Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Zhang, Wenting; Sun, Jiayue; Huang, Guangrong

doi:10.3923/ajft.2015.158.166

Cited by 3 publications

(3 citation statements)

References 27 publications

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“…Small peptides from tilapia ( Oreochromis niloticus ) skin collagen also increased zinc-chelating ability and zinc bioaccessibility [ 32 ]. Similarly, the iron-binding capacity of protein hydrolysates from mackerel ( Trachurus japonicas) processing side streams was not significantly affected during in vitro gastrointestinal digestion [ 33 ]. Based on the high bioaccessibility obtained in this study, HSH, HMH, and HSB are interesting candidates for Fe, Se, and Zn food fortification since there is a deficit of Fe (60%), Se (30%), and Zn (15%) in the world population, including in both industrial and developing countries [ 11 ].…”

Section: Resultsmentioning

confidence: 99%

Mineral Bioaccessibility and Antioxidant Capacity of Protein Hydrolysates from Salmon (Salmo salar) and Mackerel (Scomber scombrus) Backbones and Heads

et al. 2023

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Information on the bioaccessibility of minerals is essential to consider a food ingredient as a potential mineral fortifier. In this study, the mineral bioaccessibility of protein hydrolysates from salmon (Salmo salar) and mackerel (Scomber scombrus) backbones and heads was evaluated. For this purpose, the hydrolysates were submitted to simulated gastrointestinal digestion (INFOGEST method), and the mineral content was analyzed before and after the digestive process. Ca, Mg, P, Fe, Zn, and Se were then determined using an inductively coupled plasma spectrometer mass detector (ICP-MS). The highest bioaccessibility of minerals was found in salmon and mackerel head hydrolysates for Fe (≥100%), followed by Se in salmon backbone hydrolysates (95%). The antioxidant capacity of all protein hydrolysate samples, which was measured by Trolox Equivalent Antioxidant Capacity (TEAC), increased (10–46%) after in vitro digestion. The heavy metals As, Hg, Cd, and Pb were determined (ICP-MS) in the raw hydrolysates to confirm the harmlessness of these products. Except for Cd in mackerel hydrolysates, all toxic elements were below the legislation levels for fish commodities. These results suggest the possibility of using protein hydrolysates from salmon and mackerel backbones and heads for food mineral fortification, as well as the need to verify their safety.

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Section: Resultsmentioning

confidence: 99%

Mineral Bioaccessibility and Antioxidant Capacity of Protein Hydrolysates from Salmon (Salmo salar) and Mackerel (Scomber scombrus) Backbones and Heads

et al. 2023

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“…Other bio-functional peptides or hydrolysates also showed similar gastrointestinal stability. The horse mackerel protein hydrolysate was stable for 5 h in a simulated two-stage gastrointestinal digestion [29]. The peptide distribution pattern of the hydrolysate was not affected by this digestion.…”

Section: Tph-calcium Binding Activity Maintained In the Simulated Human Digestion Systemmentioning

confidence: 95%

Tilapia Protein Hydrolysate Enhances Transepithelial Calcium Transport in Caco2 cells

Buaduang

Chansuwan

Towatana

et al. 2019

FFHD

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Background: Potent calcium uptake is essential for calcium balance and normal health. Prolonged low intake of calcium is associated with osteoporosis, dental changes, cataracts, and alterations in the brain. However, calcium is difficult to be directly absorbed from the food due to the insoluble calcium salt precipitation that occurs in the intestinal environment. Methods: Tilapia protein hydrolysate (TPH) was prepared by alcalase digestion. The Calcium-binding activity was measured using calcium colorimetric assay, the absorption at 612 nm. The interaction between TPH and calcium was examined by spectroscopic analysis, ultraviolet absorption and fluorescence measurement. TPH-calcium-binding stability in the human digestion system was evaluated by in vitro pepsin-pancreatin hydrolysis simulating human gastric and intestinal digestion. The effects of food components on TPH-calcium-binding activity was also analyzed. The enhancement of transepithelial calcium transport by TPH was determined by in vitro Caco2 epithelial cell-like monolayer. Results: TPH produced from Nile tilapia (Oreochromis niloticus) exhibited calcium-binding activity. It was the peptides in the hydrolysate that contributed to calcium-binding since the spectroscopic changes induced by calcium were characteristic of peptide bonds and tryptophan residues. The calcium binding of TPH was compatible with food matrices. Most food components including saccharides, amino acids and vitamins showed positive or no effects on calcium-binding. The calcium-binding of TPH was also stable in the simulated gastrointestinal digestion system. Pepsin and pancreatin did not considerably change the calcium-binding activity of TPH. Of note, TPH reduced precipitation of calcium by oxalate and phytate, the two most anti-nutritional factors present in green leafy vegetables. Finally, we showed that TPH significantly promoted transepithelial calcium transport in the Caco-2 cell permeability model. Conclusions: Tilapia protein hydrolysate produced by alcalase digestion possessed calcium-binding activity and prevent precipitation of calcium by a mineral chelating agent as well as enhanced transepithelial calcium transport in Caco2 cell. The result implicated the potential of TPH as a functional food ingredient for promoting calcium absorption. Keywords: Tilapia protein hydrolysate; Calcium binding peptides; Calcium absorption

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“…Various edible protein hydrolysates had high Iron-Binding Capacity (IBC) or iron bioavailability, such as spirulina protein (Kim et al, 2014), mackerel processing byproducts (Zhang et al, 2015), shrimp processing byproducts (Huang et al, 2012), anchovy muscle (Wu et al, 2012), lactoglobumin (Wang et al, 2014a), soybean (Zhang et al, 2014), fish collagen (Huang et al, 2015) and chickpea protein (Torres-Fuentes et al, 2012). However, there was no literature about enzymatic hydrolysate with ironbinding capacity from scad processing byproduct.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Hydrolysis Conditions for the Production of Iron-Binding Peptides from Scad (<i>Decapterus maruadsi</i>) Processing Byproducts

Zhang¹,

Li²,

Zhang³

et al. 2016

American Journal of Biochemistry and Biotechnology

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The scad (Decapterus maruadsi) processing byproduct (SPB) was hydrolyzed by four commercial enzymes, namely, trypsin, flavourzyme, protamex and alcalase, for preparing high Iron-Binding Capacity (IBC) hydrolysate. Alcalase was the best choice for obtaining high IBC hydrolysate from SPB. Response surface methodology using a central-composite design was employed to optimize the enzymatic hydrolysis conditions with alcalase to obtain a maximum hydrolysate yield from the SPB with high iron-binding capacity. The best alcalase hydrolysis conditions were as following: Hydrolysis temperature of 46°C, enzyme substrate ratio of 6040 U/g-protein and hydrolysis time of 66 min, respectively. Under these optimal hydrolysis conditions, the predicted ironbinding capacity was 317.2 µg g −1 , which was consistent with the average of three replicates of 296.2 µg g −1 obtained in the validation experiments. The IBC of hydrolysate did not displayed linear relationship with antioxidative ability or the Degree of Hydrolysis (DH). Results indicated that the alcalase hydrolysate from scad processing byproduct can be developed into iron supplant ingredients in functional foods.

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Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Cited by 3 publications

References 27 publications

Mineral Bioaccessibility and Antioxidant Capacity of Protein Hydrolysates from Salmon (Salmo salar) and Mackerel (Scomber scombrus) Backbones and Heads

Mineral Bioaccessibility and Antioxidant Capacity of Protein Hydrolysates from Salmon (Salmo salar) and Mackerel (Scomber scombrus) Backbones and Heads

Tilapia Protein Hydrolysate Enhances Transepithelial Calcium Transport in Caco2 cells

Optimization of Hydrolysis Conditions for the Production of Iron-Binding Peptides from Scad (<i>Decapterus maruadsi</i>) Processing Byproducts

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