Optimization of goldstripe sardine (<i>Sardinella gibbosa</i>) protein hydrolysate using Alcalase® 2.4L by response surface methodology Optimización de hidrolisato de proteína de Sardinela dorada (<i>Sardinella gibbosa</i>) usando Alcalase® 2.4L a través de RSM

Taheri, Ali; Kenari, Abdolmohammad Abedian; Motamedzadegan, Ali; Rezaie, Masoud

doi:10.1080/19476337.2010.484551

Cited by 9 publications

(3 citation statements)

References 40 publications

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“…The lipid content of HPHs ranged between 2% and 3.3% (dry basis), with little variation; however, lipid content in HPHs was slightly lower than values recorded for sardine muscle (4.79%, dry basis). A decrease in the lipid content of fish protein hydrolysates is explained by the fact that the hydrolysis process favors the release of fat in muscle tissues (Taheri et al, 2011); afterward, part of the lipid material that precipitates can be easily separated from the hydrolysate after centrifugation, given the differences in density between the lipid and aqueous phases. A low concentration of lipids is appealing from a technological standpoint because it may translate into increased product stability and shelf life, given the lower possibility of lipid oxidation (Lassoued et al, 2015).…”

Section: Proximate Composition Of Raw Materials and Herring Muscle Hymentioning

confidence: 99%

Influence of enzymatic hydrolysis conditions on biochemical and antioxidant properties of pacific thread herring (Ophistonema libertate) hydrolysates

Sandoval-Gallardo

Osuna-Ruíz²,

Martínez‐Montaño

et al. 2020

CyTA - Journal of Food

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Pacific thread herring (Ophistonema libertate) muscle was hydrolyzed with Alcalase for the preparation of protein hydrolysates. The effect of enzyme concentration (EC; 1% and 3%), pH (8 and 9) and temperature (40°C and 50°C) on some biochemical properties and antioxidant activity (AOXA) was determined. The degree of hydrolysis (DH) ranged between 9.6% and 33.1%. The highest DH was obtained with the following conditons: EC of 3%, pH 9 and temperature of 50°C; however, the highest AOXA measured by DPPH (183.7 µmol TE/mg), FRAP (0.98 µmol TE/mg), and ABTS (144.9 µmol TE/mg) was obtained at EC of 3%, pH 8 and temperature of 50°C. These also exhibited a higher percentage of peptides of MW lower than 1.35 kDa and high concentrations of anionic and cationic amino acids. These results suggest that protein hydrolysates from Pacific thread herring muscle have a potential for application in the formulation of functional food.

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Section: Proximate Composition Of Raw Materials and Herring Muscle Hymentioning

confidence: 99%

Influence of enzymatic hydrolysis conditions on biochemical and antioxidant properties of pacific thread herring (Ophistonema libertate) hydrolysates

Sandoval-Gallardo

Osuna-Ruíz²,

Martínez‐Montaño

et al. 2020

CyTA - Journal of Food

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“…PRESS statistic predicted the residual error sum of square to show how well the model fits the data and smaller the PRESS is preferable [31]. Most studies on optimization of ACE inhibitory activity can be fitted using quadratic model such as for pacific hake [32], goldstripe sardine [33], fish protein hydrolysate from underutilized fish Pellona ditchela [34] tilapia scale gelatine [35], shrimp waste [36] and water-soluble fish [37]. Analysis of variance (ANOVA) statistically evaluated the suggested model to demonstrate which variable would give a significant effect on ACE inhibitory activity.…”

Section: Optimization Of Enzymatic Protein Hydrolysis Conditions Of Angelwing Clam Meat To Obtain Maximum Ace Inhibitory Activity Using Amentioning

confidence: 99%

Optimization of enzymatic protein hydrolysis conditions to obtain maximum angiotensin-iconverting enzyme (ACE) inhibitory activity from Angel Wing Clam (Pholas orientalis) meat

Amin¹

2017

Madridge J Food Tech

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Optimization of enzymatic protein hydrolysis conditions of angel wing clam (Pholas orientalis) meat to yield maximum angiotensin I-converting enzyme inhibitory (ACE inhibitory) activity was carried out using Response Surface Methodology (RSM). Protein content in angel wing clam meat was 9.04 ± 0.06%. To determine food grade enzyme and range of hydrolysis time to be used in optimization study, screening study was carried out. Four commercial food grade enzymes (Alcalase ® , Protamex™, Neutrase ® and papain) at 2 and 4 hours hydrolysis time were used to yield the highest ACE inhibitory activity. A further screening study were done on Alcalase ® and papain at 1 hour hydrolysis time. It was found that Alcalase ® (75.86% ± 2.64) and papain (77.13% ± 2.63) at 1 hour hydrolysis time exhibited the highest ACE inhibitory activity. However, Alcalase ® was chosen for the hydrolysis in the optimization study. Four protein hydrolysis parameters including temperature (50˚C-60˚C), pH (6.5-8.5), hydrolysis time (30 minutes -90 minutes) and enzyme to substrate (E/S) ratio (1.0% -2.0%) were employed at three level using a face-centered central composite design (CCD) by using RSM. The enzymatic hydrolysis of angel wing clam meat towards ACE inhibitory activity can be predicted by using quadratic model. The optimum hydrolysis conditions to yield maximum ACE inhibitory activity was at 54.8˚C, pH of 7.7, 33 minutes of hydrolysis time and E/S ratio of 1.0%. It was found that the predicted value of ACE inhibitory activity (85.21%) was close to the experimental value (85.64%). This study shows that RSM can be applied successfully to describe interrelationship between hydrolysis conditions and ACE inhibitory activity. On the other hand, the half maximal inhibitory concentration (IC 50 ) value for angel wing clam meat hydrolysate prepared under optimum condition was 3.63mg/ml±0.48.

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“…Alcalase ® 2.4L, synthesized by the Bacillus species, operates optimally under mildly alkaline conditions. As an endopeptidase-rich commercial protease formulation, it can effectively break many proteins down into smaller peptides and amino acids [18]. To investigate its hydrolysis efficiency, the protein recovery and DH of elastin hydrolysates obtained at different hydrolysis times by Alcalase ® 2.4L were evaluated.…”

Section: Introductionmentioning

confidence: 99%

Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping

Zhang,

Liu,

Jiang

et al. 2023

Molecules

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To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate’s bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase® 2.4L’s preference for these residues. The analysis not only confirms the peptides’ dose-responsive elastase inhibitory potential but also underscores the nuanced interplay between peptide content, biological function, and their collective synergy. The study sets the stage for future research aimed at refining enzymatic treatments to fully exploit the bioactive properties of elastin.

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Optimization of goldstripe sardine (Sardinella gibbosa) protein hydrolysate using Alcalase® 2.4L by response surface methodology Optimización de hidrolisato de proteína de Sardinela dorada (Sardinella gibbosa) usando Alcalase® 2.4L a través de RSM

Cited by 9 publications

References 40 publications

Influence of enzymatic hydrolysis conditions on biochemical and antioxidant properties of pacific thread herring (Ophistonema libertate) hydrolysates

Influence of enzymatic hydrolysis conditions on biochemical and antioxidant properties of pacific thread herring (Ophistonema libertate) hydrolysates

Optimization of enzymatic protein hydrolysis conditions to obtain maximum angiotensin-iconverting enzyme (ACE) inhibitory activity from Angel Wing Clam (Pholas orientalis) meat

Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping

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