Bovine plasma hydrolysates’ iron chelating capacity and its potentiating effect on ferritin synthesis in Caco-2 cells

Gómez-Grimaldos, Nathalia A; Gómez-Sampedro, L.J.; Montoya, José Edgar Zapata; López-García, Gabriel; Cilla, Antonio; Alegría‐Torán, Amparo

doi:10.1039/d0fo02502j

Cited by 17 publications

(10 citation statements)

References 25 publications

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“…The result showed that a decrease in the molecular weight leads to an increase in the AC, and FBPH-3 was the fraction that showed the greatest AC (see Table 2). It is possible that the AC of peptides from BP are more active and stable when they have peptide bonds in their structure, rather than having single amino acid residues or dipeptides (Gómez-Grimaldos et al 2020). These results are consistent with some studies which have obtained low molecular weight peptides with elevated AC (Gómez and Zapata 2016;Wiriyaphan et al 2015).…”

Section: Separation Of Antioxidant Peptides From Bphsupporting

confidence: 90%

“…Likewise, peptides separated by ultrafiltration with considerable AC and with low molecular sizes between 1 and 5 kDa have also been observed in the literature (Wiriyaphan et al 2015). When hydrolyzed, protein origin substances release amino acids, which are known for their ability to donate electrons such as tryptophan (Try), tyrosine (Tyr), and histidine (His), which increase AC when exposed by hydrolysis processes and are contained in BPH in concentrations between 3.3 ± 0.02 to 28.7 ± 0.3 mg/g of protein (Gómez-Grimaldos et al 2020).…”

Section: Separation Of Antioxidant Peptides From Bphmentioning

confidence: 79%

“…Antioxidant capacity of bovine plasma hydrolysates ultrafiltrates with (DH): 19.1 % According to the results, FBPH-3 showed a higher AC than the molecular fractions with a higher weight, which suggests that small peptides are more potent antioxidants than larger peptides. This could be due to the side chains and their amino ends, which are more available to donate electrons or hydrogen atoms and react with free radicals or reduce complexes such as Fe 3+ -TPTZ (Gómez-Grimaldos et al 2020;Phanturat et al 2010).…”

Section: Separation Of Antioxidant Peptides From Bphmentioning

confidence: 99%

“…Proteins from by-products of the food industry have been considered feasible and sustainable sources to this end, due to the lower environmental impact they entail (Samaranayaka and Li-Chan 2011). No previous studies have evaluated the efficacy of antioxidant peptides from by-products of the bovine slaughter industry using cell cultures, which provide biologically more relevant results than chemical tests because they integrate processes such as the uptake, absorption, distribution, and cellular metabolism of the antioxidant compounds (Gómez-Grimaldos et al 2020). However, there are studies on the AC of protein hydrolysates, such as the in vitro evaluation of the protective effects of Nile tilapia scales hydrolysates on DNA damage and reduction in the ROS level on RAW264.7 cells (Ngo et al 2010).…”

Section: Introductionmentioning

confidence: 99%

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Segurança alimentar e nutricional 4

Castro¹

2023

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Os autores desta obra: 1. Atestam não possuir qualquer interesse comercial que constitua um conflito de interesses em relação ao artigo científico publicado; 2.Declaram que participaram ativamente da construção dos respectivos manuscritos, preferencialmente na: a) Concepção do estudo, e/ou aquisição de dados, e/ou análise e interpretação de dados; b) Elaboração do artigo ou revisão com vistas a tornar o material intelectualmente relevante; c) Aprovação final do manuscrito para submissão.; 3. Certificam que os artigos científicos publicados estão completamente isentos de dados e/ou resultados fraudulentos; 4. Confirmam a citação e a referência correta de todos os dados e de interpretações de dados de outras pesquisas; 5.Reconhecem terem informado todas as fontes de financiamento recebidas para a consecução da pesquisa; 6. Autorizam a edição da obra, que incluem os registros de ficha catalográfica, ISBN, DOI e demais indexadores, projeto visual e criação de capa, diagramação de miolo, assim como lançamento e divulgação da mesma conforme critérios da Atena Editora. DECLARAÇÃO DA EDITORA A Atena Editora declara, para os devidos fins de direito, que: 1. A presente publicação constitui apenas transferência temporária dos direitos autorais, direito sobre a publicação, inclusive não constitui responsabilidade solidária na criação dos manuscritos publicados, nos termos previstos na Lei sobre direitos autorais (Lei 9610/98), no art. 184 do Código Penal e no art. 927 do Código Civil; 2. Autoriza e incentiva os autores a assinarem contratos com repositórios institucionais, com fins exclusivos de divulgação da obra, desde que com o devido reconhecimento de autoria e edição e sem qualquer finalidade comercial; 3. Todos os e-book são open access, desta forma não os comercializa em seu site, sites parceiros, plataformas de ecommerce, ou qualquer outro meio virtual ou físico, portanto, está isenta de repasses de direitos autorais aos autores; 4. Todos os membros do conselho editorial são doutores e vinculados a instituições de ensino superior públicas, conforme recomendação da CAPES para obtenção do Qualis livro; 5. Não cede, comercializa ou autoriza a utilização dos nomes e e-mails dos autores, bem como nenhum outro dado dos mesmos, para qualquer finalidade que não o escopo da divulgação desta obra.

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Section: Separation Of Antioxidant Peptides From Bphsupporting

confidence: 90%

Section: Separation Of Antioxidant Peptides From Bphmentioning

confidence: 79%

Section: Separation Of Antioxidant Peptides From Bphmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Segurança alimentar e nutricional 4

Castro¹

2023

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“…The poor absorption efficiency of non-heme iron in vivo is due to its low solubility [36]. The carboxyl, hydroxyl and amino groups of amino acids and peptides increase the solubility of non-heme iron in combination with it [18,37]. For example, a heptapeptide (SVNVPLY) derived from barley spontaneously formed complexes with non-heme iron, and then significantly increased iron absorption in Caco-2 cells compared to ferric sulfate [38].…”

Section: Discussionmentioning

confidence: 99%

The efficiency and safety evaluation of hemoglobin hydrolysate as a non-heme iron fortifier

Xue¹,

Jiang²,

Zhang³

et al. 2024

Food Science and Human Wellness

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Hemoglobin hydrolysate is derived from the enzymatic degradation of hemoglobin. This work aimed to evaluate whether hemoglobin hydrolysate promotes the absorption of non-heme iron and the safety of absorbed iron in mice by analyzing the iron binding content, iron circulation, and liver homeostasis. We found that hemoglobin hydrolysate promoted the absorption of non-heme iron with high efficiency in duodenum by spontaneously binding non-heme iron during digestion, and increased hepatic iron content by up-regulating divalent metal transporter 1 (DMT1), zinc transporter 14 (ZIP14), but hepatic iron content only increased at 3 weeks. Duodenal iron entered the blood through ferroportin without restriction at 3 weeks, and excessive iron entered the liver and then affected the hepatocyte membranes permeability and lipid synthesis through oxidative stress. With the prolongation of dietary intervention, the up-regulated hepcidin acted on the ferroportin to restrict excess iron from entering the blood, and then the hepatic homeostasis recovered. In addition, hemoglobin hydrolysate enhanced the hepatic antioxidant capacity. Taken together, hemoglobin hydrolysate has a strong ability to promote the absorption of non-heme iron in vivo, and the absorbed iron is relatively safe due to the regulation of hepcidin.

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Preparation, characterization, and bioavailability evaluation of antioxidant phosvitin peptide‐ferrous complex

Song,

Zhu,

Qiao

et al. 2023

J Sci Food Agric

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BACKGROUNDIron deficiency anemia (IDA) is one of the commonest global nutritional deficiency diseases, and the low bioavailability of iron is a key contributing factor. The peptide‐iron complex could be used as a novel iron supplement to improve iron bioavailability.RESULTSIn this study, antioxidant low molecular weight (<3 kDa) phosvitin peptide (named PP‐4) was separated to prepare a phosvitin peptide‐ferrous complex (named PP‐4‐Fe); then the structural conformation of PP‐4‐Fe was characterized and its bioavailability by in vitro digestion was evaluated. The results showed that PP‐4 had good ferrous‐binding activity with 96.14 ± 2.86 μg Fe2+ mg−1, and had a strong antioxidant effect with 995.61 ± 79.75 μmol TE mg−1 in 2,2'‐azinobis'3‐ethylbenzothiazoline‐6‐sulfonic acid) (ABTS) and 62.3 ± 3.95 μmol FeSO4 mg−1 in ferric ion reducing antioxidant power (FRAP). After ferrous binding, the FRAP activity of PP‐4‐Fe, enhanced by 1.8 times, formed a more ordered structure with an increase in α‐helix and decrease in γ‐random coil. The ferrous binding sites of PP‐4 involved were the amino, carboxyl, imidazole, and phosphate groups. The PP‐4‐Fe complex displayed excellent gastrointestinal stability and antioxidant effects during digestion. The iron dialysis percentage of PP‐4‐Fe was 74.59% ± 0.68%, and increased to 81.10% ± 0.89% with the addition of 0.25 times vitamin C (VC). This indicated that PP‐4‐Fe displayed excellent bioavailability and VC in sufficient quantities had a synergistic effect on improving bioavailability.CONCLUSIONSThis study demonstrated that antioxidant phosvitin peptide was an efficient delivery system to protect ferrous ions and suggested that the phosvitin peptide‐ferrous complex has strong potential as a ferrous supplement. © 2023 Society of Chemical Industry.

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Bovine plasma hydrolysates’ iron chelating capacity and its potentiating effect on ferritin synthesis in Caco-2 cells

Abstract: Bovine plasma hydrolysates with a degree of hydrolysis of 19.1% have an iron chelating capacity of 38.5 ± 0.4% and increase the synthesis of ferritin in Caco-2 cells five-fold compared to the control.

Cited by 17 publications

References 25 publications

Segurança alimentar e nutricional 4

Segurança alimentar e nutricional 4

The efficiency and safety evaluation of hemoglobin hydrolysate as a non-heme iron fortifier

Preparation, characterization, and bioavailability evaluation of antioxidant phosvitin peptide‐ferrous complex

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