Influence of Various Phosphopeptides of Caseins on Iron Absorption

Bouhallab, Saı̈d; Činga, V.; Aît-Oukhatar, Nabil; Bureau, F.; Neuville, Dominique; Arhan, Pierre; Maubois, Jean‐Louis; Bouglé, Dominique

doi:10.1021/jf025554v

Cited by 80 publications

(66 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…New studies have shown that the CPPs are a mixture of peptides with different molecular masses in the range from 1.4 to 9.6kDa and that about 50% of the CPPs identified presented the sequence (SerPSerP-SerP-Glu-Glu), responsible for the property of binding minerals [80]. In addition to increasing the solubility, absorption, and fixation of minerals to bones and teeth, the CPPs along with the caseinoglycomacropeptide (GMP) also act by inhibiting the adherence of Streptococcus sobrinus and S. mutans, thus decreasing the incidence of tooth decay and dental erosion [81].…”

Section: Caseinophosphopeptides (Cpps) and Glycomacropeptide (Gmp)mentioning

confidence: 99%

“…These peptides presented high phosphoserine content and were capable of increasing the calcium balance by 39% to 70% in newborn children with rickets. Later studies showed that the CPPs could also bind, in addition to Ca, otherminerals like Mg, Fe, Ba, Cr, Ni, Co, and Se [78,79].New studies have shown that the CPPs are a mixture of peptides with different molecular masses in the range from 1.4 to 9.6kDa and that about 50% of the CPPs identified presented the sequence (SerPSerP-SerP-Glu-Glu), responsible for the property of binding minerals [80]. In addition to increasing the solubility, absorption, and fixation of minerals to bones and teeth, the CPPs along with the caseinoglycomacropeptide (GMP) also act by inhibiting the adherence of Streptococcus sobrinus and S. mutans, thus decreasing the incidence of tooth decay and dental erosion [81].…”

mentioning

confidence: 99%

See 1 more Smart Citation

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

View full text Add to dashboard Cite

Throughout the second half of the last century and early this century the concept of the biological function of food proteins has changed significantly. While in the past the food proteins were regarded only as macronutrients capable of providing the amino acids to form the protein component of organs and tissues, also participating in the generation of metabolic energy for the normal functioning of living organisms, today it is known that certain proteins present in food, as well as fragments or peptides derived thereof, may participate in the general metabolism in a much more interactive manner, through bioactivities that go far beyond the nutritional functions that had been established by the end of the first half of the prior century.By making an analogy with the aeronautical activity we can say that in the past the food proteins functioned as black boxes holding numerous important pieces of information, which research and technology have only revealed, in part, in recent decades. In this period it Received: August 07, 2017; Accepted: September 12, 2017; Published: September 26, 2017 was found that certain proteins present in foods are naturally bioactive, and can be absorbed from the Gastrointestinal System (GIS) in their intact or slightly modified form and exercise specific bioactivities in the systemic metabolism [1], or, in addition, resist the action of digestive enzymes exercising different bioactivities in the gastrointestinal system [2]. Even more interesting were the findings that food proteins, of both plant and animal origin, contain, in their primary structures, specific amino acid sequences in their polypeptide chains, which when cleaved in the form of peptides by proteolytic enzymes or by specific chemical reagents may exercise diverse bioactivities that were latent in the original structure of the protein from which they originated.Bioactive peptides have been obtained from precursor proteins through the use of methodologies that have reached a high degree of sophistication and complexity, such as: (a) enzymatic hydrolysis by digestive enzymes; (b) proteolysis of the protein source by enzymes derived from microorganisms or plants; (c) fermentation process using culture with high proteolytic power and specificity. The bioactive potential of the peptides originating from the proteolysis of food proteins can be explored in the integral hydrolysates, produced in special conditions. However, in the current literature there are numerous research works and literature reviews emphasizing the importance of the isolation, purification, characterization, study of mechanisms and impact of these peptides on human health [3][4][5][6][7][8]. Production and Processing of Bioactive Peptides Derived from Food ProteinsA large number of plants and animals have been object of study as source of Bioactive Peptides (BAPs). Several studies were conducted, particularly with milk proteins [9,10], eggs [11,12], and muscle proteins from pigs [13], cattle [14], poultry [15], and fish [16]. BAPs have been obtained from...

show abstract

Section: Caseinophosphopeptides (Cpps) and Glycomacropeptide (Gmp)mentioning

confidence: 99%

mentioning

confidence: 99%

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

View full text Add to dashboard Cite

show abstract

“…The reviews describe randomised controlled trials investigating the effect of iron supplementation on prevention of iron deficiency and on haemoglobin concentrations in infants and young children (Iannotti et al, 2006;Gera et al, 2007). The applicant also provided in vitro and animal studies (Bouhallab et al, 2002;Etcheverry et al, 2004a, b;Kibangou et al, 2005;Rohner et al, 2007), three extracts from textbooks in German and six reports/papers from scientific bodies as being pertinent to the health claim (IoM, 2001;Aggett et al, 2002;INACG, 2002;JHCI, 2003;FAO/WHO, 2004;DGE, 2008).…”

Section: Scientific Substantiation Of the Claimed Effectmentioning

confidence: 99%

Scientific Opinion on the substantiation of a health claim related to iron and contribution to normal formation of haemoglobin and red blood cells pursuant to Article 14 of Regulation (EC) No 1924/2006

Products¹

2014

EFS2

View full text Add to dashboard Cite

Following an application from Specialised Nutrition Europe (formerly IDACE), submitted pursuant to Article 14 of Regulation (EC) No 1924/2006 via the Competent Authority of France, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA) was asked to deliver an opinion on the scientific substantiation of a health claim related to iron and contribution to normal formation of haemoglobin and red blood cells. The food constituent, iron, which is the subject of the health claim, is sufficiently characterised. Contribution to normal formation of haemoglobin and red blood cells is a beneficial physiological effect for infants and young children. A claim on iron and contribution to normal formation of haemoglobin and red blood cells in the general population has already been assessed by the Panel with a favourable outcome. The Panel considers that the role of iron in normal formation of haemoglobin and red blood cells applies to all ages, including infants and young children (from birth to three years). The Panel concludes that a cause and effect relationship has been established between dietary intake of iron and contribution to normal formation of haemoglobin and red blood cells.

show abstract

“…This is of nutritional interest because of the importance of iron in human health. In addition, in vitro availability of iron bound to casein phosphopeptides and net absorption of iron in animals perfused with β-caseinophosphopeptide (f1-25) are high as a result of the increase in the solubility of iron bound to Antioxidant activity of β-casein hydrolysate 451 the peptides [1,9,48,59]. The phosphorylated groups of casein may also play an important role in regulating the oxidation state of iron [15] and the subsequent development of lipid oxidation.…”

Section: Introductionmentioning

confidence: 99%

?-Caseinophosphopeptide (f1-25) confers on ?-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes

Kansci

Génot²,

Meynier³

et al. 2004

Lait

View full text Add to dashboard Cite

-Protein ingredients such as hydrolysates of milk proteins may improve the nutritive value of functional foods. For instance, β-casein tryptic hydrolysate could simultaneously increase iron absorption and prevent lipid oxidation in foods containing high contents of polyunsaturated fatty acids (PUFA). The aim of this study was to determine the antioxidant activity of β-casein tryptic hydrolysate and of its β-caseinophosphopeptide (f1-25) on Fe(III)/ascorbate-induced oxidation of muscle phospholipids in a liposome system. Oxygen consumption, conjugated dienes (CD), thiobarbituric acid reactive substances (TBARS) and volatile compounds were measured during oxidation at 25 °C of the liposomes in the presence of either the β-casein tryptic hydrolysate (0.24-2.4 mg·mL -1 ) or of its phosphopeptide (0.1-0.31 mg·mL -1 ). Oxygen consumption was significantly enhanced in the presence of β-casein tryptic hydrolysate or of the phosphopeptide (f1-25) and staircase curves were observed for the highest concentrations, showing complex oxidative interactions between iron, β-casein tryptic hydrolysate or phosphopeptide and the phospholipids. In contrast, on an hourly scale, formation of CD, TBARS and total volatile compounds were inhibited. The inhibition of CD and TBARS reached 50% after 20 h of oxidation in the presence of 1.2 mg·mL -1 β-casein tryptic hydrolysate or 0.16 mg·mL -1 phosphopeptide (f1-25). Amounts of total volatile compounds produced after 24 h decreased by about 60% in the presence of the hydrolysate (1.2 mg·mL -1 ) and 50% with the phosphopeptide (f1-25) (0.31 mg·mL -1 ) due to drastic decrease or even disappearance of alkanals and 2-alkenals. Several alcohols such as pentanol and hexanol were produced in higher amounts. Thus β-casein tryptic hydrolysate can protect rich-in-PUFA phospholipid liposomes against long-term iron-induced oxidation, mainly due to iron chelation by β-caseinophosphopeptide (f1-25). This antioxidant activity could benefit specific food products.

show abstract

Influence of Various Phosphopeptides of Caseins on Iron Absorption

Cited by 80 publications

References 19 publications

Food Proteins and Bioactive Peptides, Functional Diets

Food Proteins and Bioactive Peptides, Functional Diets

Scientific Opinion on the substantiation of a health claim related to iron and contribution to normal formation of haemoglobin and red blood cells pursuant to Article 14 of Regulation (EC) No 1924/2006

?-Caseinophosphopeptide (f1-25) confers on ?-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes

Contact Info

Product

Resources

About