dry weight). Besides, the application of antioxidant peptides is often limited due to a reduction in their activities by enzymatic hydrolysis during gastrointestinal digestion. Therefore, the objective of this study was to obtain stable, anti-digestive and strongly antioxidative protein hydrolysates against non-communicable diseases (NCDs) by investigating the changes in the antioxidant capacities of the protein fractions (albumin, globulin and glutelin) from Sacha inchi seeds (PFFSIS) during simulated gastrointestinal digestion (SGID). The results showed SGID promoted the release of smaller bioactive peptides from PFFSIS evidenced by the increased soluble peptide content, DH and low MW distribution. Besides, the extracellular antioxidant capacity (ABTS•+ radical-scavenging activity, reducing power and ORAC value) and intracellular antioxidant capacity (inhibiting erythrocyte hemolysis by enzyme system (SOD, CAT and GSH-Px) and non-enzyme substances (GSH)) of PFFSIS were significantly increased after the SGID due to potential antioxidant mechanisms inside and outside the cell. The glutelin fraction showed the highest antioxidant activity after the SGID, followed by albumin and globulin fractions. These results highlight the potential application of glutelin fraction hydrolysates of Sacha inchi seeds as natural antioxidant supplements to prevent NCDs.
Fish is an important source of protein with complete and balanced amino acids. In Indonesia, they are available abundantly at a relatively affordable price and found year-round. Thus, they provide human’s need of essential amino acids. For the Indonesian people, fish is the main animal protein source. Since Indonesia still has stunting problems, the Government makes efforts, one of which is the provision of high-protein foods. Fish protein hydrolysates (FPHs) are hydrolysis products of fish protein containing peptides and amino acids that are readily absorbed and beneficial for health. The unique functional properties of FPH and its various bioactivities pay much attention for research to develop their applications for functional foods or nutraceutical products. This review paper highlights the nutritional values, health benefits, and potential application of FPH for food, and gives a brief overview of FPH research in Indonesia.
The aim of the present study is to present a new anchovy protein concentrate and compare it to other similar fishery products. A 76.4% protein concentrate was prepared from fresh Peruvian anchoveta (Engraulis ringens) (APC) by means of acid treatment with 1% citric acid, solubilization with 1% sodium chloride, and isoelectric precipitation processes. Remaining fat was 5.2%, and 0.51 Aw indicates good stability. When APC was rehydrated for 10 minutes, it had a 3.5 initial weight increase. It provided 17.8% protein of very high nutritional quality, with only histidine content deficient for children 1–2 years old. Fat content in APC offered 33.4% EPA+DHA. No changes in the essential/non-essential amino acids (EAA/non-EAA), polyunsaturated/saturated fatty acids (PUFA/SFA), or w6/w3 ratios were observed as a result of the process in the raw material. Because of the high sodium content, a 25 g portion is recommended to fulfill nutritional FAO recommendations. APC can be considered as an important source of calcium (30% adults and 35% children requirements), phosphorous (30% adults and 52% children requirements), and iron content (approximately 20% adults and children needs). APC is an important high-quality protein, providing w-3 fatty acids, calcium, phosphorous, and iron.
Zein is a major by-product of corn processing and has a wide range of applications in many fields due to its unique solubility and specific amino acid composition. The aim of this study is to hydrolyze zein stepwise using alcalase and proteinase K while considering the enzymatic hydrolysis sequence and assessing the zein-chelating ability, solubility, foaming, and emulsification properties of the zein hydrolysate. The antioxidant activity of Zn²⁺ chelating peptide was determined. Zinc-chelating ability was used as the evaluation index, and proteinase K was further hydrolyzed on the basis of alcalase hydrolysis. The optimal hydrolysis conditions were reaction time of 2 h, substrate concentration of 10 mg mL⁻¹, enzyme addition amount of 2.8 U mg⁻¹, reaction temperature of 60 °C, and hydrolysate chelation ability of 12.16 mg g⁻¹, thereby corresponding to a degree of hydrolysis (DH) of 35.30%. On the basis of the hydrolysis by proteinase K, alcalase was further hydrolyzed, and the optimal hydrolysis conditions were reaction time of 3 h, substrate concentration of 10 mg mL⁻¹, enzyme addition amount of 8.0×10⁵ U mg⁻¹, reaction temperature of 50 °C, and hydrolysate chelation ability of 13.72 mg g⁻¹, thereby corresponding to a DH of 29.32%. Zein Zn²⁺-chelating peptide is significant for 1,1-diphenyl-2-picrylhydrazyl free radicals, hydroxyl radicals, and ABTS·⁺. The clearance effect is positively correlated with the mass concentration of the polypeptide. Zein Zn²⁺-chelating peptide has good Zn²⁺ chelating ability and antioxidant activity. Hence, it has broad research prospects for new dietary supplements.
The aim of this work is to provide a timely examination of the structure–activity relationship of antioxidative peptides. The main production approach involves enzymatic hydrolysis of animal and plant proteins to produce protein hydrolyzates, which can be further processed by membrane ultrafiltration into size‐based peptide fractions. The hydrolyzates and peptide fractions can also be subjected to separation by column chromatography to obtain pure peptides. Although the structural basis for enhanced antioxidant activity varies, protein hydrolyzates and peptide fractions that contain largely low molecular weight peptides have generally been shown to be potent antioxidants. In addition to having hydrophobic amino acids such as Leu or Val in their N‐terminal regions, protein hydrolyzates, and peptides containing the nucleophilic sulfur‐containing amino acid residues (Cys and Met), aromatic amino acid residues (Phe, Trp, and Tyr) and/or the imidazole ring‐containing His have been generally found to possess strong antioxidant properties.
Practical applications
High levels of reactive oxygen species (ROS) in addition to the presence of metal cations can lead to oxidative stress, which promotes reactions that cause destruction of critical cellular biopolymers, such as proteins, lipids, and nucleic acids. Oxidative stress could be due to insufficient levels of natural cellular antioxidants, which enables accumulation of ROS to toxic levels. A proposed approach to ameliorating oxidative stress is the provision of exogenous peptides that can be consumed to complement cellular antioxidants. Food protein‐derived peptides consist of amino acids joined by peptides bonds just like glutathione, a very powerful natural cellular antioxidant. Therefore, this review provides a timely summary of the in vitro and in vivo reactions impacted by antioxidant peptides and the postulated mechanisms of action, which could aid development of potent antioxidant agents. The review also serves as a resource material for identifying novel antioxidant peptide sources for the formulation of functional foods and nutraceuticals.
Protein solubility, protein recovery, antioxidant activity, and antigenicity of microwave pretreatment and/or microwave-assisted hydrolysis of trout frame protein hydrolysates was investigated. Treatments consisted of (1) microwave pretreatment at low temperature (55 °C) followed by conventional enzymatic hydrolysis or (2) high temperature (90 °C) followed by conventional enzymatic hydrolysis; (3) microwave pretreatment at high temperature (90 °C) followed by microwave-assisted enzymatic hydrolysis, and (4) no microwave pretreatment followed by microwave-assisted enzymatic hydrolysis. Compared to controls, microwave treatments significantly improved (P < 0.05) protein solubility, protein recovery, degree of hydrolysis, and 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) free radical scavenging radical scavenging activity. Decrease of antigenicity (55–93 %) was obtained in all microwave-treated samples. Based on the results of this study, the use of microwave pretreatment for 5 min at 90 °C, followed by conventional enzymatic hydrolysis with alcalase for 2–10 min was the best treatment condition to produce fish peptides with antioxidant activity and the lowest immunoreactivity. These peptides have potential to be applied as hypoallergenic ingredients in food formulations and nutraceuticals.
Glutamine and glutamate are not considered essential amino acids but they play important roles in maintaining growth and health in both neonates and adults. Although glutamine and glutamate are highly abundant in most feedstuffs there is increasing evidence that they may be limiting during pregnancy, lactation and neonatal growth, particularly when relatively low protein diets are fed. Supplementation of diets with glutamine, glutamate or both at 0.5 to 1.0% to both suckling and recently weaned piglets improves intestinal and immune function and results in better growth. In addition such supplementation to the sow prevents some of the loss of lean body mass during lactation, and increases milk glutamine content. However, a number of important questions related to physiological condition, species under study and the form and amount of the supplements need to be addressed before the full benefits of glutamine and glutamate supplementation in domestic animal production can be realized.
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.
Protein extracted from mussel processing co-products was hydrolyzed with four different food-grade enzyme preparations and assessed for angiotensin converting-enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) inhibitory and oxygen radical antioxidant capacity (ORAC) activities. All hydrolysates tested showed higher activity than the intact protein. ACE and DPP-IV IC50 values in the range 1.13 – 3.34 and 0.33-2.43 mg mL−1, respectively, and ORAC values in the range 66.26-121.56 umol Trolox g−1 were obtained. These results suggest that some of the mussel meat protein hydrolysates may have potential as functional food ingredients for the management of diseases such as type II diabetes and hypertension.
Previously, we have reported the composition, molecular mass distribution and in vivo immunomodulatory effects of common carp roe protein hydrolysates. In the current study, antioxidative activity and functional properties of common carp (Cyprinus carpio) roe (egg) protein hydrolysates, prepared by pepsin, trypsin and Alcalase, were evaluated. The three hydrolysates showed excellent antioxidant activities in a dose dependent manner in various in vitro models such as 2,2 diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, 2,2′–azino-bis(3-ethylbenzthiazoline-6)-sulfonic acid (ABTS+) radical scavenging activity, ferric reducing antioxidant power (FRAP) and ferrous ion (Fe2+) chelating ability. Enzymatic hydrolysis significantly increased protein solubility of the hydrolysates to above 62 % over a wide pH range (2–12). Carp roe hydrolysates exhibited good foaming and emulsification properties. The results suggest that bioactive carp roe protein hydrolysates (CRPHs) with good functional properties could be useful in health food/nutraceutical/pharmaceutical industry for various applications.
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.
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.
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.
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
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.
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.
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.
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.
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
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.
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.
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.
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.
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.
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.
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 H.
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.