A novel calcium-chelating peptide purified from Auxis thazard protien hydrolysate and its binding properties with calcium

Chen, Ming; Ji, Hongwu; Zhang, Zewei; Zeng, Xuege; Su, Weiming; Liu, Shucheng

doi:10.1016/j.jff.2019.103447

Cited by 56 publications

(34 citation statements)

References 39 publications

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“…The SEM image for optimized A. lecanora hydrolysates showed a smooth structure with pores ( Figure 6). A similar smooth vesicular pattern was reported from the peptide sequence of Glu-Pro-Ala-His, generated from Auxis thazard hydrolysates [40]. Meanwhile, the porous form indicates that the protein was degraded into smaller peptides.…”

Section: Scanning Electron Microscpysupporting

confidence: 77%

Response Factorial Design Analysis on Papain-Generated Hydrolysates from Actinopyga lecanora for Determination of Antioxidant and Antityrosinase Activities

et al. 2020

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Actinopyga lecanora (A. lecanora) is classified among the edible species of sea cucumber, known to be rich in protein. Its hydrolysates were reported to contain relatively high antioxidant activity. Antioxidants are one of the essential properties in cosmeceutical products especially to alleviate skin aging. In the present study, pH, reaction temperature, reaction time and enzyme/substrate ratio (E/S) have been identified as the parameters in the papain enzymatic hydrolysis of A. lecanora. The degree of hydrolysis (DH) with antioxidant activities of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric-reducing antioxidant power (FRAP) assays were used as the responses in the optimization. Analysis of variance (ANOVA), normal plot of residuals and 3D contour plots were evaluated to study the effects and interactions between parameters. The best conditions selected from the optimization were at pH 5.00, 70 °C of reaction temperature, 9 h of hydrolysis time and 1.00% enzyme/substrate (E/S) ratio, with the hydrolysates having 51.90% of DH, 42.70% of DPPH activity and 109.90 Fe2+μg/mL of FRAP activity. The A. lecanora hydrolysates (ALH) showed a high amount of hydrophobic amino acids (286.40 mg/g sample) that might be responsible for antioxidant and antityrosinase activities. Scanning electron microscopy (SEM) image of ALH shows smooth structures with pores. Antityrosinase activity of ALH exhibited inhibition of 31.50% for L-tyrosine substrate and 25.40% for L-DOPA substrate. This condition suggests that the optimized ALH acquired has the potential to be used as a bioactive ingredient for cosmeceutical applications.

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Section: Scanning Electron Microscpysupporting

confidence: 77%

Response Factorial Design Analysis on Papain-Generated Hydrolysates from Actinopyga lecanora for Determination of Antioxidant and Antityrosinase Activities

et al. 2020

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“…Both are rich in glutamic acid, arginine and histidine. The carboxyl groups (G1u and Asp) of acidic amino acids and the imidazolyl (His) of histidine were identified as major calcium‐binding sites (Chen et al ., 2019; Chen et al ., 2020), and the nutritional value of proteins is mainly determined by their amino acid content. This indicated that GSP and GSPP contain sites that offer ability to chelate with calcium ions, and the resulting chelated compound with calcium ions increased the nutritional value.…”

Section: Resultsmentioning

confidence: 99%

“…Over the last decades, calcium-chelating peptides have been identified in different food sources, including animal sources, aquatic sources and plant sources. Prominent examples are the calcium-binding peptide isolated from Auxis thazard protein hydrolysate (Chen et al, 2019), the calcium-binding peptide from pig bone (Wu et al, 2019), the calcium-peptide complex from Antarctic krill (Hou et al, 2018) and soluble soya bean protein hydrolysate-calcium complexes (Liu et al, 2017a(Liu et al, , 2017b. These studies showed that the calcium-binding activities of calcium-binding peptides, isolated and purified from various sources, significantly exceeded those of the original protein hydrolysate.…”

Section: Introductionmentioning

confidence: 99%

“…At the same time, grape seed protein (GSP) and its hydrolysates are rich in glutamic acid, arginine and histidine (Ding et al ., 2018). Furthermore, the carboxyl groups (G1u and Asp) of acidic amino acids and the imidazolyl (His) of histidine have been identified as major calcium‐binding sites (Chen et al ., 2019). The bioactive peptides of grape seeds also have many unique physiological functions, but few related studies exist.…”

Section: Introductionmentioning

confidence: 99%

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Preparation of grape seed polypeptide and its calcium chelate with determination of calcium bioaccessibility and structural characterisation

Jiang

Zhao

et al. 2020

Int J of Food Sci Tech

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Grape seed polypeptide (GSPP) was obtained by liquid fermentation with Bacillus subtilis TK15.015 from waste grape seed pomace. Its chelation ability with calcium ions was excellent. Simulation of in vitro gastrointestinal digestion showed that GSPP and calcium chelate (GSPP-Ca) slowly released calcium and decreased stomach stimulation. The solubility and transmission rate of GSPP-Ca after digestion in the gastrointestinal tract for 8 h maintained high levels of 74.4% and 46.4%, respectively, which far exceeded the levels achieved by other calcium supplements. Structural characterisation showed that calcium ions mainly react with binding sites present in peptides such as carboxyl oxygen, hydroxyl oxygen, amino nitrogen and amide bonds. GSPP-Ca may be a state in which a calcium-encapsulating complex formed, leaving calcium ions in a soluble state, suggesting its possible use as a high-quality calcium supplement.

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“…For example, sunflower meal is the major byproduct of oil extraction and copper-chelating peptides have been identified from defatted sunflower meal hydrolysates produced with pepsin and pancreatin [ 91 ]. Besides agri-food byproducts, a recent study identified a novel calcium-binding peptide (Glu-Pro-Ala-His) from Auxis thazard protein hydrolysates; this protein material is a type of tuna with low nutritional value [ 62 ]. Nonetheless, further research efforts are still needed to enhance the sustainable production of metal-chelating peptides using alternative protein sources.…”

Section: Sustainable Production Of Mineral-binding Peptidesmentioning

confidence: 99%

Peptide–Mineral Complexes: Understanding Their Chemical Interactions, Bioavailability, and Potential Application in Mitigating Micronutrient Deficiency

Sun

Sarteshnizi

Boachie

et al. 2020

Foods

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Iron, zinc, and calcium are essential micronutrients that play vital biological roles to maintain human health. Thus, their deficiencies are a public health concern worldwide. Mitigation of these deficiencies involves micronutrient fortification of staple foods, a strategy that can alter the physical and sensory properties of foods. Peptide–mineral complexes have been identified as promising alternatives for mineral-fortified functional foods or mineral supplements. This review outlines some of the methods used in the determination of the mineral chelating activities of food protein-derived peptides and the approaches for the preparation, purification and identification of mineral-binding peptides. The structure–activity relationship of mineral-binding peptides and the potential use of peptide–mineral complexes as functional food ingredients to mitigate micronutrient deficiency are discussed in relation to their chemical interactions, solubility, gastrointestinal digestion, absorption, and bioavailability. Finally, insights on the current challenges and future research directions in this area are provided.

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A novel calcium-chelating peptide purified from Auxis thazard protien hydrolysate and its binding properties with calcium

Cited by 56 publications

References 39 publications

Response Factorial Design Analysis on Papain-Generated Hydrolysates from Actinopyga lecanora for Determination of Antioxidant and Antityrosinase Activities

Response Factorial Design Analysis on Papain-Generated Hydrolysates from Actinopyga lecanora for Determination of Antioxidant and Antityrosinase Activities

Preparation of grape seed polypeptide and its calcium chelate with determination of calcium bioaccessibility and structural characterisation

Peptide–Mineral Complexes: Understanding Their Chemical Interactions, Bioavailability, and Potential Application in Mitigating Micronutrient Deficiency

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