Background: Porcine nasal cartilage type II collagen-derived peptides (PNCPs) may be complexed with calcium to provide a highly bioavailable, low-cost, and effective calcium food supplement. However, the calcium-binding characteristics of PNCPs have not yet been investigated. In the present study, calcium-binding peptides were derived from porcine nasal cartilage type II collagen and the resulting PNCPs-Ca complex was characterized.
Results: The study reveals that the calcium-binding capacity of PNCPs is closely related to enzymatic hydrolysis conditions. The highest calcium-binding capacity of PNCPs was observed at a hydrolysis time of 4 h, temperature of 40 °C, enzyme dosage of 1%, and solid-to-liquid ratio of 1:10. Scanning electron microscopy and energy dispersive X-ray spectroscopy revealed that the PNCPs had a pronounced capacity for calcium binding, with the PNCPs-Ca complex exhibiting a clustered structure consisting of aggregated spherical particles. Fourier-transform infrared spectroscopy, fluorescence spectroscopy, X-ray diffraction, dynamic light scattering, amino acid composition, and molecular weight distribution analyses all indicated that the PNCPs and calcium complexed via the carboxyl oxygen and amino nitrogen atoms, leading to the formation of a β-sheet structure during the chelation process. In addition, the stability of the PNCPs-Ca complex was maintained over a range of pH values consistent with those found in the human gastrointestinal tract, facilitating calcium absorption.
Conclusion: These research findings suggest the feasibility of converting by-products from livestock processing into calcium-binding peptides, providing a scientific basis for the development of novel calcium supplements and the potential reduction of resource waste. © 2023 Society of Chemical Industry.
Keywords: calcium-binding peptides; porcine nasal cartilage; stability analysis; structural characterization; type II collagen.
© 2023 Society of Chemical Industry.