Potential Uses of Caseinophosphopeptides
Abstract
Caseinophosphopeptides (CPPs) are phosphorylated casein-derived peptides which possess the ability to bind and solubilise minerals, such as Ca2+. Consumption of high concentrations of Ca2+ in early life contributes to the development of maximal bone density, which in turn can prevent osteoporosis in later life. Furthermore, a recent report has shown a positive correlation between Ca2+ intake and the prevention of hypertension. The high bioavailability of Ca2+ from milk and dairy products has, in part, been attributed to the production of CPPs which have different levels of phosphorylation and are produced in vivo following digestion of and β-casein by the action of gastrointestinal proteinases. CPPs which appear to be resistant to extensive proteolytic degradation, accumulate in the distal small intestine where they are purported to play a role in enhancing the passive absorption of Ca2+ and other trace elements. CPPs have also been produced in vitro using a range of commercially available proteinases of pancreatic origin. Several CPP enrichment procedures from casein hydrolysates have been reported, generally involving Ca2+ induced aggregation followed by ultrafiltration. These CPP enriched preparations have been used to characterise their interaction with Ca2+ and trace elements and to determine their effect on the bioavailability of dietary Ca2+ during animal and human feeding trials. There are conflicting reports, arising from the results of animal feeding studies, on the effectiveness of CPPs in enhancing Ca2+ bioavailability. However, a recent human feeding trial reported improved Ca2+ and Zn2+ absorption following CPP incorporation into a rice-based infant food. In vitro produced CPPs may also find application in the prevention and treatment of dental calculus. This review summarises the production, characterisation and potential applications of CPPs.
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Effects of casein phosphopeptides on thermal stability and sensory quality of whey protein emulsions containing calcium beta-hydroxy-beta-methylbutyrate
2023, International Journal of Biological MacromoleculesThis study aimed to elucidate the effect of casein phosphopeptides (CPP) on the thermal stability and sensory quality of whey protein emulsions containing calcium beta-hydroxy-beta-methylbutyrate (WPEs-HMB-Ca). The interaction mechanism among CPP, HMBCa, and WP in the emulsions before and after autoclaving (121 °C, 15 min) was systematically investigated from macroscopic external and microscopic molecular perspectives. It was found that WPEs-HMB-Ca treated by autoclaving resulted in an increase in droplet size (d4,3 = 24.09 μm) due to aggregation/flocculation of proteins, along with a stronger odor with higher viscosity, compared to those without autoclaving. When CPP:HMB-Ca = 1:25 (w/w) in the emulsion, the droplets exhibited a more uniform and consistent state in the emulsion. In addition, CPP was able to inhibit the formation of complex spatial network structures of proteins during autoclaving by binding with Ca2+, thus improving the thermal stability and storage stability of WPEs-HMB-Ca. This work might provide theoretical guidance for developing functional milk drinks with good thermal stability and flavor.
Casein calcium-binding peptides: Preparation, characterization, and promotion of calcium uptake in Caco-2 cell monolayers
2023, Process BiochemistryIn this study, casein calcium-binding peptides were isolated from casein hydrolysate using calcium-peptide binding properties and their banding properties were characterized. Subsequently, the promoted calcium absorption abilities of casein calcium-binding peptides in the Caco-2 cells monolayers were investigated. Amino acid composition analysis showed that casein calcium-binding peptide-calcium chelate are rich in Glu, Ser, and Asp, with a significant increase in proportion compared to the casein hydrolysate. Molecular weight analysis showed that approximately 90 % of the casein calcium-binding peptides are oligopeptides. Thirty-seven peptide sequences were identified by mass spectrometry, and the presence, quantity, and position of some specific amino acid residues were found to correlate with calcium-binding ability. Additionally, calcium-peptide binding properties were characterized by using Ultraviolet-Visible spectroscopy, Fourier transform infrared spectroscopy, and scanning electron microscopy, which indicated that calcium ions were mainly chelated with the amino nitrogen atoms and oxygen atoms on the carboxyl group of casein calcium-binding peptides, thus forming chelate with porous microstructures. Compared with the control group, the casein calcium-binding peptides treatment group showed a significant increase in calcium transport at 30, 60, 120 and 180 min, respectively, by 44.25 %, 31.21 %, 20.67 % and 24.08 %. Therefore, casein calcium-binding peptides are expected to be used as dietary calcium supplements.
Identification, production and bioactivity of casein phosphopeptides – A review
2022, Food Research InternationalMilk and dairy products are significant sources of proteins and peptides impacting human health. In this way, the interest in CPPs, bioactive phosphorylated peptides resulting from the hydrolysis of caseins, has grown in the past years. CPPs were mainly studied for their capacity to chelate and increase the bioavailability of essential minerals involved in multiple physiological processes. Moreover, CPPs harbour interesting antioxidant and anti-inflammatory properties. Recent in vivo and in vitro studies demonstrated that these different roles are strongly linked to the intrinsic properties of CPPs and CPP concentrate preparations.
This review first comments on the different methods of CPP analytical characterization, focusing on recent techniques. Then, the CPP release occurring during the gastrointestinal digestion was reviewed, followed by the different CPP obtention processes and their impact on their physicochemical characteristics. Finally, the different bioactive roles attributed to CPPs, including mineral chelating properties, are discussed.
We show that CPPs have a promising role in treating various pathologies, notably to compensate for deficiencies in certain nutrients and an anti-oxidant and anti-inflammatory role. Nevertheless, the mechanisms by which CPPs exert their role remain to be elucidated, and this requires precise characterization of CPPs.
This work highlights the key parameters to be considered to study and produce CPPs and the different ways to be investigated in the future to elucidate their roles in vivo and characterize their potential for human health.
Peptidomics in Food
2020, Comprehensive FoodomicsPeptides are important food components with bioactive properties (including, e.g., antimicrobial, antioxidative, ACE-inhibitory or anticariogenic effects) and technological function. By now, targeted and untargeted mass spectrometry, mainly MALDI-TOF-MS and LC–ESI-high resolution MS/MS, allow for the comprehensive analysis of the peptide composition in food. Food peptidomics or food peptide profiling are crucial techniques to identify and quantify bioactive peptides in food and to understand the influence of peptides on food quality. Bioinformatic tools facilitate linking peptide structures and functions. Additionally, peptide profiles can complement the analytical toolbox to assure food authenticity.
The protein and peptide fractions of kashk, a traditional Middle East fermented dairy product
2020, Food Research InternationalKashk is a typical dairy product of Iran, made from sour milk. It is traditionally produced from buttermilk in a dry, round-shaped form. Today, it is also produced at industrial level in a liquid form starting from fermented milk. We aimed to characterise the kashk proteome and peptidome comparing a traditional product with the industrial using a combination of proteomic approaches including advanced chromatographic and electrophoretic separation technique coupled to tandem mass spectrometry. We identified also phosphorylated casein-derived peptides (CPP) and investigated kashk protein digestibility using a static model of food protein digestion. The molecular characterization, coupled with bioinformatic in silico analysis, allowed the identification of potential bioactive peptides.
Influence of the production technology on kefir characteristics: Evaluation of microbiological aspects and profiling of phosphopeptides by LC-ESI-QTOF-MS/MS
2020, Food Research InternationalThe influence of production technology, namely, temperature, pH and 2-step fermentation (back-slopping approach), on the microbiological characteristics and on the phosphopeptide profile of kefir obtained with kefir grains was investigated. The growth of yeasts, lactic acid bacteria (LAB) and acetic acetic bacteria (AAB) in both grains and kefir was affected by the incubation temperature and by the use of back-slopping. In particular, at 25 °C the microbiota of kefir grains was mainly composed by LAB and yeasts, while at 18 °C yeasts represented the dominant group in kefir. Back-slopping at 25 °C determined a significant increase of AAB.
A comprehensive characterization of potentially bioactive peptides, including caseino-phosphopeptides (CPPs), was performed, for the first time, in kefir obtained with kefir grains, using preliminary enrichment on hydroxyapatite followed by dephosphorylation and analysis by Liquid Chromatography-ElectroSpray Ionization-Quadrupole-Time of Flight-tandem mass spectrometry (LC-ESI-QTOF-MS/MS). As a result, seventy-three phosphopeptides, mostly arising from caseins (79% β-casein, 8% αs1-casein and 9% αs2-casein) and all including from three to five serine residues in their sequences, were identified. Seventy-one of them showed the typical motif “SerP-SerP-SerP-Glu-Glu”, which is crucial for the ability of caseins to bind to minerals. Several peptides were observed, for the first time, from the 1–40 region of β-casein. As for the effect of production technology, phosphopeptide profiles of kefirs obtained at 25 °C and 18 °C were very similar, whereas kefir produced under acidic conditions showed a predominance of smaller peptides, suggesting a higher level of proteolysis. Conversely, kefir obtained through back-slopping at 25 °C contained longer peptides, thus indicating a lower proteolytic activity and a poor reproducibility in the kefir phosphopeptide profile occurring when grains are reused.