Preparation of cattle bone collagen peptides-calcium chelate and its structural characterization and stability

Zhang, Hongru; Zhao, Laiyu; Shen, Qingshan; Qi, Liwei; Jiang, Shan; Guo, Yujie; Zhang, Chunhui; Richel, Aurore

doi:10.1016/j.lwt.2021.111264

Cited by 57 publications

(59 citation statements)

References 28 publications

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“…The amide I band of CPPs was detected around wave number 1,654.84 cm −1 , while the amide I band of CPP-Ca appeared at 1,655.86 cm −1 , suggesting the formation of peptide–calcium chelate was associated with C = O, and the complex have an α-helix structure. The vibration spectral region at 1,430–1,370 cm −1 is mainly caused by the stretching vibration of -COO- ( 39 ). After the interaction with calcium ions, the FTIR spectra shifted from 1,399.64 cm −1 to 1,413.93 cm −1 , which may be due to the interaction between the positive divalent calcium ions and -COO- to form -COO- Ca.…”

Section: Resultsmentioning

confidence: 99%

Preparation, characterization, and osteogenic activity mechanism of casein phosphopeptide-calcium chelate

et al. 2022

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Casein phosphopeptides (CPPs) are good at calcium-binding and intestinal calcium absorption, but there are few studies on the osteogenic activity of CPPs. In this study, the preparation of casein phosphopeptide calcium chelate (CPP-Ca) was optimized on the basis of previous studies, and its peptide-calcium chelating activity was characterized. Subsequently, the effects of CPP-Ca on the proliferation, differentiation, and mineralization of MC3T3-E1 cells were studied, and the differentiation mechanism of CPP-Ca on MC3T3-E1 cells was further elucidated by RNA sequencing (RNA-seq). The results showed that the calcium chelation rate of CPPs was 23.37%, and the calcium content of CPP-Ca reached 2.64 × 105 mg/kg. The test results of Ultraviolet–Visible absorption spectroscopy (UV) and Fourier transform infrared spectroscopy (FTIR) indicated that carboxyl oxygen and amino nitrogen atoms of CPPs might be chelated with calcium during the chelation. Compared with the control group, the proliferation of MC3T3-E1 cells treated with 250 μg/mL of CPP-Ca increased by 21.65%, 26.43%, and 28.43% at 24, 48, and 72 h, respectively, and the alkaline phosphatase (ALP) activity and mineralized calcium nodules of MC3T3-E1 cells were notably increased by 55% and 72%. RNA-seq results showed that 321 differentially expressed genes (DEGs) were found in MC3T3-E1 cells treated with CPP-Ca, including 121 upregulated and 200 downregulated genes. Gene ontology (GO) revealed that the DEGs mainly played important roles in the regulation of cellular components. The enrichment of the Kyoto Encyclopedia of Genes and Genomes Database (KEGG) pathway indicated that the AMPK, PI3K-Akt, MAPK, and Wnt signaling pathways were involved in the differentiation of MC3T3-E1 cells. The results of a quantitative real-time PCR (qRT-PCR) showed that compared with the blank control group, the mRNA expressions of Apolipoprotein D (APOD), Osteoglycin (OGN), and Insulin-like growth factor (IGF1) were significantly increased by 2.6, 2.0 and 3.0 times, respectively, while the mRNA levels of NOTUM, WIF1, and LRP4 notably decreased to 2.3, 2.1, and 4.2 times, respectively, which were consistent both in GO functional and KEGG enrichment pathway analysis. This study provided a theoretical basis for CPP-Ca as a nutritional additive in the treatment and prevention of osteoporosis.

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Section: Resultsmentioning

confidence: 99%

Preparation, characterization, and osteogenic activity mechanism of casein phosphopeptide-calcium chelate

et al. 2022

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“…The molecular weight of the CP sample was analyzed using an HPLC apparatus (Agilent 1260, Agilent Technologies, Walnut Creek, CA, USA) equipped with DAWN HELEOS-II (Wyatt Technology Corporation, America) and Optilabr EX (Wyatt Technology Corporation, USA) detectors coupled with a TSK gel G4000PWxl column (7.8 × 300 mm, TOSOH, Tokyo, Japan), following the previous study ( 25 ). The mobile phase included 0.1% trifluoroacetic acid, 45% acetonitrile, and 54.9% ultrapure water (ultrapure water machine, Milli-Q Synthesis, Millipore Corporation, USA).…”

Section: Methodsmentioning

confidence: 99%

Comparative Analysis of the Bioactive Compounds in Chicken Cartilage: Protective Effects of Chondroitin Sulfate and Type II Collagen Peptides Against Osteoarthritis Involve Gut Microbiota

Zhang

Shen

et al. 2022

Front. Nutr.

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This study was designed to explore osteoarthritis (OA) treatment from bioactive compounds of chicken cartilage food supplements. The OA rat model induced by sodium iodoacetate was used to evaluate the treatment effect in vivo. In this study, we used animal experiments to show that oral chondroitin sulfate (CS), cartilage powder, and type II collagen peptides could increase the athletic ability of rats and reduce inflammatory cytokine levels in serum or synovial fluid, including prostaglandin E2, tumor necrosis factor-α, interleukin (IL) 1β, IL-6, and IL-17. CS displayed the best treatment effect against OA. The morphological structure of articular cartilage indicated that CS could significantly improve cartilage tissue morphology and reduce OA score. Oral CS slowed down the development of OA by modulating gut microbiota. These results provided a useful scientific basis for the high-value utilization of chicken cartilage.

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“…The peptide calcium was separated from the supernatant by absolute ethanol [ 32 ]. The supernatant with the same volume (V Ca ) was added to a centrifuge tube, mixed with absolute ethanol (1:5, v / v ), and then blended thoroughly with a vortex oscillator (MS3, IKA, Staufen, Germany) at 600 rpm for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Conformational Changes in Proteins Caused by High-Pressure Homogenization Promote Nanoparticle Formation in Natural Bone Aqueous Suspension

et al. 2022

Foods

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As a natural calcium resource, animal bone needs to be miniaturized to the nanoscale to improve palatability and absorption capacity. To explore the mechanism of high-pressure homogenization (HPH) in preparing natural bone aqueous nanosuspensions, the relationships between the changes in protein conformation, solubility and quality characteristics of rabbit bone aqueous suspensions (RBAS) prepared by different HPH cycles were studied. The results showed that the improvements in particle size, stability and calcium solubility of RBASs could be mainly attributed to the improvement of protein solubility induced by the changes in protein conformation. HPH treatment led to the denaturation and degradation of protein in rabbit bone, generating soluble peptides and improving the stability of the suspensions by enhancing the surface charge of the particles. When collagen as the main protein was partially degraded, the hydroxyapatite in the bone was crushed into tiny particles. The increase in the particle-specific surface area led to the release of calcium ions, which chelated with the peptides to produce peptide calcium. However, excessive HPH treatment caused the production of protein macromolecular aggregates and affected the quality of RBASs. This study is helpful to promote the application of HPH technology in animal bone nanoprocessing.

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Preparation of cattle bone collagen peptides-calcium chelate and its structural characterization and stability

Cited by 57 publications

References 28 publications

Preparation, characterization, and osteogenic activity mechanism of casein phosphopeptide-calcium chelate

Preparation, characterization, and osteogenic activity mechanism of casein phosphopeptide-calcium chelate

Comparative Analysis of the Bioactive Compounds in Chicken Cartilage: Protective Effects of Chondroitin Sulfate and Type II Collagen Peptides Against Osteoarthritis Involve Gut Microbiota

Conformational Changes in Proteins Caused by High-Pressure Homogenization Promote Nanoparticle Formation in Natural Bone Aqueous Suspension

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