RETRACTED: Hemp bioactive peptides: Nutrition, functional properties and action mechanisms to maximize their nutraceutical applications and future prospects

Ashaolu, Tolulope Joshua; Le, Thanh-Do; Suttikhana, Itthanan; Olatunji, Opeyemi Joshua; Farag, Mohamed A.

doi:10.1016/j.foodchem.2023.135691

Cited by 3 publications

(2 citation statements)

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“…Succinylation involves the covalent attachment of succinic acid groups to the protein molecules, inducing structural modifcations that impact the protein's fexibility and overall behavior [97]. Tese alterations subsequently afect the thermal stability and decomposition characteristics of the protein [98]. Moreover, the binding of zinc ions to the chickpea protein further infuences its structural properties and thermal behavior.…”

Section: Diferential Scanning Calorimeter (Dsc)mentioning

confidence: 99%

Enhancing Zinc Uptake through Dual-Modification of Cicer arietinum Protein

Patil,

Bains,

Sridhar

et al. 2023

Journal of Food Biochemistry

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Zinc is crucial for physiological processes; however, deficiency persists globally. Binding zinc to plant proteins enhances absorption, minimizing toxicity risks and offering a potential solution for deficiency. Mineral binding efficiency of the unmodified protein is limited; hence, dual modification (succinylation and ultrasonication) is potentially used to achieve higher binding efficiency. Enhancing zinc uptake is crucial for cellular health due to its vital roles in various biological processes including enzymatic activity, DNA repair, immune function, antioxidant defense, hormone regulation, brain function, signaling, growth, gene expression, and reproduction. Therefore, this research aimed to develop a chickpea protein-zinc complex and to evaluate the influence of dual modification on their physiochemical, bioavailability, and cellular mineral uptake attributes. Succinylation exhibited significant improvements in the water-holding capacity by 28.73%, oil-holding capacity by 34.09%, and solubility by 5.46% of the chickpea protein-zinc complex as compared to the native complex. Mineral bioavailability increased by 8.32%, and there were notable increases in cellular uptake of zinc by 2.10%, retention by 5.80%, and transport by 3.96%, respectively. Furthermore, the dual modification approach resulted in a notable decrease in the particle size of the chickpea protein-zinc complex, with a substantial reduction of 73.25% and an increased zeta potential value of −21 mV compared to the succinylated complex. As well, dual modification concurrently led to a substantial decline of 48.04% in the sulfhydryl (SH) content, coupled with a marked increase of 21.92% in the surface hydrophobicity. In addition, zinc bioavailability, cellular uptake, retention, and transport were further enhanced by 1.89, 3.34, and 4.8% through dual modification. Our findings highlight that the dual modification of the chickpea protein-zinc complex shows a promising strategy for enhancing the techno-functional characteristics, bioavailability, and cellular uptake of zinc, which could be a better platform for developing vegan foods.

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Section: Diferential Scanning Calorimeter (Dsc)mentioning

confidence: 99%

Enhancing Zinc Uptake through Dual-Modification of Cicer arietinum Protein

Patil,

Bains,

Sridhar

et al. 2023

Journal of Food Biochemistry

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“…Although a daily diet is usually rich in iron, the absorption efficiency of iron is usually reduced because iron can easily react with phytic acid and oxalic acid contained in food and form insoluble compounds. The current oral iron supplements were usually made from ferrous salts, such as ferrous sulphate, ferrous gluconate and ferrous lactate, the applications of which were limited by the low bioavailability, gastric mucosal injury and chemical instability (Ashaolu et al ., 2023). Therefore, there is a strong need to develop a new type of iron supplement with higher efficiency and fewer side effects.…”

Section: Introductionmentioning

confidence: 99%

Egg yolk peptide‐iron chelate: preparation, conformational structure, chelating mechanism and stability in vitro

Wei,

Huo,

Lin

et al. 2024

Int J of Food Sci Tech

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SummaryIn this study, a method to produce iron‐chelating peptides derived from egg yolk proteins was developed and optimised. The egg yolk proteins were enzymolysed and ultrafiltered to prepare egg yolk peptide (EYP), and then the EYP was chelated with Fe to produce egg yolk peptide‐Fe (EYP‐Fe). The optimised mass ratio of peptide to iron, pH, temperature and reaction time were found at 8:1, pH 8.0, 40 °C and 30 min, respectively. The mean particle size of EYP‐Fe was 389.2 ± 2.61 nm, and the chelating ratio was 95.38 ± 1.93%. The measurements of FTIR, X‐ray photoelectron spectroscopy (XPS) and NMR showed that ferrous ions mainly combined with the amino and carboxyl of EYP to form EYP‐Fe. In vitro stability studies have shown that the iron release rate of the EYP‐Fe is maintained at around 5% under alkaline conditions, and there is no significant difference in iron release rate under conditions of 30 °C–80 °C; besides, it has a lower iron release rate (18%) in gastrointestinal digestion compared to FeSO4 (97.93%), indicating that the EYP‐Fe has good heat tolerance, alkalinity and digestion tolerance. The above results provide a scientific basis for the use of EYP‐Fe derived from egg yolk protein as a potential alternative to iron supplements.

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