ArticleScientific reports2022
Discovery of calcium-binding peptides derived from defatted lemon basil seeds with enhanced calcium uptake in human intestinal epithelial cells, Caco-2.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 38 citations in OpenAlex.
- From Synthesis Optimization to Chelation Mechanism: A Rice Protein Peptide-Calcium Complex Enhances Intestinal Calcium Absorption and Bone Formation via the TRPV6-Calbindin9k Axis.Foods (Basel, Switzerland) · 2026Article
- AI-assisted screening of soybean varieties: Linking protein composition to tofu quality.Food hydrocolloids · 2026Article
- Skipjack tuna bone derived biocalcium ameliorates C2C12 myotube atrophy through microRNA29b regulation.Scientific reports · 2026Article
- Primary Metabolites in ThreeLife (Basel, Switzerland) · 2026Article
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- Evaluating the capability of soybean peptides as calcium ion carriers: a study through sequence analysis and molecular dynamics simulations.RSC advances · 2024Article
- Article
- Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate.Frontiers in nutrition · 2023Article
- The Formation, Structural Characteristics, Absorption Pathways and Bioavailability of Calcium-Peptide Chelates.Foods (Basel, Switzerland) · 2022Review
- Calcium supplements and structure-activity relationship of peptide-calcium chelates: a review.Food science and biotechnology · 2022Review
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is anticipated that calcium-chelating peptides may serve to enhance the absorption of calcium. This research examined defatted lemon basil seeds (DLBS) which had been treated with Alcalase under optimized parameters for the degree of hydrolysis for proteolysis, discovering that the activity for calcium-binding in a competitive condition with phosphate ion was 60.39 ± 1.545%. The purification of the hydrolysates was performed via ultrafiltration along with reversed-phase high performance liquid chromatography (RP-HPLC). Determination of the purified peptide amino acid sequence was confirmed for both peptides and reported as Ala-Phe-Asn-Arg-Ala-Lys-Ser-Lys-Ala-Leu-Asn-Glu-Asn (AFNRAKSKALNEN; Basil-1), and Tyr-Asp-Ser-Ser-Gly-Gly-Pro-Thr-Pro-Trp-Leu-Ser-Pro-Tyr (YDSSGGPTPWLSPY; Basil-2). The respective activities for calcium-binding were 38.62 ± 1.33%, and 42.19 ± 2.27%. Fluorescence spectroscopy, and fourier transform infrared spectroscopy were employed in order to assess the chelating mechanism between calcium and the peptides. It was found that the calcium ions took place through the activity of the amino nitrogen atoms and the oxygen atoms on the carboxyl group. Moreover, both of these peptides served to improve calcium transport and absorption in Caco-2 cell monolayers, depending on the concentration involved. It was revealed that the peptide-calcium complexes offered an increased calcium absorption percentage when compared to free calcium at similar concentrations. It might be concluded that the peptide within the peptide-calcium complex can promote calcium absorption through both active and passive transport pathways by increasing calcium concentration and promoting cell membrane interaction. Accordingly, DLBS protein can be considered a strong potential source of protein which can be used to produce calcium-binding peptides and might therefore play a role in the production of nutraceutical foods as a bioactive ingredient.
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