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Aspectos nutricionais da caseína - referências

 
1: Am J Clin Nutr. 2006 Nov;84(5):1070-9. Related Articles, Links
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Compared with casein or total milk protein, digestion of milk soluble proteins is too rapid to sustain the anabolic postprandial amino acid requirement.

Lacroix M, Bos C, Léonil J, Airinei G, Luengo C, Daré S, Benamouzig R, Fouillet H, Fauquant J, Tomé D, Gaudichon C.

UMR INRA 914, Physiology of Nutrition and Feeding Control Unit, Institut National Agronomique Paris-Grignon, Paris, France.

BACKGROUND: The in vivo quality of milk protein fractions has seldom been studied in humans. OBJECTIVE: Our objective was to compare the postprandial utilization of dietary nitrogen from 3 [(15)N]-labeled milk products: micellar caseins (MC), milk soluble protein isolate (MSPI), and total milk protein (TMP). DESIGN: The macronutrient intakes of 23 healthy volunteers were standardized for 1 wk, after which time the subjects ingested a meal containing MC (n = 8), MSPI (n = 7), or TMP (n = 8). [(15)N] was measured for an 8-h period in plasma amino acids, proteins, and urea and in urinary urea. RESULTS: The transfer of dietary nitrogen to urea occurred earlier after MSPI ingestion than after MC and TMP ingestion, and concentrations remained high for 8 h, concomitantly with higher but transient hyperaminoacidemia and a higher incorporation of dietary nitrogen into plasma amino acids. In contrast, deamination, postprandial hyperaminoacidemia, and the incorporation of dietary nitrogen into plasma amino acids were lower in the MC and TMP groups. Finally, total postprandial deamination values were 18.5 +/- 2.9%, 21.1 +/- 2.8%, and 28.2 +/- 2.9% of ingested nitrogen in the TMP, MC, and MSPI groups, respectively. CONCLUSIONS: Our results confirm the major role of kinetics in dietary nitrogen postprandial utilization and highlight the paradox of MSPI, which, despite its high Protein Digestibility Corrected Amino Acid Score, ensures a rate of amino acid delivery that is too rapid to sustain the anabolic requirement during the postprandial period. Milk proteins had the best nutritional quality, which suggested a synergistic effect between soluble proteins and caseins.

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PMID: 17093159 [PubMed - indexed for MEDLINE]

 
2: Am J Clin Nutr. 2007 Apr;85(4):1031-40. Related Articles, Links
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Consumption of fluid skim milk promotes greater muscle protein accretion after resistance exercise than does consumption of an isonitrogenous and isoenergetic soy-protein beverage.

Wilkinson SB, Tarnopolsky MA, Macdonald MJ, Macdonald JR, Armstrong D, Phillips SM.

Exercise Metabolism Research Group, Department of Kinesiology, McMaster University, Hamilton, Canada.

BACKGROUND: Resistance exercise leads to net muscle protein accretion through a synergistic interaction of exercise and feeding. Proteins from different sources may differ in their ability to support muscle protein accretion because of different patterns of postprandial hyperaminoacidemia. OBJECTIVE: We examined the effect of consuming isonitrogenous, isoenergetic, and macronutrient-matched soy or milk beverages (18 g protein, 750 kJ) on protein kinetics and net muscle protein balance after resistance exercise in healthy young men. Our hypothesis was that soy ingestion would result in larger but transient hyperaminoacidemia compared with milk and that milk would promote a greater net balance because of lower but prolonged hyperaminoacidemia. DESIGN: Arterial-venous amino acid balance and muscle fractional synthesis rates were measured in young men who consumed fluid milk or a soy-protein beverage in a crossover design after a bout of resistance exercise. RESULTS: Ingestion of both soy and milk resulted in a positive net protein balance. Analysis of area under the net balance curves indicated an overall greater net balance after milk ingestion (P < 0.05). The fractional synthesis rate in muscle was also greater after milk consumption (0.10 +/- 0.01%/h) than after soy consumption (0.07 +/- 0.01%/h; P = 0.05). CONCLUSIONS: Milk-based proteins promote muscle protein accretion to a greater extent than do soy-based proteins when consumed after resistance exercise. The consumption of either milk or soy protein with resistance training promotes muscle mass maintenance and gains, but chronic consumption of milk proteins after resistance exercise likely supports a more rapid lean mass accrual.

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PMID: 17413102 [PubMed - indexed for MEDLINE]

 
3: Am J Clin Nutr. 2004 Nov;80(5):1246-53. Related Articles, Links
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Glycemia and insulinemia in healthy subjects after lactose-equivalent meals of milk and other food proteins: the role of plasma amino acids and incretins.

Nilsson M, Stenberg M, Frid AH, Holst JJ, Björck IM.

Department of Applied Nutrition and Food Chemistry, Lund University, Sweden. mikael.nilsson@inl.lth.se

BACKGROUND: Milk products deviate from other carbohydrate-containing foods in that they produce high insulin responses, despite their low GI. The insulinotropic mechanism of milk has not been elucidated. OBJECTIVE: The objective was to evaluate the effect of common dietary sources of animal or vegetable proteins on concentrations of postprandial blood glucose, insulin, amino acids, and incretin hormones [glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide 1] in healthy subjects. DESIGN: Twelve healthy volunteers were served test meals consisting of reconstituted milk, cheese, whey, cod, and wheat gluten with equivalent amounts of lactose. An equicarbohydrate load of white-wheat bread was used as a reference meal. RESULTS: A correlation was found between postprandial insulin responses and early increments in plasma amino acids; the strongest correlations were seen for leucine, valine, lysine, and isoleucine. A correlation was also obtained between responses of insulin and GIP concentrations. Reconstituted milk powder and whey had substantially lower postprandial glucose areas under the curve (AUCs) than did the bread reference (-62% and -57%, respectively). Whey meal was accompanied by higher AUCs for insulin (90%) and GIP (54%). CONCLUSIONS: It can be concluded that food proteins differ in their capacity to stimulate insulin release, possibly by differently affecting the early release of incretin hormones and insulinotropic amino acids. Milk proteins have insulinotropic properties; the whey fraction contains the predominating insulin secretagogue.

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PMID: 15531672 [PubMed - indexed for MEDLINE]

 
4: J Nutr. 2003 Sep;133(9):2733-40. Related Articles, Links
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Increasing habitual protein intake accentuates differences in postprandial dietary nitrogen utilization between protein sources in humans.

Morens C, Bos C, Pueyo ME, Benamouzig R, Gausserès N, Luengo C, Tomé D, Gaudichon C.

Institut National de la Recherche Agronomique, Unité de Physiologie de la Nutrition et du Comportement Alimentaire, Institut National Agronomique Paris-Grignon, 75005 Paris, France.

It is appropriate to characterize the nutritional value of dietary proteins in humans through the specific study of dietary nitrogen metabolism during the postprandial period. However, the influence of the habitual protein intake on this variable has not been studied. We aimed to describe the influence of prior protein intake on the specific metabolic utilization of dietary nitrogen in humans. Healthy men and women were adapted for 7 d to two diets with a normal [NP, 1 g/(kg x d)] and high protein content [HP, 2 g/(kg x d)]. After each period, they were studied for an 8-h postmeal period after ingesting a single (15)N-labeled mixed meal (0.41 g/kg protein) containing either milk (n = 12) or soy protein (n = 8). The HP diet reduced the peak of dietary N incorporation into free serum amino acids in the soy group but had no effect in the milk group. The incorporation of dietary N into plasma protein was higher after soy than after milk protein, but habitual protein level had no effect. The postprandial retention of milk protein was reduced by the HP diet compared with the NP diet by only 5% and that of soy protein was diminished by 13% (protein source: P < 0.0001, protein level: P < 0.0001, interaction: P < 0.001). In conclusion, the efficiency of the meal N postprandial retention was lower after HP adaptation, but this decrease was much more pronounced for soy than for milk protein, indicating that increasing the habitual protein intake accentuates differences in metabolic utilization among dietary proteins.

PMID: 12949358 [PubMed - indexed for MEDLINE]
 
5: J Dairy Sci. 1998 Apr;81(4):909-17. Related Articles, Links
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The digestible amino acid composition of several milk proteins: application of a new bioassay.

Rutherfurd SM, Moughan PJ.

Monogastric Research Centre, College of Sciences, Massey University, Palmerston North, New Zealand.

The aim of the present study was to determine the composition of amino acids that were truly digestible in the ileum. Several bovine milk products and two soy protein products were tested using the newly developed enzymatically hydrolyzed casein-ultrafiltration (UF) method. This method provides a novel approach for determining endogenous flows of amino acids at the terminal ileum, which are required for correcting apparent ileal digestibility values to true digestibility values. Digestibility was determined by sampling digesta of Sprague-Dawley male rats at the end of the small intestine (ileum). Chromic oxide was used as an indigestible marker. The traditional protein-free method for determining endogenous losses of amino acids was also used for comparison with the enzymatically hydrolyzed casein-UF method. Flows of endogenous amino acids at the terminal ileum of the rat following peptide alimentation were generally higher (1.8-fold) than those determined after a protein-free diet was fed. Compared with values for true amino acid digestibility, apparent values underestimated digestibility by 2 to 30%. True amino acid digestibility was high (79 to 102%) for all of the protein sources. The digestible amounts of methionine and lysine were 2 and 1.3 times higher, respectively, in dairy proteins than in soy proteins. The enzymatically hydrolyzed casein-UF method provides a physiological estimate of endogenous amino acid flow and appeared to be an appropriate method for correcting apparent digestibility values to true digestibility values. The data for true ileal digestibility of amino acids obtained using this technique demonstrated the high quality of bovine milk proteins.

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PMID: 9594381 [PubMed - indexed for MEDLINE]

 
6: Br J Nutr. 2003 Feb;89(2):239-48. Related Articles, Links
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Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite.

Hall WL, Millward DJ, Long SJ, Morgan LM.

Centre for Nutrition and Food Safety, School of Biomedical and Life Sciences, University of Surrey, Guildford, Surrey GU2 7XH. w.hall@surrey.ac.uk

Protein, generally agreed to be the most satiating macronutrient, may differ in its effects on appetite depending on the protein source and variation in digestion and absorption. We investigated the effects of two milk protein types, casein and whey, on food intake and subjective ratings of hunger and fullness, and on postprandial metabolite and gastrointestinal hormone responses. Two studies were undertaken. The first study showed that energy intake from a buffet meal ad libitum was significantly less 90 min after a 1700 kJ liquid preload containing 48 g whey, compared with an equivalent casein preload (P<0.05). In the second study, the same whey preload led to a 28 % increase in postprandial plasma amino acid concentrations over 3 h compared with casein (incremental area under the curve (iAUC), P<0.05). Plasma cholecystokinin (CCK) was increased by 60 % (iAUC, P<0.005), glucagon-like peptide (GLP)-1 by 65 % (iAUC, P<0.05) and glucose-dependent insulinotropic polypeptide by 36 % (iAUC, P<0.01) following the whey preload compared with the casein. Gastric emptying was influenced by protein type as evidenced by differing plasma paracetamol profiles with the two preloads. Greater subjective satiety followed the whey test meal (P<0.05). These results implicate post-absorptive increases in plasma amino acids together with both CCK and GLP-1 as potential mediators of the increased satiety response to whey and emphasise the importance of considering the impact of protein type on the appetite response to a mixed meal.

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PMID: 12575908 [PubMed - indexed for MEDLINE]

 
1: Curr Pharm Des. 2003;9(16):1257-75. Related Articles, Links
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Antibacterial and antiviral effects of milk proteins and derivatives thereof.

Florisa R, Recio I, Berkhout B, Visser S.

Department of Product Technology, NIZO food research, P.O. Box 20, 6710 BA Ede, The Netherlands.

Milk forms a rich source of biologically interesting components. In particular, its protein fraction is known to encompass many kinds of biological functions. In this review we focus on antibacterial and antiviral properties of milk proteins and milk protein derivatives. The latter include chemically modified proteins and enzymatically induced peptides. If such peptides are released by enzymes present within the digestive tract (e.g. trypsin or pepsin), it is likely that they play a role in the health defense system. This is especially the case when the active fragments can survive the intestinal conditions long enough to arrive at the right place to exert their beneficial function. In the first part of this paper attention is paid to the antibacterial proteins lactoferrin, lactoperoxidase, and lysozyme. Furthermore, antibacterial peptides originating from caseins and whey proteins are described. The second part reports on studies of antiviral effects of milk proteins and derivatives thereof. Special focus is directed to the antiviral action towards the human immunodeficiency virus (HIV) and the human cytomegalovirus (HCMV). Unmodified milk proteins are generally not active against these viruses. An exception is lactoferrin, which shows significant antiviral activity against both HIV and HCMV. Several other milk proteins tested showed strong antiviral effects only after chemical modification, i.e. by making them polyanionic (for anti-HIV activity) or polycationic (for anti-HCMV activity). In a number of cases, conclusions are drawn concerning possible relationships between antibacterial/antiviral activity and molecular structure of the components described.

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PMID: 12769735 [PubMed - indexed for MEDLINE]

 
2: J Exp Ther Oncol. 2007;6(2):89-106. Related Articles, Links

Milk-derived proteins and peptides of potential therapeutic and nutritive value.

Zimecki M, Kruzel ML.

Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

Milk and colostrum are rich in proteins and peptides which play a crucial role in development of the immune system in mammalian offspring. Immunotropic properties of these compounds prompted investigators to search for their utility in prevention and therapy of various disorders in humans. The following constituents of milk are of particular interest: 1) Lactoferrin (LF)--exhibits antibacterial, antifungal, antiviral, antiparasite and antitumor activities. It is protective with regard to intestinal epithelium, promotes bone growth and accelerates recovery of the immune system function in immunocompromised animal; 2) A Proline-Rich Polypeptide (PRP) shows a variety of immunotropic functions, including promotion of T-cell maturation and inhibition'of autoimmune disorders. PRP was recently found to improve or stabilize the Instrumental Activity of Daily Living status in Alzheimer's disease patients. 3) Casein--has been protective in experimental bacteremia by eliciting myelopoiesis. Casein hydrolyzates were also protective in diabetic animals, reduced the tumor growth and diminished colicky symptoms in infants. Casein-derived peptides have been found to have antihypertensive effects. Glycomacropeptide (GMP)--a peptide derived from kappa casein, exhibits antibacterial and antithrombotic activities. 4) Alpha lactalbumin (LA)--demonstrates antiviral, antitumor and anti-stress properties. LA-enriched diets were anxiolytic, lowered blood pressure in rats, prevented diarrhea and led to a better weight gain in malnourished children. 5) Lysozyme--is effective in treatment of periodentitis and prevention of tooth decay. Milk enriched in lysozyme was used in feeding premature infants suffering from concomitant diseases. 6) Lactoperoxidase--shows antibacterial properties. In conclusion, milk-derived proteins and peptides are bio-accessible and safe for the prevention and treatment of numerous disorders in humans.

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PMID: 17407968 [PubMed - indexed for MEDLINE]

 
3: Life Sci. 2000 Oct 20;67(22):2745-52. Related Articles, Links
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First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation.

Wang H, Ye X, Ng TB.

Department of Microbiology, China Agricultural University, Beijing.

A variety of milk proteins including lactoferrin, angiogenin-1, alpha-lactalbumin, beta-lactoglobulin, lactoperoxidase, casein and the novel whey proteins lactogenin and glycolactin were tested for inhibitory activity toward human immunodeficiency virus-1 reverse transcriptase (HIV-1 RT), alpha-glucosidase, beta-glucosidase and beta-glucuronidase. Lactoferrin exerted the most potent inhibitory action with an IC50 of about 6 microM. Lactoperoxidase, lactogenin, angiogenin-1 and glycolactin inhibited HIV-1 RT activity with decreasing potencies. Beta-lactoglobulin, alpha-lactalbumin and casein displayed little or no inhibitory effect. Succinylation with succinic anhydride augmented the inhibitory effect of glycolactin, beta-lactoglobulin, alpha-lactalbumin, casein and human lactoferrin. The inhibitory effect of the various milk proteins on the activities of alpha-glucosidase, beta-glucosidase and beta-glucuronidase was meager. Succinylation tended to increase the alpha-glucosidase-inhibitory effect of milk proteins but neither their beta-glucosidase-inhibitory nor beta-glucuronidase-inhibitory effect was affected.

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PMID: 11105990 [PubMed - indexed for MEDLINE]

 
4: Curr Pharm Des. 2003;9(16):1239-55. Related Articles, Links
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Biodefense properties of milk: the role of antimicrobial proteins and peptides.

Clare DA, Catignani GL, Swaisgood HE.

Southeast Dairy Foods Research Center, Department of Food Science, North Carolina State University, Raleigh, NC 27695-7624, USA. debra_clare@ncsu.edu

Mammary fluids, colostrum and milk, deliver nature's first host defense systems upon birth, and these essential liquids are critical for survival of the neonate. The identification and characterization of anti-infectious proteins were among the early scientific discoveries and this group of proteins has long been recognized for promoting health benefits in both newborns and adults. Among the more widely studied are the immunoglobulins, lactoperoxidase, lysozyme, and lactoferrin. Recently, it was shown that alpha--lactalbumin may also function in a protective capacity dependent upon its folding state. Some of these, especially lactoferrin, also display an immunomodulatory role in which case a totally separate cascade of host defense responses is initiated. It was noted that the mechanism of action for this cluster of sentry proteins does vary; thus, this protective strategy provides for a broad range of responsive reactions to infection. Presently, there is a major focus on the discovery of novel peptides that can be generated from existing milk proteins via proteolytic reactions. To date, this substrate list includes alpha--lactalbumin, beta-lactoglobulin, all casein fractions, and lactoferrin. Again, the immunoregulatory effects prompted as a result of the appearance of these peptides are currently being defined. Herein, we review the principal biological properties associated with each of these contributing milk components with a special emphasis on the role of biodefensive milk peptides. We envision future contributions emerging from this research field as an opportunity to develop effective new therapies to be used in treating infectious diseases and promoting health benefits in vivo.

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PMID: 12769734 [PubMed - indexed for MEDLINE]

 
5: Curr Pharm Des. 2006;12(13):1637-43. Related Articles, Links
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Emerging therapeutic potential of whey proteins and peptides.

Yalçin AS.

Department of Biochemistry, School of Medicine, Marmara University, Istanbul, Turkey. asyalcin@marmara.edu.tr

Whey is a natural by-product of cheese making process. Bovine milk has about 3.5% protein, 80% of which are caseins and the remaining 20% are whey proteins. Whey proteins contain all the essential amino acids and have the highest protein quality rating among other proteins. Advances in processing technologies have led to the industrial production of different products with varying protein contents from liquid whey. These products have different biological activities and functional properties. Also recent advances in processing technologies have expanded the commercial use of whey proteins and their products. As a result, whey proteins are used as common ingredients in various products including infant formulas, specialized enteral and clinical protein supplements, sports nutrition products, products specific to weight management and mood control. This brief review intends to focus on scientific evidence and recent findings related to the therapeutic potential of whey proteins and peptides.

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PMID: 16729875 [PubMed - indexed for MEDLINE]

 
6: Food Chem Toxicol. 1996 Jan;34(1):131-45. Related Articles, Links
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Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides.

Lahov E, Regelson W.

Medical College of Virginia/Virginia Commonwealth University, Richmond 23298, USA.

Apart from immunoglobulin A and G antibodies and plasma cells, milk also contains antibiotic/host protective peptides that are of value not only for maintenance of its nutritional integrity but also for protection of the newborn and, possibly, protection of the lactating mother. Among the first such peptides identified with casecidin; following chymosin digestion of casein at pH 6 or 7, casecidin inhibited in vitro staphylococci, sarcina, Bacillus subtilis, Diplococcus pneumoniae and Streptococcus pyogenes. Inhibition occurred at high concentrations, in vitro, compared with commercial antibiotics, and thus interest in casecidin languished. Work with casecidin was followed by investigation of a related refined non-immunogenic product of chymosin digestion of alpha s1-casein. This product consisted of the N -terminal segment (1-23) of alpha s1-casein B, named "isracidin", and was significantly effective in vivo at concentrations that were competitive with known antibiotics, as seen in the protection of mice against lethal infection by Staphylococcus aureus strain Smith. Field trials showed that injection of isracidin into the udder gave protection against mastitis in sheep and cows. Isracidin was both therapeutic and prophylactic and responses to its therapeutic effect produced long-term immune resistance. Isracidin protected mice against Candida albicans, by stimulation of both phagocytosis and immune responses. However, like other recently described milk-derived peptides, despite its clinical value, isracidin was overlooked because of the lack of commercial interest in the 1970s and early 1980s, in host-mediated non-specific resistance as a therapeutic approach to infection. Another problem that impeded commercial interest was the isomeric variation in isracidin peptides seen on a large-scale batch production for commercial use. It is hoped that this review of previous studies of the activity of isracidin action will revive interest in milk as an antibiotic source.

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PMID: 8603791 [PubMed - indexed for MEDLINE]

 
7: Biopolymers. 1997;43(2):99-117. Related Articles, Links
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Milk protein-derived opioid receptor ligands.

Teschemacher H, Koch G, Brantl V.

Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität, Giessen, Germany.

Milk is mammalian characteristic and is of particular importance for humans: Mother's milk or its substitutes from cows' milk are absolutely essential nutriments for the neonate and cows' milk also represents a basic foodstuff for adults. However, in addition to their well-known nutritive role, milk constituents apparently are also able to carry specific information from the milk producer's to the milk receiver's organism: Thus, a number of milk protein fragments has been shown to behave like opioid receptor ligands able to address opioidergic systems in the adult's or in the neonate's organism. With respect to the proteins, which they are derived off these peptides have been named alpha-casein exorphins or casoxin D (alpha-casein), beta-casomorphins or beta-casorphin (beta-casein), casoxin or casoxin A, B, or C (k-casein), alpha-lactorphins (alpha-lactalbumin), beta-lactorphin (beta-lactoglobulin) or lactoferroxins (lactoferrin). Only casoxins and lactoferroxins display antagonistic properties; the other peptides behave like opioid receptor agonists. Most of the information available so far has been collected about beta-casomorphins. These peptides obviously can be released from beta-casein in the adult's or in the neonate's organism, where they might elicit opioid effects in the frame of a regulatory role as "food hormones". Several synthetic beta-casomorphin derivatives have been shown to be highly specific and potent mu-type opioid receptor ligands which frequently have been used as standard tools in opioid research.

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PMID: 9216246 [PubMed - indexed for MEDLINE]

 
8: Postepy Hig Med Dosw (Online). 2006;60:352-69. Related Articles, Links
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[Antitumor and chemopreventive activity of lactoferrin]

[Article in Polish]

Artym J.

Zakład Terapii Doświadczalnej Instytutu Immunologii i Terapii Doświadczalnej PAN, im. Ludwika Hirszfelda we Wrocławiu. limbiol@iitd.pan.wroc.pl

Lactoferrin, an evolutionarily old protein of the transferrin family, is among the proteins constituting the system of innate immunity; its action, however, also extends to the regulation of acquired immunity and other immunological phenomena. The actions of LF, confirmed in numerous in vitro and in vivo models, include participation in iron homeostasis, immunoregulatory properties, anti-inflammatory, anti-tumor, and analgesic actions, regulation of bone metabolism, participation in embryonic development, reproductive functions, and others. LF plays an important role in the normal development of a newborn. The anti-tumor properties of LF were discovered about a decade ago and have been confirmed in many laboratory, preclinical, and clinical studies. The immunomodulatory properties of LF play a major role in its anti-tumor actions. Such actions of LF appeared particularly effective in cancer patients with impaired immunity. The growth of tumors is facilitated by low expressions of MHC and co-stimulatory antigens on tumor cells and the induction of suppressor cells and other inhibitory products by tumors. Enhancement of an anti-tumor immunological response may, therefore, restrict tumor growth. Studies showed that LF elevates the number and increases the activity of T and B lymphocytes and NK cells, stimulates the release of a number of cytokines (IL-1, -6, -8, -18, IFN-gamma, TNF alpha), increases phagocytic activity and cytotoxicity of monocytes/macrophages, accelerates the maturation of T and B cells, and elevates the expression of several types of cellular receptors, such as CD4, zeta chain of the CD3 complex, LFA-1, CD11, ICAM-1, and selectin P. Apart from its immunomodulatory properties, LF exhibits direct anti-tumor actions, such as lytic, pro-apoptotic, anti-proliferative, anti-angiogenic, anti-oxidant activity and the chelation of iron ions. LF also possesses chemo-preventive properties, regulates the activity of phase I and II enzymes participating in the activation and detoxification of carcinogens, and regulates the composition of the intestinal microflora. In this way it prevents the generation of tumors and their development at early stages of carcinogenesis.

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PMID: 16885906 [PubMed - indexed for MEDLINE]

 
9: Biol Neonate. 1998;74(2):163-76. Related Articles, Links
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Protective function of proteins and lipids in human milk.

Hamosh M.

Department of Pediatrics, Georgetown University Medical Center, Washington, DC 20007, USA. hamoshp@medlib.georgetown.edu

Human milk provides the infant with protection against infectious diseases. This protection is conferred through several mechanisms: specific antibody targeted protection against pathogens in the infant's environment (through milk IgA, IgG, and IgM) and broad-spectrum, nonspecific protection provided through several distinct mechanisms. These are: bactericidal effects (lactoferrin), bacteriostatic action (lactoferrin, lysozyme), lysis of microorganisms (lysozyme), antiviral effects (lactoferrin, products of milk fat digestion), antiprotozoan activity (free fatty acids produced during gastric and intestinal digestion of milk fat), and ligand action (inhibition of Helicobacter pylori adhesion to gastric mucosa by kappa-casein). In addition to these protective functions of the proteins and lipids of human milk, several enzymes present in human milk might provide protection by generating components that are bactericidal (bile salt dependent lipase, peroxidase), prevent inflammatory reactions (platelet-activating factor acetylhydrolase), or protect the integrity of milk proteins (antiproteases).

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PMID: 9691157 [PubMed - indexed for MEDLINE]

 
10: J Nutr. 2005 Jun;135(6):1438-43. Related Articles, Links
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Substitution of casein by beta-casein or of whey protein isolate by alpha-lactalbumin does not affect mineral balance in growing rats.

Van Dael P, Kastenmayer P, Clough J, Jarret AR, Barclay DV, Maire JC.

Nestlé Research Centre, Vers-chez-les-Blanc, CH-1000 Lausanne, Switzerland.

Bovine milk protein fractions that enable modification of the protein composition and amino acid profile of infant formulas to mimic those of human milk have recently become available. To determine the effects on protein quality and mineral bioavailability of replacing casein by beta-casein and of whey protein isolate by alpha-lactalbumin, 4 groups of growing rats were fed for 3 wk diets containing 10% protein as 1) casein (control); 2) beta-casein; 3) casein:whey (40:60); or 4) beta-casein:alpha-lactalbumin (40:60). Protein quality, determined as protein efficiency ratio (PER), net protein utilization (NPU), biological value (BV) and protein digestibility (PD), as well as body weight gain, were higher (P < 0.05) with consumption of the whey-adapted diets [casein:whey (40:60); beta-casein:alpha-lactalbumin (40:60)] compared with the casein diets (casein; beta-casein); however, there were no differences between the 2 casein diets or between the 2 whey-adapted diets. Apparent absorption of minerals (Ca, P, Fe, Zn) from the whey-adapted diets was higher than that from the casein diets (P < 0.05); but again, no differences were observed when casein or whey protein isolate were replaced by beta-casein or alpha-lactalbumin, respectively. Thus, substitution of casein by beta-casein or of whey protein isolate by alpha-lactalbumin does not affect protein quality or mineral bioavailability as determined in growing rats.

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PMID: 15930449 [PubMed - indexed for MEDLINE]

 
11: Biopolymers. 1997;43(2):119-28. Related Articles, Links
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Biochemical properties of regulatory peptides derived from milk proteins.

Meisel H.

Federal Dairy Research Centre, Institute for Chemistry and Physics, Kiel, Germany.

Biologically active peptides derived from milk proteins are inactive within the sequence of the precursor proteins but can be released by enzymatic proteolysis. Based on structure-activity studies, peptides with a defined bioactivity show common structural features. Moreover, many milk protein-derived peptides reveal multifunctional bioactivities. Bioactive peptide fragments originating from milk proteins should be taken into account as potential modulators of various regulatory processes in the body. Opioid peptides are opioid receptor ligands with agonistic or antagonistic activities. Angiotensin converting enzyme (ACE) inhibitory peptides can exert an antihypertensive effect. Immunomodulating casein peptides have been found to stimulate the proliferation of human lymphocytes and the phagocytic activities of macrophages. Antimicrobial peptides have been shown to kill sensitive microorganisms. Antithrombotic peptides inhibit the fibrinogen binding to a specific receptor region on the platelet surface and also inhibit aggregation of platelets. Casein phosphopeptides can form soluble organophosphate salts and may function as carriers for different minerals, especially calcium. In relation to their mode of action, bioactive peptides may reach target sites (e.g., receptors, enzymes) at the luminal side of the intestinal tract or after absorption, in peripheral organs. The physiological significance of bioactive peptides as exogenous regulatory substances is not yet fully understood. Nevertheless, several bioactive peptides derived from milk proteins have been shown to exert beneficial physiological effects. Milk-derived peptides were already produced on an industrial scale and as a consequence these peptides have been considered for application both as dietary supplements in "functional foods" and as drugs.

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PMID: 9216247 [PubMed - indexed for MEDLINE]

 
12: Altern Med Rev. 2004 Jun;9(2):136-56. Related Articles, Links
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Therapeutic applications of whey protein.

Marshall K.

Whey, a protein complex derived from milk, is being touted as a functional food with a number of health benefits. The biological components of whey, including lactoferrin, beta-lactoglobulin, alpha-lactalbumin, glycomacropeptide, and immunoglobulins, demonstrate a range of immune-enhancing properties. In addition, whey has the ability to act as an antioxidant, antihypertensive, antitumor, hypolipidemic, antiviral, antibacterial, and chelating agent. The primary mechanism by which whey is thought to exert its effects is by intracellular conversion of the amino acid cysteine to glutathione, a potent intracellular antioxidant. A number of clinical trials have successfully been performed using whey in the treatment of cancer, HIV, hepatitis B, cardiovascular disease, osteoporosis, and as an antimicrobial agent. Whey protein has also exhibited benefit in the arena of exercise performance and enhancement.

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PMID: 15253675 [PubMed - indexed for MEDLINE]

 
13: Antiviral Res. 2002 Aug;55(2):341-55. Related Articles, Links
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Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and protein-derived peptides.

Berkhout B, van Wamel JL, Beljaars L, Meijer DK, Visser S, Floris R.

Department of Human Retrovirology, Academic Medical Center, University of Amsterdam, Meibergdreef 15, 1105 AZ, Amsterdam, The Netherlands. b.berkhout@amc.uva.nl

In a search for natural proteins with anti-HIV activity, we screened a large set of purified proteins from bovine milk and peptide fragments thereof. Because several charged proteins and peptides are known to inhibit the process of virus entry, we selected proteins with an unusual charge composition or hydrophobicity profile. In contrast with some chemically modified (strongly negative) milk proteins, unmodified alpha(s2)-, beta- and kappa-casein, as well as several negatively and positively charged fragments thereof, did not show significant inhibition of virus replication. In fact, HIV-1 replication was elevated in the presence of beta-casein or amphiphilic fragments thereof. Bovine lactoferrin (bLF), a milk protein of 80 kDa, showed considerable inhibitory activity against HIV-1 with an IC50 of 0.4 microM. Modest inhibition was obtained with lactoferricin, a highly positively charged loop domain of bLF, indicating that other domains within the native bLF protein may also be required for inhibition. bLF blocked HIV-1 variants that use either the CXCR4 or the CCR5 coreceptor. In order to obtain further insight into the mechanism of action of this antiviral protein, we selected a bLF-resistant HIV-1 variant. The bLF-resistance phenotype is mediated by the viral envelope protein, which contains two interesting mutations that have previously been associated with an altered virus-host interaction and a modified receptor-coreceptor interaction. These results demonstrate that bLF targets the HIV-1 entry process. Copyright 2002 ElsevierScience BV.

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PMID: 12103434 [PubMed - indexed for MEDLINE]

 
14: Oral Dis. 2002 Jan;8(1):23-9. Related Articles, Links
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Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety.

Tenovuo J.

Institute of Dentistry and Turku Immunology Centre, University of Turku, Finland. jorma.tenovuo@utu.fi

Innate human salivary defence proteins, lysozyme, lactoferrin and peroxidase, are known to exert a wide antimicrobial activity against a number of bacterial, viral and fungal pathogens in vitro. Therefore, these proteins, alone or in combinations, have been incorporated as preservatives in foods and pharmaceuticals as well as in oral health care products to restore salivas' own antimicrobial capacity in patients with dry mouth. These antimicrobials used in oral health care products, such as dentifrices, mouth-rinses, moisturizing gels and chewing gums, have been purified from bovine colostrum. In this review I critically evaluate the clinical efficacy and safety of this kind of preventive approach against various oral diseases and symptoms.

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PMID: 11936452 [PubMed - indexed for MEDLINE]

 
15: Crit Rev Food Sci Nutr. 2003;43(6):607-33. Related Articles, Links

Peptides from milk proteins and their properties.

Kilara A, Panyam D.

Arun Kilara Worldwide, 1020 Lee Road, Suite 200, Northbrook, IL 60062-3818, USA. kilara@akilara.com

This review has attempted to study the literature pertaining to peptides derived from milk proteins. Hydrolysis of milk proteins to generate peptides has been practiced for a long time and it was recognized early on in this process that the taste of hydrolyzates might hinder use of these products in food formulations. Modification of protein is necessary to form a more acceptable or utilizable product, to form a product that is less susceptible to deteriorative reactions and to form a product that is of higher nutritionall quality. Modifications may be achieved by a number of chemical and enzymatic means. This review has considered only enzymatic modification of dairy proteins. Modified proteins contain peptides and some of these peptides have been purified and their functionalities have been compared with unmodified proteins. This paper has examined the literature pertaining to improvement in functionality of enzyme-modified proteins. Improvements in solubility, emulsification, foaming and gelation were examined. There is limited information available on the sequence of the peptides necessary to improve the functional characteristics of proteins. Knowing the sequences of desirable functional peptides can lead to genetic alteration of proteins to improve functionality. Addition of synthetic peptides to intact proteins may be another way in which the functionality of proteins can be augmented. Some of the peptides in milk proteins are capable of affecting biological functions of an organism. These effects can be antimicrobial and probiotic, i.e., prevent the growth and proliferation of undesirable and pathogenic organisms, or they may promote the growth of desirable bacteria in the digestive tract of humans and animals. Peptides derived from milk protein have been shown to exert digestive and metabolic effects as well. They may also influence the immune system. These biological effects may play an important role in the development of medical foods that treat or mitigate the effects of diseases. Proteins are allergens and therefore it is possible that products derived from modification of proteins may also be allergens. The known literature about the allergenicity of peptides derived from milk proteins has been examined in this article. Last, but not the least, the taste attributes of peptides is also considered. Bitterness of hydrolyzates is a common occurrence and the origins of these bitter peptides and possible ways of mitigating this sensory defect has been discussed. Many of the peptides that enhance functionality and exert biological activity are likely to be bitter. Therefore, the bitter taste of hydrolysis products has to be dealt with in boosting the functional or nutraceutical aspects of foods containing these peptides. Analytical techniques for sequencing peptides have become more accessible and purification of peptides is commercially feasible. Computer based modeling techniques have aided the prediction of structures in these peptides. These advances, coupled with the advances in biotechnology, promise to revolutionize the future of nutraceutical and functional foods.

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PMID: 14669880 [PubMed - indexed for MEDLINE]

 
16: J Dairy Sci. 1993 Jan;76(1):301-10. Related Articles, Links
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Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities.

Fiat AM, Migliore-Samour D, Jollès P, Drouet L, Bal dit Sollier C, Caen J.

Laboratoire des Protéines, Centre National de la Recherche Scientifique, URA 1188, University of Paris V, France.

The present paper is devoted to the study of short peptides derived from milk proteins with physiological activities. Some of them behaved as opioids, enzyme inhibitors that convert angiotensin I, peptides that enhance calcium absorption, antiaggregating and antithrombotic peptides, and immunomodulating peptides. Some possessed several physiological properties, such as the C-terminal part of bovine alpha s1-casein. A strategic zone, containing immunostimulating and opioid peptides, could be located in cow and human beta-caseins. Few of these peptides or precursor peptides have so far been characterized in vivo in blood or brain after ingestion of milk. If, in the future, some of the active peptides cannot be characterized in vivo, they can all nevertheless be synthesized and used either as food additives or in pharmacology.

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PMID: 8436680 [PubMed - indexed for MEDLINE]

 
17: Curr Pharm Des. 2007;13(8):829-43. Related Articles, Links
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Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum.

Korhonen H, Pihlanto A.

MTT Agrifood Research Finland, Biotechnology and Food Research, FIN-31600 Jokioinen, Finland. hannu.j.korhonen@mtt.fi.

Milk proteins are known to exert a wide range of nutritional, functional and biological activities. Apart from being a balanced source of valuable amino acids, milk proteins contribute to the consistency and sensory properties of various dairy products. Furthermore, many milk proteins possess specific biological properties which make them potential ingredients of health-promoting foods. These properties are attributed to both native protein molecules and to physiologically active peptides encrypted in the protein molecules. Considerable progress has been made over the last twenty years in technologies aimed at separation, fractionation and isolation in a purified form of many interesting proteins occurring in bovine colostrum and milk. Industrial-scale methods have been developed for native whey proteins such as immunoglobulins, lactoferrin, lactoperoxidase, alpha-lactalbumin and beta-lactoglobulin. Their large-scale manufacture and commercial exploitation is still limited although validated research data about their physiological health benefits is rapidly accumulating. Promising product concepts and novel fields of use have emerged recently, and some of these molecules have already found commercial applications. The same applies to bioactive peptides derived from different milk proteins. Active peptides can be liberated during gastrointestinal digestion or milk fermentation with proteolytic enzymes. Such peptides may exert a number of physiological effects in vivo on the gastrointestinal, cardiovascular, endocrine, immune, nervous and other body systems. However, at present the industrial-scale production of such peptides is limited by a lack of suitable technologies. On the other hand, a number of bioactive peptides have been identified in fermented dairy products, and there are already a few commercial dairy products enriched with blood pressure-reducing milk protein peptides. There is a need to develop methods to optimise the activity of bioactive peptides in food systems and to enable their optimum utilisation in the body. This review highlights existing modern technologies applicable for the isolation of bioactive native proteins and peptides derived from bovine colostrum, milk and cheese whey, and discusses aspects of their current and potential applications for human nutrition and promotion of human health.

PMID: 17430184 [PubMed - in process]
 
18: J Agric Food Chem. 2005 Oct 5;53(20):7673-80. Related Articles, Links
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Sialic acid-containing milk proteins show differential immunomodulatory activities independent of sialic acid.

Mikkelsen TL, Bakman S, Sørensen ES, Barkholt V, Frøkiaer H.

BioCentrum-DTU, Biochemistry and Nutrition, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.

The immunomodulatory activities of four sialic acid-containing milk proteins (kappa-casein, glycomacropeptide, lactoferrin, and proteose peptone-3 component) were determined, and the role of sialic acid was evaluated. Two in vitro models were used: murine splenocyte proliferation, where the effect on LPS-, Con A-, and PHA-stimulated proliferation was studied, and cytokine production in LPS-stimulated murine dendritic cells (DC). All four proteins inhibited LPS-induced splenocyte proliferation, though to different degrees, and independently of sialic acid. kappa-Casein strongly inhibited PHA-induced proliferation and had a weak inhibitory effect on Con A-induced proliferation, whereas lactoferrin stimulated Con A-induced proliferation. kappa-Casein, glycomacropeptide, and lactoferrin differentially affected cytokine production by DC: kappa-casein significantly inhibited production of TNF-alpha, IL-10, -12, -6, and -1beta, independent of sialic acid, whereas less-marked effects of glycomacropeptide and lactoferrin were seen. These findings thus point to important immunosuppressive effects of some milk proteins and indicate that they may function via different mechanisms.

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PMID: 16190615 [PubMed - indexed for MEDLINE]