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Peer-reviewedCC BYFoods (Basel, Switzerland)

Moringa oleifera Lam. Leaf Peptide-Calcium Chelates: Structural Characterization, Stability and Calcium Absorption-Promoting Transport Capability.

  • Ruijing Gu1
  • Xinyu Wang1
  • Zilin Wang1
  • Yu Zhou1
  • Jiahe Dai1,2,3
  • Lei Peng1,2,3
  • Yang Tian2,3
  • Liang Tao1,2,3
  1. 1College of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
  2. 2Engineering Research Center of Development and Utilization of Food and Drug Homologous Resources, Ministry of Education, Yunnan Agricultural University, Kunming 650201, China.
  3. 3Yunnan Key Laboratory of Precision Nutrition and Personalized Food Manufacturing, Yunnan Agricultural University, Kunming 650201, China.
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Abstract

A novel calcium-chelating peptide, KTFQGPPHG, was identified and screened from Moringa oleifera Lam. leaf protein hydrolysate, and further used to prepare a highly stable peptide-calcium chelate (KTFQGPPHG-Ca). The structure of KTFQGPPHG-Ca was characterized, while assessing its chelation stability and calcium transport potential. It was found that the calcium binding capacity of KTFQGPPHG reached 62.401 µg/mg. After chelation with calcium, KTFQGPPHG transitioned from an amorphous structure to a stable crystalline form. Carboxyl oxygen atoms and amino nitrogen atoms on KTFQGPPHG served as binding sites for Ca²⁺. The KTFQGPPHG-Ca demonstrates excellent phosphate stability and thermal stability. In addition, the calcium transport amount of KTFQGPPHG at 30 min and 60 min was significantly higher than that of the CaCl₂ group (p < 0.05). Particularly, the calcium transport capacity at 30 min was 1.40-fold that of the CaCl₂ group. KTFQGPPHG effectively counteracted the suppressive impact of dietary factors on Ca²⁺ absorption, and likely promoted Ca²⁺ translocation via the TRPV6 calcium channel pathway. The present results offer a theoretical basis for KTFQGPPHG-Ca to serve as a promising calcium source to improve intestinal calcium absorption.

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Cite

BibTeXRIS
BibTeX
@article{gu2026moringa,
  title = {{Moringa oleifera Lam. Leaf Peptide-Calcium Chelates: Structural Characterization, Stability and Calcium Absorption-Promoting Transport Capability.}},
  author = {Ruijing Gu and Xinyu Wang and Zilin Wang and Yu Zhou and Jiahe Dai and Lei Peng and Yang Tian and Liang Tao},
  journal = {Foods (Basel, Switzerland)},
  year = {2026},
  month = sep,
  doi = {10.3390/foods15193496},
  url = {https://europepmc.org/article/MED/42883604},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Moringa oleifera Lam. Leaf Peptide-Calcium Chelates: Structural Characterization, Stability and Calcium Absorption-Promoting Transport Capability.
AU  - Ruijing Gu
AU  - Xinyu Wang
AU  - Zilin Wang
AU  - Yu Zhou
AU  - Jiahe Dai
AU  - Lei Peng
AU  - Yang Tian
AU  - Liang Tao
PY  - 2026
DA  - 2026/09/29
JO  - Foods (Basel, Switzerland)
DO  - 10.3390/foods15193496
UR  - https://europepmc.org/article/MED/42883604
AB  - A novel calcium-chelating peptide, KTFQGPPHG, was identified and screened from Moringa oleifera Lam. leaf protein hydrolysate, and further used to prepare a highly stable peptide-calcium chelate (KTFQGPPHG-Ca). The structure of KTFQGPPHG-Ca was characterized, while assessing its chelation stability and calcium transport potential. It was found that the calcium binding capacity of KTFQGPPHG reached 62.401 µg/mg. After chelation with calcium, KTFQGPPHG transitioned from an amorphous structure to a stable crystalline form. Carboxyl oxygen atoms and amino nitrogen atoms on KTFQGPPHG served as binding sites for Ca²⁺. The KTFQGPPHG-Ca demonstrates excellent phosphate stability and thermal stability. In addition, the calcium transport amount of KTFQGPPHG at 30 min and 60 min was significantly higher than that of the CaCl₂ group (p < 0.05). Particularly, the calcium transport capacity at 30 min was 1.40-fold that of the CaCl₂ group. KTFQGPPHG effectively counteracted the suppressive impact of dietary factors on Ca²⁺ absorption, and likely promoted Ca²⁺ translocation via the TRPV6 calcium channel pathway. The present results offer a theoretical basis for KTFQGPPHG-Ca to serve as a promising calcium source to improve intestinal calcium absorption.
SN  - 2304-8158
ER  -