Purification and identification of antioxidative peptides from mackerel (<i>Pneumatophorus japonicus</i>) protein

Wang, Xueqin; Yu, Huahua; Xing, Ronge; Chen, Xiaolin; Li, Rongfeng; Li, Kecheng; Liu, Song; Li, Pengcheng

doi:10.1039/c8ra03350a

Cited by 11 publications

(9 citation statements)

References 35 publications

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“…Nevertheless, our data do not suggest a general correlation between increased hydrolysis and increased antioxidant activity, although several studies have found antioxidative peptides to be rather short and usually in the range 5-16 AAs [8,50,63,64]. However, the highest DPPH RSA was found for the FPHs obtained by sequential hydrolysis (i.e., highest DH and lowest PCL) for both MCF and HCM compared to other treatments on the same substrate [65]. There does not appear to be any apparent correlation with the mean peptide charge, Pz avg (Table 2) for neither RSA nor MCA.…”

Section: Bulk Antioxdiative Propertiescontrasting

confidence: 86%

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

et al. 2020

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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.

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Section: Bulk Antioxdiative Propertiescontrasting

confidence: 86%

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

et al. 2020

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“…Furthermore, the optimum enzyme conditions may also depend on the response values; for example, neutrase has an optimum temperature of 39.55 °C when the hydrolysate has a higher DPPH-scavenging activity, and an optimum temperature of 43.72 °C when the hydrolysate has higher cellular antioxidant activity [ 16 , 17 ]. The hydroxyl-radical-scavenging activity and DH and BCAA contents are related, and hydrolysates with different response values may be applied to different research fields.…”

Section: Resultsmentioning

confidence: 99%

“…The analysis of variance (ANOVA) results for the model are given in Table 3 . The model F-value implies that the models were significant, and Prob > F values of less than 0.0500 indicate that the model terms were significant [ 17 ]. As shown in Table 3 , the p -values for the three models of DH content, hydroxyl-radical-scavenging activity, and BCAA content were all <0.01, which indicated that all the models were significant; the lack of fit values of the three models were 0.6612, 0.4923, and 0.4359, which further indicated that the models were significant.…”

Section: Resultsmentioning

confidence: 99%

“…The final peptide compositions were identified by LC-MS/MS according to the method of Wang et al [ 17 ], with some modifications. The target peptide was further separated on an Acclaim PepMap RSLC column (C18, 5 μm, 100 Å, 300 μm × 5 mm) with a 60 min gradient of 5 min 6–9% Buffer B (80% ACN, 0.1% formic acid), 15 min 9–14% Buffer B, 30 min 14–30% Buffer B, 8 min 30–40% Buffer B, and 2 min 40–95% Buffer B. Peptides were analyzed using a Thermo Scientific Q Exactive mass spectrometer in data-dependent mode, with an automatic switch between MS and MS/MS scans using a top 20 method.…”

Section: Methodsmentioning

confidence: 99%

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Optimization of Oyster (Crassostrea talienwhanensis) Protein Hydrolysates Using Response Surface Methodology

Wang

Xing

et al. 2020

Molecules

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Oyster (Crassostrea talienwhanensis) protein was hydrolyzed by trypsin to produce peptides with different response values, and response surface methodology (RSM) was applied to optimize the hydrolysis conditions. The highest degree of hydrolysis (DH) of the oyster peptide (OP) was obtained at an enzyme concentration of 1593.2 U/g, a pH of 8.2, a hydrolysis temperature of 40.1 °C, a hydrolysis time of 6.0 h, and a water/material ratio of 8.2. The greatest hydroxyl-radical-scavenging activity of OP was obtained at an enzyme concentration of 1546.3 U/g, a pH of 9.0, a hydrolysis temperature of 50.2 °C, a hydrolysis time of 5.1 h, and a water/material ratio of 5.6. The largest branched-chain amino acid (BCAA) content of OP was obtained at an enzyme concentration of 1323.8 U/g, a pH of 8.3, a hydrolysis temperature of 41.7 °C, a hydrolysis time of 6.7 h, and a water/material ratio of 4.8. The three experimental values were significantly in agreement with the predicted values within the 95% confidence interval. Furthermore, ultrafiltration and chromatographic methods were used to purify the OP, and 13 peptides that were rich in Lys, Arg, His, and Thr were identified by LC-MS/MS. The results of this study offer different optimum hydrolysis conditions to produce target peptides from oyster protein by using RSM, and this study provide a theoretical basis for the high-value utilization of oyster protein.

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“…However, the highest DPPH RSA was found for the FPHs obtained by sequential hydrolysis (i.e. highest DH and lowest PCL) for both MCF and HCM compared to other treatments on the same substrate [64]. There does not appear to be any apparent correlation with the mean peptide charge, Pzavg (Table 2) for neither RSA nor MCA.…”

Section: Bulk Antioxdiative Propertiesmentioning

confidence: 88%

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk in vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

Jafarpour¹,

Gregersen²,

Gomes³

et al. 2020

Preprint

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Protein hydrolysates show great promise as bioactive food and feed ingredient and for valorization of side-streams from e.g. the fish processing industry. This study characterizes bulk emulsifying, foaming, and in vitro antioxidative properties of hydrolysates derived from cod frame by application of Alcalase and Neutrase, individually and sequentially as well as the influence of heat-treatment prior to hydrolysis. We present a novel approach that utilizes proteomics data for calculation of weighted mean peptide properties (length, molecular weight, and charge) and peptide-level abundance estimation. Using subsequent bioinformatic prediction of biofunctional properties to describe observed bulk properties, we are able to provide an in-depth hydrolysate characterization not previously seen. 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. Combining peptide abundance with predicted emulsifying activity, we were able to identify several peptides that are likely linked to the observed differences in bulk emulsifying properties. In general, decreased hydrolysis resulted in significantly higher chelating activity, while the opposite was observed for radical scavenging activity. The study highlights the prospects of applying proteomics and bioinformatics for hydrolysate characterization and in food protein science.

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Purification and identification of antioxidative peptides from mackerel (Pneumatophorus japonicus) protein

Abstract: The heptapeptide LDIQKEV (843.5 Da) and the octapeptide TAAIVNTA were identified from mackerel (Pneumatophorus japonicus) protein.

Cited by 11 publications

References 35 publications

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

Optimization of Oyster (Crassostrea talienwhanensis) Protein Hydrolysates Using Response Surface Methodology

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk in vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

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