2015
DOI: 10.1016/j.jff.2014.12.042
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Characterization and comparative assessment of antioxidant and ACE inhibitory activities of thornback ray gelatin hydrolysates

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Cited by 87 publications
(68 citation statements)
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References 52 publications
(52 reference statements)
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“…This is because it affects size, amount, amino acid composition and amino acid sequence of the peptides produced, which in turn influences the bioactive and functional properties of the hydrolysates (Sarmadi and Ismail, 2010). Although crude proteases extracts (e.g., from fish) have been successfully used as catalysts in enzymatic hydrolysis Lassoued et al, 2015b), commercially purified enzymes are preferably employed since they allow a better control over the hydrolysis process (e.g., shorter reaction time for a desired DH, more consistent peptides size and composition) (Samaranayaka and Li-Chan, 2011). Consequently, industrial proteases derived from different sources such as microorganisms (e.g., Alcalase, Neutrase, Protease P "Amano" 6, Flavourzyme, Protamex) (Halldorsdottir et al, 2013;Venuste et al, 2013), animals (e.g., PTN, pepsin, trypsin, a-chymotrypsin, pancreatin) (Wu et al, 2015a, b;Garc ıa-Moreno et al, 2017) and plants (e.g., papain, bromelain) (Salampessy et al, 2015;Elavarasan et al, 2016) have been widely employed for the production of protein hydrolysates exhibiting bioactive and/or functional properties.…”
Section: Enzymatic Protein Hydrolysismentioning
confidence: 99%
“…This is because it affects size, amount, amino acid composition and amino acid sequence of the peptides produced, which in turn influences the bioactive and functional properties of the hydrolysates (Sarmadi and Ismail, 2010). Although crude proteases extracts (e.g., from fish) have been successfully used as catalysts in enzymatic hydrolysis Lassoued et al, 2015b), commercially purified enzymes are preferably employed since they allow a better control over the hydrolysis process (e.g., shorter reaction time for a desired DH, more consistent peptides size and composition) (Samaranayaka and Li-Chan, 2011). Consequently, industrial proteases derived from different sources such as microorganisms (e.g., Alcalase, Neutrase, Protease P "Amano" 6, Flavourzyme, Protamex) (Halldorsdottir et al, 2013;Venuste et al, 2013), animals (e.g., PTN, pepsin, trypsin, a-chymotrypsin, pancreatin) (Wu et al, 2015a, b;Garc ıa-Moreno et al, 2017) and plants (e.g., papain, bromelain) (Salampessy et al, 2015;Elavarasan et al, 2016) have been widely employed for the production of protein hydrolysates exhibiting bioactive and/or functional properties.…”
Section: Enzymatic Protein Hydrolysismentioning
confidence: 99%
“…The activity increased 7.5-fold, suggesting that ACE inhibitory peptides are encrypted within the sequence of the parent protein. High ACE inhibitory activity of TRGH-Alcalase was attributed to the high level of hydrophobic peptides [19]. Byun, et al [15] reported also the ACE inhibitory activity of Alaska pollack skin digested by Alcalase; the IC 50 value is 0.629 mg/ml.…”
Section: Ace Inhibitory and Antioxidant Activitiesmentioning
confidence: 99%
“…Thornback Ray Gelatin Hydrolysate (TRGH) generated by Alcalase, was prepared according to Lassoued, et al [19]. The degree of hydrolysis, defined as the percent ratio of the number of peptide bonds broken to the total number of peptide bonds per unit weight (h tot ), in each case, was calculated from the amount of base (NaOH) added to keep the pH constant during the hydrolysis [22].…”
Section: Preparation Of Thornback Ray Gelatin Hydrolysate (Trgh)mentioning
confidence: 99%
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