Bioactive Peptides Isolated from Casein Phosphopeptides Enhance Calcium and Magnesium Uptake in Caco-2 Cell Monolayers

Cao, Yong; Miao, Jianyin; Guo, Liangqia; Luo, Zhen; Zhang, Xia; Liu, Fei; Yao, Mingfei; Cao, Xiaoqiong; Sun, Shengwei; Lin, Yanyin; Lan, Yaqi; Xiao, Hang

doi:10.1021/acs.jafc.6b05711

Cited by 51 publications

(30 citation statements)

References 46 publications

(106 reference statements)

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“…The CPP1 and CPP2 high-performance liquid chromatography (HPLC) analyses of samples were performed using a Shimadzu LC-15C system with a reversed phase HPLC column [Diamond C18 (2), 5 µm, 4.6 mm, Dikma, China]. The elution condition was chosen based on a previously published method with minor changes (18). Briefly, solution A was 0.1% trifluoroacetic acid in deionized water, and solution B was 0.1% trifluoroacetic acid in acetonitrile.…”

Section: High-performance Liquid Chromatography Analysismentioning

confidence: 99%

“…The calcium binding capacity was defined as the calcium amount (mg) bound to CPP (g) after chelation. This capacity was measured according to the previously published procedure with minor modifications (13,18). Briefly, samples of CPP were made by dissolving it in 0.02 M of sodium phosphate buffer (pH 7.8) and were subsequently mixed with 5 mM of CaCl 2 .…”

Section: Calcium Binding Capacity In Pbs Buffermentioning

confidence: 99%

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Promoting the Calcium-Uptake Bioactivity of Casein Phosphopeptides in vitro and in vivo

et al. 2021

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Casein phosphopeptides have been studied widely for their ability to chelate calcium. However, systematic studies on the effects of casein phosphopeptides (CPP) on calcium absorption in vitro and in vivo are scarce. The purities of two commercially available products, CPP1 and CPP2, are 18.37 and 25.12%, respectively. Here, the in vitro calcium binding capacity of CPP2 was 142.56 ± 7.39 mg/g, which was higher than that of CPP1 (107.15 ± 6.27 mg/g). The calcium transport results in a Caco-2 monolayer model indicated that, relative to controls, CPP1 and CPP2 increased calcium transport by 21.78 and 53.68%, respectively. Subsequent animal experiments showed that the CPP2-Ca-H group (1% Ca, 0.4% CPP2) had significant increases in the femur index, serum Ca2+ and serum osteocalcin levels, and femoral Ca content. The CPP2-Ca-H animal also had decreased serum alkaline phosphatase levels, parathyroid hormone content, and urinary pyridinoline content. Overall, our results demonstrated that CPP2 had stronger effects on promoting calcium uptake than CPP1.

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Section: High-performance Liquid Chromatography Analysismentioning

confidence: 99%

Section: Calcium Binding Capacity In Pbs Buffermentioning

confidence: 99%

Promoting the Calcium-Uptake Bioactivity of Casein Phosphopeptides in vitro and in vivo

et al. 2021

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“…They also increased zinc uptake similarly to the increase observed in the presence of zinc sulfate alone, suggesting that, for this ion, the peptide did not exert a specific function. A recent study showed that five CPPs named P1-P5, characterized by means of LC-MS/MS, were able to promote Mg 2þ absorption over Ca 2þ in Caco-2 cells growing in a medium enriched with both cations (Cao et al 2017). The fragmentation of aand b-CN generated several antimicrobial peptides.…”

Section: Caseins Deriving Cryptidesmentioning

confidence: 99%

Cryptides: latent peptides everywhere

Iavarone

Desiderio

Vitali

et al. 2018

Critical Reviews in Biochemistry and Molecular Biology

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Proteomic surveys with top-down platforms are today revealing thousands of naturally occurring fragments of bigger proteins. Some of them have not functional meaning because they derive from pathways responsible for protein degradation, but many have specific functions, often completely different from that one of the parent proteins. These peptides encrypted in the protein sequence are nowadays called cryptides. They are frequent in the animal and plant kingdoms and represent a new interesting -omic field of investigation. To point out how much widespread is their presence, we describe here the most studied cryptides from very common sources such as serum albumin, immunoglobulins, hemoglobin, and from saliva and milk proteins. Given its vastness, it is unfeasible to cover the topic exhaustively, therefore only several selected examples of cryptides from other sources are thereafter reported. Demanding is the development of new -omic platforms for the functional screening of new cryptides, which could provide suggestion for peptides and peptido-mimetics with variegate fields of application.

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“…The studies showed that protein hydrolysate from several food sources contain calcium-binding peptides. These peptides are bioactive able to promote calcium uptake via epithelium absorption, such as casein phosphopeptides (CPPs) [8,5,9], chicken eggshell matrix proteins [10], and tilapia scale protein hydrolysate [6].…”

Section: Introductionmentioning

confidence: 99%

Tilapia Protein Hydrolysate Enhances Transepithelial Calcium Transport in Caco2 cells

Buaduang

Chansuwan

Towatana

et al. 2019

FFHD

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Background: Potent calcium uptake is essential for calcium balance and normal health. Prolonged low intake of calcium is associated with osteoporosis, dental changes, cataracts, and alterations in the brain. However, calcium is difficult to be directly absorbed from the food due to the insoluble calcium salt precipitation that occurs in the intestinal environment. Methods: Tilapia protein hydrolysate (TPH) was prepared by alcalase digestion. The Calcium-binding activity was measured using calcium colorimetric assay, the absorption at 612 nm. The interaction between TPH and calcium was examined by spectroscopic analysis, ultraviolet absorption and fluorescence measurement. TPH-calcium-binding stability in the human digestion system was evaluated by in vitro pepsin-pancreatin hydrolysis simulating human gastric and intestinal digestion. The effects of food components on TPH-calcium-binding activity was also analyzed. The enhancement of transepithelial calcium transport by TPH was determined by in vitro Caco2 epithelial cell-like monolayer. Results: TPH produced from Nile tilapia (Oreochromis niloticus) exhibited calcium-binding activity. It was the peptides in the hydrolysate that contributed to calcium-binding since the spectroscopic changes induced by calcium were characteristic of peptide bonds and tryptophan residues. The calcium binding of TPH was compatible with food matrices. Most food components including saccharides, amino acids and vitamins showed positive or no effects on calcium-binding. The calcium-binding of TPH was also stable in the simulated gastrointestinal digestion system. Pepsin and pancreatin did not considerably change the calcium-binding activity of TPH. Of note, TPH reduced precipitation of calcium by oxalate and phytate, the two most anti-nutritional factors present in green leafy vegetables. Finally, we showed that TPH significantly promoted transepithelial calcium transport in the Caco-2 cell permeability model. Conclusions: Tilapia protein hydrolysate produced by alcalase digestion possessed calcium-binding activity and prevent precipitation of calcium by a mineral chelating agent as well as enhanced transepithelial calcium transport in Caco2 cell. The result implicated the potential of TPH as a functional food ingredient for promoting calcium absorption. Keywords: Tilapia protein hydrolysate; Calcium binding peptides; Calcium absorption

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Bioactive Peptides Isolated from Casein Phosphopeptides Enhance Calcium and Magnesium Uptake in Caco-2 Cell Monolayers

Cited by 51 publications

References 46 publications

Promoting the Calcium-Uptake Bioactivity of Casein Phosphopeptides in vitro and in vivo

Promoting the Calcium-Uptake Bioactivity of Casein Phosphopeptides in vitro and in vivo

Cryptides: latent peptides everywhere

Tilapia Protein Hydrolysate Enhances Transepithelial Calcium Transport in Caco2 cells

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