Bioactivity and Functionality of Gelatin Hydrolysates from the Skin of Oneknife Unicornfish (
            <i>Naso thynnoides</i>
            )

Alolod, Garner Algo L.; Nuñal, Sharon N.; Nillos, Mae Grace; Peralta, Jose P.

doi:10.1080/10498850.2019.1682094

Cited by 11 publications

(16 citation statements)

References 39 publications

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“…As a result, they quickly disrupt the emulsion process. Similar studies have observed that emulsion stability is improved with increasing the molecular weight of peptides [34,35].…”

Section: Emulsifying Propertiessupporting

confidence: 76%

Bioactive Peptide Fractions from Collagen Hydrolysate of Common Carp Fish Byproduct: Antioxidant and Functional Properties

et al. 2022

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Collagen isolated from byproducts of common carp was hydrolyzed with alcalase enzyme to obtain peptide fractions. The resulting >30 kDa (PF1), 10–30 kDa (PF2), 3–10 kDa (PF3) and <1 kDa (PF4) fractions were studied for their antioxidant and functional properties. All peptide fractions illustrated antioxidant activity at different concentrations (1, 5, and 10 mg/mL). Although PF4 indicated the highest DPPH radical-scavenging activity (87%) at a concentration of 1 mg/mL, the highest reducing power (0.34) and hydroxyl radical scavenging activity (95.4%) were also observed in PF4 at a concentration of 10 mg/mL. The solubility of the peptide fractions was influenced by pH. The lowest solubility of the peptide fractions was observed at pH 4. The highest emulsifying activity index (EAI) was observed for PF4 (121.1 m2/g), followed by PF3 (99.6 m2/g), PF2 (89.5 m2/g) and PF1 (78.2 m2/g). In contrast to what has been found in the case of EAI, the emulsion stability of the peptide fractions decreased at lower molecular weight, which ranged from 24.4 to 31.6 min. Furthermore, it was revealed that PF1 had the highest foam capacity (87.4%) and foam stability (28.4 min), followed by PF2 and PF3. Overall, the findings suggest that peptide fractions isolated from byproducts of common carp are a promising source of natural antioxidants for application in functional food and pharmaceutical products.

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“…As a result, they quickly disrupt the emulsion process. Similar studies have observed that emulsion stability is improved with increasing the molecular weight of peptides [34,35].…”

Section: Emulsifying Propertiessupporting

confidence: 76%

Bioactive Peptide Fractions from Collagen Hydrolysate of Common Carp Fish Byproduct: Antioxidant and Functional Properties

et al. 2022

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“…Smaller molecules are less efficient at reducing interfacial stress and hence the emulsion of these compounds will break down at a higher rate. Alolod [ 48 ] stated that the emulsion properties of gelatin hydrolysates of unicorn skin depend to a large extent on the concentration and size of peptides. Smaller peptides move faster into the water–oil interfacial space and form an emulsion, but emulsions are not very stable due to the reduced hydrophobic-hydrophilic balance on both sides of the emulsion surfaces.…”

Section: Resultsmentioning

confidence: 99%

“…3 ). Alolod [ 48 ] reported that the foaming capacity of the hydrolysates of unicorn fish skin gelatin was 5.83% higher than the control sample. In this study, the foaming capacity depended on the molecular weight of the hydrolysates, and the weakness in the foaming capacity was observed in low molecular weight hydrolysates.…”

Section: Resultsmentioning

confidence: 99%

Assessment of the biotechnological activity of wheat hydrolysates prepared with the Biarum bovei extract

Khosravi

H²,

Azizi

et al. 2022

Food Measure

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In this study, Biarum bovei extract was used to produce bioactive peptides from wheat gluten protein and the biological and functional properties of the hydrolysates were determinated. The results showed that Biarum bovei extract has its highest protease activity (7.3 U/mg protein) at 45 °C and pH 5. Based on electrophoresis analysis, the molecular weight of hydrolysate was < 10 kDa. F1 fraction had the highest antioxidant activity in DPPH (65.85 ± 2.64 µmol TE/g)) and ABTS radical scavenging assays (295.81 µmol TE/g). F2 fraction with 86.3 ± 0.48 had the ability to inhibit the ACE enzyme. The F3 and F1 fractions had statistically the highest inhibition rate (49.37 ± 0.12%. and 79.19 ± 1.13%) in alpha-glucosidase and alpha amylase, respectively. The F1, F2 fractions hydrolysate had an inhibitory effect on Escherichia coli , Staphylococcus aureus , Listeria monocytogenes and Bacillus cereus . Functional properties of hydrolysates with increasing molecular weight, increased significantly. The presence of high levels (p ≤ 0.05) of amino acids with hydroxyl groups, hydrophobic and positive charged in fractions had critical role on biological and technological activity. These findings confirmed the efficiency of gluten hydrolysates with low molecular weight (F1 < 3 kDa) on biofunctionality such as scavenging radical activity, ACE inhibitory, antidiabetic and antibacterial activity could be beneficial from health and technological perspectives.

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“…The ACE inhibitory activity of the ultrafiltration fraction depending on the protein concertation and the IC 50 value of 10.17

\umu

g/ml was determined. The amino acid composition of the fraction revealed the presence of a high level of glycine and glutamic acid/glutamine, which plays a vital role in the inhibitory effect (Alolod et al., 2019). A di‐peptide (AY) have been isolated and identified from the carp ( C. carpio ) skin hydrolysate with ACE inhibitory activity using HPLC and MS/MS, respectively (Tkaczewska et al., 2019).…”

Section: Biological Activities Of Fph (In Vitro Studies)mentioning

confidence: 99%

Valorization of fish byproducts: Sources to end‐product applications of bioactive protein hydrolysate

Nirmal

Santivarangkna

Rajput

et al. 2022

Comp Rev Food Sci Food Safe

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Fish processing industries result in an ample number of protein‐rich byproducts, which have been used to produce protein hydrolysate (PH) for human consumption. Chemical, microbial, and enzymatic hydrolysis processes have been implemented for the production of fish PH (FPH) from diverse types of fish processing byproducts. FPH has been reported to possess bioactive active peptides known to exhibit various biological activities such as antioxidant, antimicrobial, angiotensin‐I converting enzyme inhibition, calcium‐binding ability, dipeptidyl peptidase‐IV inhibition, immunomodulation, and antiproliferative activity, which are discussed comprehensively in this review. Appropriate conditions for the hydrolysis process (e.g., type and concentration of enzymes, time, and temperature) play an important role in achieving the desired level of hydrolysis, thus affecting the functional and bioactive properties and stability of FPH. This review provides an in‐depth and comprehensive discussion on the sources, process parameters, purification as well as functional and bioactive properties of FPHs. The most recent research findings on the impact of production parameters, bitterness of peptide, storage, and food processing conditions on functional properties and stability of FPH were also reported. More importantly, the recent studies on biological activities of FPH and in vivo health benefits were discussed with the possible mechanism of action. Furthermore, FPH‐polyphenol conjugate, encapsulation, and digestive stability of FPH were discussed in terms of their potential to be utilized as a nutraceutical ingredient. Last but not the least, various industrial applications of FPH and the fate of FPH in terms of limitations, hurdles, future research directions, and challenges have been addressed.

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Bioactivity and Functionality of Gelatin Hydrolysates from the Skin of Oneknife Unicornfish ( Naso thynnoides )

Cited by 11 publications

References 39 publications

Bioactive Peptide Fractions from Collagen Hydrolysate of Common Carp Fish Byproduct: Antioxidant and Functional Properties

Bioactive Peptide Fractions from Collagen Hydrolysate of Common Carp Fish Byproduct: Antioxidant and Functional Properties

Assessment of the biotechnological activity of wheat hydrolysates prepared with the Biarum bovei extract

Valorization of fish byproducts: Sources to end‐product applications of bioactive protein hydrolysate

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