ArticlePDF AvailableLiterature Review

Emerging Therapeutic Potential of Whey Proteins and Peptides


Abstract and Figures

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.
Content may be subject to copyright.
Current Pharmaceutical Design, 2006, 12, 1637-1643 1637
1381-6128/06 $50.00+.00 © 2006 Bentham Science Publishers Ltd.
Emerging Therapeutic Potential of Whey Proteins and Peptides
A. Süha Yalçın
Department of Biochemistry, School of Medicine, Marmara University, Istanbul, Turkey
Abstract: 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 pro-
duction of different products with varying protein contents from liquid whey. These products have different biological ac-
tivities 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.
Key Words: Whey proteins, α-lactalbumin, β-lactoglobulin, immunoglobulin, lactoferrin, bioactive peptide.
Whey is a natural by-product of cheese making process.
Bovine milk has about 3.5 % protein, 80 % of which are ca-
seins and the remaining 20 % are whey proteins. During
cheese manufacture when casein is removed from whole
milk, what remains is whey which contains lactose, proteins
and lipids. Advances in processing technologies have led to
the industrial production of different products with varying
protein contents from liquid whey [1]. Table 1 lists some of
these products and their functional properties.
Recent studies have shown that whey proteins contain all
the essential amino acids and have the highest protein quality
rating among other proteins [2]. Whey proteins are also con-
sidered to be “fast proteins” since they reach the jejunum
almost immediately, their hydrolysis within the intestine is
slower than other proteins and their digestion and absorption
occurs over a greater length of the intestine [2, 3]. Some
whey proteins have even been detected intact in the intestinal
lumen. Recent advances in processing technologies have
expanded the commercial use of whey proteins and their
products [4, 5]. As a result, whey proteins are used as com-
mon ingredients in various products including infant formu-
las, specialized enteral and clinical protein supplements,
sports nutrition products, products specific to weight man-
agement and mood control [6-8]. This brief review intends to
focus on scientific evidence and recent findings related to the
therapeutic potential of whey proteins and peptides.
Milk is a complex food containing different bioactive
molecular species. It is produced by the mammary glands to
nourish and protect the mammalian young. Milk contains
*Address correspondence to this author at the Department of Biochemistry,
School of Medicine, Marmara University, 34668, Haydarpasa-Istanbul,
Turkey; Tel: 90-216-4144733; Fax: 90-216-4181047;
essential nutrients as well as hormones, modulators and
growth factors that are capable of influencing the develop-
ment and growth of the gastrointestinal tract [9, 10]. Milk
influences other specific organs, modulates the gut micro-
flora population, provides immunological protection, im-
munoregulation and non-immune defence. Factors such as
breeding conditions, seasonal differences and geographic
variations affect milk composition. Approximate composi-
tion of milk may be given as: 87 % water, 5 % sugar (mainly
lactose), 3.5 % fat and 3.5 % proteins (casein micelles and
soluble whey proteins) and 1 % salts (minerals). The nitro-
gen content of milk is distributed among caseins, whey pro-
teins and non-protein compounds.
Caseins represent around 80 % of milk proteins. The
principal casein fractions are α-s1- and α-s2-caseins, β-
casein and κ-casein. All are conjugated proteins, most with
phosphate groups esterified to serine residues. Phosphate
groups are important for the structure of the casein micelle.
The distinguishing property of caseins is their low solubility
at pH 4.6. The high number of proline residues causes par-
ticular bending of the protein chain and inhibits the forma-
tion of close-packed, ordered secondary structures. Most of
the casein proteins exist in colloidal particles known as the
casein micelle. Casein micelles carry large amounts of highly
insoluble CaP and form a clot in the stomach for more effi-
cient nutrition [2]. Caseins do not contain disulfide bonds.
Although the casein micelle is fairly stable, there are differ-
ent ways by which its aggregation may be induced. Chy-
mosin or rennet is most often used for enzymatic coagulation
of casein micelles. Different forms of caseins have distin-
guishing features, for example κ-casein is very resistant to
calcium precipitation and stabilizes other caseins. Rennet
cleavage eliminates the stabilizing ability of κ-casein by
forming hydrophobic (para-κ-casein) and hydrophilic (κ-
casein glycomacropeptide or caseinomacropeptide) portions.
1638 Current Pharmaceutical Design, 2006, Vol. 12, No. 13 A. Süha Yalçın
Proteins appearing in the supernatant of milk after pre-
cipitation of casein are called whey proteins. These globular
proteins are more water soluble than caseins and are subject
to heat denaturation [9, 10].
Whey proteins are grouped as major and minor protein
fractions each with different molecular weights and critical
for healthy metabolism (Table 2). The major whey proteins
are β-lactoglobulin, α-lactalbumin, serum albumin, immu-
noglobulins and glycomacropeptide, while minor proteins
include lactoperoxidase, lactoferrin, β-microglobulin,
lysozyme, insulin-like growth factor (IGF), γ-globulins and
several other small proteins [10-12].
ß-Lactoglobulin is a major whey protein that corresponds
to approximately half of the total whey proteins in bovine
milk. It is a noncovalently linked dimer that has two internal
disulfide bonds and one free thiol group. It binds calcium
and zinc and has partial sequence homology to retinol bind-
ing proteins. ß-Lactoglobulin has numerous binding sites for
minerals, fat-soluble vitamins and lipids.
α-Lactalbumin is another major whey protein that makes
up 25 % of total bovine whey protein. It is a calcium binding
protein that enhances calcium absorption and is a rich source
of lysine, leucine, threonine, tryptophan and cystine. α-
Lactalbumin is specifically produced during lactation in the
mammary epithelial cells and plays an essential role in milk
synthesis. It is one of the few proteins that remains intact
upon pasteurization.
Serum albumin and immunoglobulins are blood proteins
that become incorporated into milk and are recoverable as
whey proteins. Serum albumin binds fatty acids as well as
other small molecules. Immunoglobulins include IgG1,
IgG2, IgA and IgM. Bovine immunoglobulins have been put
forward as possible effective means of preventing and com-
batting bacteria.
Glycomacropeptide, the glycosylated portion of caseino-
macropeptide, is present in sweet whey formed after cleav-
age of κ-casein by rennin [13, 14]. This protein is absent
from acid whey that is formed when caseins are precipitated
by lowering the pH to 4.6. Glycomacropeptide is a powerful
stimulator of cholecystokinin which is an appetite suppress-
ing hormone that has essential roles relating to gastrointesti-
nal function. In addition to being a regulator of food intake,
cholecystokinin stimulates gallbladder contraction and bowel
motility, regulates gastric emptying and stimulates the re-
lease of enzymes from the pancreas. Glycomacropeptide
alters pigment production in melanocytes, may act as a pre-
biotic and has immunomodulatory action [14].
Table 1. Typical Composition of Whey Products and their Functional Properties
Product Typical Composition Functional Properties
Sweet whey powder Protein: 11.0 % - 14.5 %
Lactose: 63.0 % - 75.0
Fat: 1.0 % - 1.5 %
Ash: 8.2 % - 8.8 %
Moisture: 3.5 % - 5.0 %
Low protein source
Dairy flavor and solids
Acid whey powder Protein: 11.0 % - 13.5 %
Lactose: 61.0 % - 70.0
Fat: 0.5 % - 1.5 %
Ash: 9.8 % - 12.3 %
Moisture: 3.5 % - 5.0 %
Low protein source
Dairy flavor and solids
Whey protein concentrate
(34 % protein)
Protein: 34.0 % - 36.0 %
Lactose: 48.0 % - 52.0
Fat: 3.0 % - 4.5 %
Ash: 6.5 % - 8.0 %
Moisture: 3.0 % - 4.5 %
Protein source
Mild dairy flavor
Color and flavor development
Whey protein concentrate
(80 % protein)
Protein: 80.0 % - 82.0 %
Lactose: 4.0 % - 8.0
Fat: 4.0 % - 8.0 %
Ash: 3.0 % - 4.0 %
Moisture: 3.5 % - 4.5 %
High protein source
Fat binding
Heat setting/gelling
Water binding
Whey protein isolate Protein: 90.0 % - 92.0 %
Lactose: 0.5 % - 1.0
Fat: 0.5 % - 1.0 %
Ash: 2.0 % - 3.0 %
Moisture: 4.5 %
High protein source
Adapted from [1].
Emerging Therapeutic Potential of Whey Proteins and Peptides Current Pharmaceutical Design, 2006, Vol. 12, No. 13 1639
Lactoperoxidase and lactoferrin are minor whey proteins.
The lactoperoxidase system inactivates a broad spectrum of
microorganisms through an enzymatic reaction [15]. The
reaction involves hydrogen peroxide and thiocyanate which
together with the enzyme constitute the lactoperoxidase sys-
tem. The lactoperoxidase system is a major part of the anti-
bacterial activity of milk. Lactoferrin is a member of the
transferrin gene family with metal binding properties [16,
17]. It is a 78 kDa glycoprotein made up of a single poly-
peptide chain and is linked to two glycans by N-glycosidic
linkages. Metals that are bound by lactoferrin are mainly
and Fe
, but Cu
, Zn
, Mn
are bound as well. Lac-
toferrin is important for the delivery of essential metals to
the newborn and is considered to be an important component
of the non-specific immune system. Lactoferrin plays a stra-
tegic role in the first line of defense against many pathogens
that tend to enter the body via mucosa. It is present in several
mucosal secretions such as tears, saliva, seminal and vaginal
Whey proteins of special therapeutic importance are α-
lactalbumin, β-lactoglobulin, bovine serum albumin, immu-
noglobulins, lactoferrin and lactoperoxidase. These proteins
exhibit different biological activities and are used as ingredi-
ents in different forms of pharmaceuticals, nutraceuticals and
cosmeceuticals [5-7, 12]. Additionally, specific digestion
products of milk proteins identified as bioactive peptides
have diverse biological activities [18-20]. The bioactive
peptide sequences are in an inactive state inside the polypep-
tide chain of the intact whey protein. Peptides released dur-
ing intestinal digestion of whey proteins may be involved in
the regulation of nutrient entry as well as postprandial me-
tabolism via stimulation of hormone secretion. Therapeutic
benefits of whey proteins can also result from bioactive pep-
tide production during fermentation [20]. Infant formula de-
velopment has been a long lasting effort to create a substitute
for mother’s milk. It is aimed to approach the nutrient com-
position of human breast milk using bovine milk as raw ma-
terial. However, the protein composition of human milk dif-
fers both quantitatively and qualitatively from that of bovine
milk [21]. The use of individual whey proteins particularly
α-lactalbumin to enrich infant formulas has significantly
increased after large-scale fractionation procedures utilizing
membrane filtration and ion-exchange techniques became
available [22].
Table 2. Concentration and Biological Activities of Milk Proteins
Protein Concentration (g/L) Biological Activity
Caseins 28
Transport of ions (Ca, PO
, Fe, Zn, Cu)
Precursor of bioactive peptides
β-lactoglobulin 1.3
Retinol carrier
Binding of fatty acids
α-lactalbumin 1.2
Lactose synthesis
Ca carrier
Immunoglobulins 0.7 Immune protection
Glycomacropeptide 1.2
Bifidobacteria growth
Lactoferrin 0.1
Antimicrobial, wound healing
Fe absorption
Lactoperoxidase 0.03 Antimicrobial, wound healing
Lysozyme 0.0004
Antimicrobial, wound healing
Synergistic effect with lactoferrin
Synergistic effect with immunoglobulins
Adapted from [11].
1640 Current Pharmaceutical Design, 2006, Vol. 12, No. 13 A. Süha Yalçın
Immune Function
The human immune system has a central role in the de-
fence against bacterial, viral, fungal and parasitic infections
as well as different forms of cancers [23]. Deficiencies in
any aspect of the immune system can predispose an individ-
ual to a greater risk of infection and may enhance severity of
a disease. The immune system employs both specific and
nonspecific immune responses for protection against disease.
Specific immune responses are mediated by T-lymphocytes
and antibodies produced by B-lymphocytes. Non-specific
components of the host defense include physicochemical
barriers such as skin, mucus, lysozyme, complement and
interferons, as well as natural killer cells and phagocytic
Milk contains unique constituents which have been
shown to modulate immune function [24, 25]. Among these
are immunoglobulins, lactoferrin, growth factors and amino
acids necessary to support glutathione production. Pluripo-
tent polypeptides called cytokines that have autocrine and/or
paracrine actions are also present in milk. An active area of
research is the formation of biologically active peptide se-
quences during digestion and their effects on secretion of
enterohormones as well as immune enhancement [26].
Passive immunity against infection in the intestinal lu-
men is afforded by lysozyme, lactoperoxidase, lactoferrin,
and caseinomacropeptides all of which are constituents of
whey that could also reduce oxidant burdens imposed by
inflammation [27]. Immunoglobulins are also involved in the
passive protection of the young and they partly resist degra-
dation in the intestinal lumen [28]. Studies have also been
performed using immunoglobulins from non-immunized
cows and from cows hyperimmunized against specific
pathogens [29-32]. Colostrum, which is the first milk pro-
duced after birth, is particularly rich in immunoglobulins,
antimicrobial peptides, growth factors as well as other bio-
active molecules [33]. Immunoglobulin concentrations are
greater in whey derived from colostrum. The high immuno-
globulin concentration of colostrum declines during lacta-
Whey products provide active lactoferrin/metal-binding
activities. Lactoferrin acts as a means of both stable iron
delivery and scavenging of free iron by binding iron which
would otherwise catalyze oxidative reactions [34]. Lactofer-
rin has bacteriostatic and bacteriocidal activity against both
Gram-negative and Gram-positive bacteria [35]. Binding to
lipopolysaccharides of Gram-negative bacteria is one of the
antibacterial mode of action of lactoferrin. Fungicidal activ-
ity particularly against Candida species has also been de-
scribed [36]. These activities are not only related to depriva-
tion of iron from the microenvironment but also to binding
of lactoferrin to cell walls causing membrane perturbation
and leakage of intracellular components. Besides a broad
antimicrobial spectrum against bacteria and fungi, lactoferrin
is capable of inhibiting replication of viruses [37]. Lactofer-
rin prevents infection of the host cell, rather than inhibiting
virus replication after the target cell has become infected.
The antiviral activity is in the early phase of the infection
where lactoferrin prevents entry of virus into the host cell,
either by blocking cellular receptors, or by direct binding to
the virus particles. Proteolysis of lactoferrin by pepsin pro-
duces an antimicrobial peptide called lactoferricin. Various
synthetic analogs of lactoferricin are also available. Lactofer-
ricin kills target organisms by membrane perturbation and
acts synergistically with some antimicrobial agents. It inhib-
its a diverse range of microorganisms such as Gram-negative
bacteria, Gram-positive bacteria, yeast, filamentous fungi,
and parasitic protozoa, including some antibiotic-resistant
pathogens [38].
Oxidative Stress and HIV Infection
A seemingly important feature of whey proteins is the
high concentration of cysteine which is a rate-limiting amino
acid in glutathione synthesis. Glutathione is a major nonpro-
tein sulfhydryl compound of the living cells. It is also a key
molecule for cellular protection against free radicals and
oxidative stress [39]. It has been reported that whey protein
feeding enhances immune responsiveness by increasing tis-
sue glutathione levels [40, 41]. Whey proteins are also good
candidates for dietary suppression of oxidative stress. They
have enhanced host antioxidant defenses and lowered oxi-
dant burden in different experimental models [42-45]. Anti-
oxidant status of the host organism is very important in viral
infections since virulence is linked to passage of non-virulent
forms through hosts with compromised antioxidant status.
HIV infection is characterized by increased oxidative stress
and a systemic deficiency of glutathione [46, 47]. HIV has a
dual response to glutathione. Low cellular glutathione levels
allow the virus to multiply, whereas high glutathione dra-
matically slows viral replication [48]. It was reported that
supplementation with whey proteins increased plasma glu-
tathione levels in glutathione-deficient patients with HIV-
infection [49-51].
Anticancer Activity
Nutritional studies, reports and trials to identify antican-
cer properties of foods have been extensive [52]. It is gener-
ally agreed that diets that are high in grains, green vegeta-
bles, fresh fruit and fiber, and low in total and saturated fats
are beneficial to health. Relatively less emphasis has been
placed on bovine milk. Epidemiological studies indicate that
humans who consume milk are less likely to develop cancer
of the colon and rectum than those who do not consume milk
[53]. Calcium and vitamin D were identified as protective
against colorectal cancer. The results of a recent study
showed that whey protein concentrate renders tumor cells
more vulnerable to chemotherapy by depleting glutathione
[54]. Whey proteins have also been reported to protect
against chemically induced carcinogenesis in animal models
[55, 56].
Stress, Depression and Anxiety
Stress is an important problem of the urban and industri-
alized society. People with increased brain serotonin levels
are able to cope with stress conditions, while a decline in
serotonin activity is associated with depression and anxiety.
Elevated levels of serotonin in the body will result in the
relief of depression, as well as a substantial reduction of pain
sensitivity, anxiety and stress [57]. Recently, investigators
Emerging Therapeutic Potential of Whey Proteins and Peptides Current Pharmaceutical Design, 2006, Vol. 12, No. 13 1641
examined whether α-lactalbumin would increase plasma
tryptophan levels and reduce cortisol concentrations in sub-
jects considered to be vulnerable to stress [58]. They sug-
gested that whey proteins may serve as safe and effective
supplements in the battle against depression and stress.
Oral Health
Adequate flow of saliva is a prerequisite for good oral
health. Hyposalivation leads to many oral problems includ-
ing rapid dental decay, mucosal infections and increased
susceptibility to fungal infections [59]. There have been at-
tempts to enhance or restore salivary antimicrobial capacity
using commercially available oral health care products. The
antimicrobial proteins used in these products are lysozyme,
lactoferrin and lactoperoxidase all of which are present in
whey [60]. On the other hand, demineralization of tooth
enamel, which consists mainly of crystalline calcium phos-
phate embedded in a protein matrix, is initially brought about
by the action of acids which create small cavities. Tooth de-
cay takes place by the action of microflora present in the
plaque. It has been shown that whey proteins exhibit protec-
tive effect against demineralization and act as anticariogenic
agents [61].
Gastrointestinal Health
Whey contains biologically active molecules capable of
enhancing intestinal health. There are four beneficial areas of
intestinal health modification with whey components: prebi-
otic effects, antimicrobial and antiviral properties, anticancer
properties and influences on immunity [62]. A prebiotic is a
nondigestible food ingredient that beneficially affects the
host by selectively stimulating the growth and/or activity of
one or a limited number of bacteria in the colon. Bifidobacte-
ria and lactobacilli are two groups of bacteria capable of
utilizing prebiotics [63]. They are considered to be beneficial
due to their antimicrobial effects against pathogenic bacteria,
production of B group vitamins, and inhibition of intestinal
precarcinogenic enzymes. Growth promotion of Bifidobacte-
rium species by different whey fractions have been reported
[64]. Glycomacropeptide and lactoferrin have been shown to
support the growth of Bifidobacteria and exhibit prebiotic
activity [65].
Antimicrobial and Bactericidal Activity
Whey contains several unique components with broad
antimicrobial and antibacterial properties. Significant levels
of these compounds have been shown to survive passage
through the stomach and small intestine, and arrive as intact
proteins in the large intestine where they exert their biologi-
cal effects. Immunoglobulins are the best-known of the whey
components that provide antimicrobial action in the intestinal
tract. They predominate in milk-derived sources and may
comprise up to 1 % of the total weight of whey proteins. IgG
has been shown to bind the toxin produced by Clostridium
difficile, thereby reducing the deleterious effects of infection
[66]. Glycomacropeptide also inhibits cholera toxin by
binding to receptors in the intestinal tract [14].
Antimicrobial peptides represent an important component
of the innate immunity. They can be generated through pro-
teolytic digestion of milk proteins and have the advantage of
being derived from harmless substances. A number of short
peptides with high bactericidal activity have been developed
from the bactericidal domains of α-lactalbumin and β-
lactoglobulin as well as lactoferrin [11, 67, 68].
Bioactive Peptides
The role of proteins in the diet as physiologically active
components has been increasingly acknowledged in recent
years [11, 12]. Accordingly, peptides from milk proteins
exhibiting different bioactivities, immunomodulatory action
and mineral utilization properties have been identified (Table
3). Bioactive peptides usually contain 3-20 amino acid resi-
dues per molecule. The biological activity is based on the
Table 3. Bioactive Peptides from Milk Proteins, their Precursors and Bioactivities
Bioactive Peptide Precursor Bioactivity
Casomorphins α- and β-Casein Opioid agonists
α-Lactorphin α-Lactalbumin Opioid agonist
β-Lactoglobulin β-Lactoglobulin Opioid agonist
Lactoferroxins Lactoferrin Opioid antagonists
Casoxins κ-Casein Opioid antagonists
Casokinins α- and β-Casein Antihypertensive
Lactokinins α-Lactalbumin and β-Lactoglobulin ACE-inhibitory
Casoplatelins κ-Casein and Transferrin Antithrombotic
Immunopeptides α- and β-Casein Immunostimulants
Phosphopeptides α- and β-Casein Mineral transport
Lactoferricin Lactoferrin Antimicrobial
Adapted from [11]
1642 Current Pharmaceutical Design, 2006, Vol. 12, No. 13 A. Süha Yalçın
inherent amino acid composition and sequence. Bioactivities
of several milk proteins are latent, either absent or incom-
plete in the native protein. The active peptide fractions are
released from the native protein/peptide during proteolytic
digestion of the protein. Once the bioactive peptides are lib-
erated, they may act as regulatory compounds with hormone-
like activity. There are a number of methods by which pep-
tides with biological activity can be produced. Pancreatic
enzymes have been utilized for the chemical characterization
and identification of many known bioactive peptides. ACE-
inhibitory peptides are most commonly produced by trypsin
but other enzymes and various combinations of proteinases
as well as enzymes from bacterial and fungal sources have
also been utilized to generate bioactive peptides [69].
The health promoting powers of whey was discovered
long time ago. Ancient Greeks as well as Hippocrates in 460
B.C., prescribed cheese whey for the assortment of human
ailments. Later in the 17th century during the Italian Renais-
sance sayings about whey flourished in Florence. The im-
portance of whey as a nutrient-rich protein source was rec-
ognized by the scientific community only recently. The
worldwide supply of whey as a co-product of cheese and
casein production has grown rapidly and along with ad-
vanced processing technologies this has expanded the com-
mercial use of whey proteins and their products. Today, it is
accepted that whey products offer a wide range of bioactive
elements capable of promoting health. Many in vitro and in
vivo studies have shown that individual whey proteins have
one or more biological activities.
Whey and its components are involved in different bio-
logical functions including antioxidant activity, anticarcino-
genic effects, immunomodulation, passive immunity, disease
protection, anti-bacterial, anti-microbial and anti-viral ef-
fects, binding of toxins, promotion of cell growth, platelet
binding, anti-inflammatory and anti-hypertensive actions. In
some cases the benefits of whey proteins and peptides have
been demonstrated by clinical trials on humans. In others
there are still gaps in scientific evidence. Nevertheless, the
attention devoted to whey proteins by the industry and the
scientific community strongly indicates that a dynamic
knowledge database will build upon current information and
expand the therapeutic use of whey proteins and peptides.
References 70-72 are related articles recently published in
Current Pharmaceutical Design.
[1] Reference Manual for US Whey and Lactose Products, U.S. Dairy
Export Council, 2001;
[2] Hoffman JR, Falvo MJ. Protein-which is best? J Sport Sci Med
2004; 3: 118-30.
[3] Boine Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beau-
frere B. Slow and fast dietary proteins differently modulate post-
prandial protein accretion. Procl Natl Acad Sci USA 1997; 94:
[4] Huffman L, Harper WJ. Maximizing the value of milk through
separation techniques. J Dairy Sci 1999; 82: 2238-44.
[5] Etzel MR. Manufacture and use of dairy protein fractions. J Nutr
2004; 134: 996-1002.
[6] Smithers GW, Ballard FJ, Copeland AD, De Silva KJ, Dionysius
DA, Francis GL, et al. New opportunities from the isolation and
utilization of whey proteins. J Dairy Sci 1996; 79: 1454-9.
[7] Horton BS. Commercial utilization of minor milk components in
the health and food industries. J Dairy Sci 1995; 78: 2584-9.
[8] Steijns JM. Milk ingredients as nutraceuticals. Int J Dairy Tech
2001; 54: 81-88.
[9] Jensen RG. Handbook of Milk Composition. Academic Press, San
Diego 1995.
[10] Fox PF, Flynn A. In: Fox PF Ed, Biological properties of milk
proteins. Advanced Dairy Chemistry. Elsevier, London 1992; Vol.
1: 255-84.
[11] Korhonen H, Pihlanto-Leppala A, Rantamaki P, Tupasela T. Im-
pact of processing on bioactive proteins and peptides. Trends Food
Sci Technol 1998; 9: 307-19.
[12] Pihlanto A, Korhonen H. In: Taylor SL Ed, Bioactive peptides and
proteins. Advances in Food and Nutrition Research, Elsevier, San
Diego 2003; 47: 175-276.
[13] Abd El Salam MH, El-Shibiny S, Buchheim W. Characteristics and
potential uses of the casein macropeptide. Int Dairy J 1996; 6: 327-
[14] Brody EP. Biological activities of bovine glycomacropeptide. Br J
Nutr 2000; 84: S39-49.
[15] Reiter B, Harnulv G. Lactoperoxidase antibacterial system: natural
occurence, biological functions and practical applications. J Food
Prot 1984; 47: 724-32.
[16] Lonnerdal B, Iyer S. Lactoferrin: molecular structure and biological
function. Ann Rev Nutr 1995; 15: 93-110.
[17] Levay PF, Viljoen M. Lactoferrin: a general review. Haema-
tologica 1995; 80: 252-67.
[18] Meisel H. Bioactive peptides from milk proteins: a perspective for
consumers and producers. Aust J Dairy Tech 2001; 56: 83-92.
[19] Clare DA, Swaisgood HE. Bioactive milk peptides: a prospectus. J
Dairy Sci 2000; 83: 1187-95.
[20] Korhonen H, Pihlanto A. Food-derived bioactive pep-
tides—opportunities for designing future foods. Curr Pharm Des
2003; 9: 1297-308.
[21] Jenness R. In: Fox PF Ed, Interspecies comparison of milk pro-
teins. Developments in Dairy Chemistry. Appl Sci Pub, New York,
1982; 87-114.
[22] Jost R, Maire J-C, Maynard F, Secretin M-C. Aspects of whey
protein usage in infant nutrition, a brief review. Int J Food Sci
Technol 1999; 34: 533-42.
[23] Roitt I, Brostoff J, Male D. Immunology. Churchill Livingstone,
London 1985.
[24] Cross ML, Gill HS. Immunomodulatory properties of milk. Br J
Nutr 2000; 84: 81-9.
[25] Gill HS, Doull F, Cross ML. Immunoregulatory peptides in milk.
Br J Nutr 2000; 84: 111-7.
[26] Kilara A, Panyam D. Peptides from milk proteins and their proper-
ties. Crit Rev Food Sci Nutr 2003; 43: 607-33.
[27] Björck L, Hopkin E. Significance of the indigenous antimicrobial
agents of milk to the dairy industry. Bull Int Dairy Fed 1991; 246:
[28] Roos N, Mahe S, Benamouzig R, Sick H, Rauterau J, Tome D.
labeled immunoglobulins from bovine colostrum are partially re-
sistant to digestion in human intestine. J Nutr 1995; 125: 1238-44.
[29] Reiter B. Protective proteins in milk- biological significance and
exploitation. Bull Int Dairy Fed 1985; 191: 1-35.
[30] Goldman AS. Immunologic supplementation of cow’s milk for-
mulations. Bull Int Dairy Fed 1989; 244: 38-43.
[31] Weiner C, Pan Q, Hurtig M, Boren T, Bostwick E, Hammarström
L. Passive immunity against human pathogens using bovine anti-
bodies. Clin Exp Immunol 1999; 116: 193-205.
[32] Korhonen H, Marnila P, Gill S. Bovine milk antibodies for health.
Br J Nutr 2000; 84(Suppl 1): S135-S146.
[33] Uruakpa FO, Ismond MAH, Akobundu ENT. Colostrum and its
benefits: a review. Nutr Res 2002; 22: 755-67.
[34] Halliwell B, Gutteridge JMC. Free Radicals in Biology and Medi-
cine. 2
Ed, Clarendon Press, Oxford 1989.
[35] Arnold RR, Cole MF, McGhee JR. A bactericidal effect for human
lactoferrin. Science 1977; 197: 263-5.
[36] Kuipers ME, de Vries-Hospers HG, Eikelboom MC, Meijer DKF,
Swart PJ. Synergistic fungistatic effects of lactoferrin in combina-
tion with antifungal drugs against clinical Candida isolates. An-
timicr Agent Chemother 1999; 43: 2635-41.
Emerging Therapeutic Potential of Whey Proteins and Peptides Current Pharmaceutical Design, 2006, Vol. 12, No. 13 1643
[37] Van der Strate BWA, Beljaars L, Molema G, Harmsen MC, Meijer
DKF. Antiviral activities of lactoferrin. Antiviral Res 2001; 52:
[38] Wakayabashi H, Takase M, Tomita M. Lactoferricin derived from
milk protein lactoferrin. Curr Pharm Des 2003; 9: 1277-87.
[39] Meister A. Glutathione metabolism and its selective modification. J
Biol Chem 1988; 263: 17205-8.
[40] Bounous G, Letourneau L, Kongshavn PAL. Influence of dietary
protein type on the immune system of mice. J Nutr 1983; 113:
[41] Bounous G, Gold P. The biological activity of undenatured dietary
whey proteins: role of glutathione. Clin Invest Med 1991; 14: 296-
[42] Kent KD, Harper WJ, Bomser JA. Effect of whey protein isolate on
intracellular glutathione and oxidant-induced cell death in human
prostate epithelial cells. Toxicol In vitro 2003; 17: 27-33.
[43] Bouthegourd J-C J, Roseau SM, Makarios-Lanham L, Leruyet PM,
Tome DG, Even PC. A preexercise α-lactalbumin-enriched whey
protein meal preserves lipid oxidation and decreases adiposity in
rats. Am J Physiol Endocrinol Metab 2002; 46: E565-72.
[44] Zommara M, Tachibana N, Sakono M, Suzuki Y, Oda T, Hashiba
H, et al. Whey from cultured skim milk decreases serum choles-
terol and increases antioxidant enzymes in liver and red blood cells
in rats. Nutrition Res 1996; 16: 293-302.
[45] Veliogˇlu-Ögˇünç A, Manukyan M, Cingi A, Aktan AÖ, Yalçın AS.
The effect of dietary whey supplementation on wound healing,
Med J Kocatepe 2003; S: 51-54.
[46] Legrand-Poels S, Vaira D, Pincemail J, van de Vorst A, Piette J.
Activation of human immunodeficiency virus type 1 by oxidative
stress. AIDS Res Hum Retrovir 1990; 6: 1389-97.
[47] Buhl R, Jaffe HA, Holroyd KJ, Wells FB, Mastrangeli A, Saltini C,
et al. Systemic glutathione deficiency in symptom-free HIV sero-
positive individuals. Lancet 1989; 2: 1294-8.
[48] Staal FJ. Glutathione and HIV infection: reduced reduced, or in-
creased oxidized? Eur J Clin Invest 1998; 28: 194-6.
[49] Bounous G, Baruchel S, Falutz J, Gold P. Whey proteins as a food
supplement in HIV-seropositive individuals. Clin Invest Med 1993;
16: 204-9.
[50] Micke P, Beeh KM, Schlaak JF, Buhl R. Oral supplementation with
whey proteins increases plasma glutathione levels of HIV-infected
patients. Eur J Clin Invest 2001; 31: 171-8.
[51] Micke P, Beeh KM, Buhl R. Effects of long-term supplementation
with whey proteins on plasma glutathione levels of HIV-infected
patients. Eur J Nutr 2002; 41: 12-8.
[52] Food, Nutrition and Cancer: a global perspective. World Cancer
Research Fund and American Institute for Cancer Research 1997.
[53] Gill HS, Cross ML. Anticancer properties of bovine milk. Brit J
Nutr 2000; 84: S161-6.
[54] Tsai WY, Chang W-H, Chen C-H, Lu F-J. Enhancing effect of
patented whey protein isolate (Immunocal) on cytotoxicity of an
anticancer drug. Nutr Canc 2000; 30: 200-8.
[55] Bounous G, Batist G, Gold P. Whey proteins in cancer prevention.
Cancer Lett 1991; 57: 91-4.
[56] Bounous G. Whey protein concentrate (WPC) and glutathione
modulation in cancer treatment. Anticancer Res 2000; 20: 4785-92.
[57] Stanford SC. In: Stanford SC, Salmon P Eds, Monoamines in re-
sponse and adaptation to stress. Stress: from Synapse to Syndrome.
London, Academic Press 1993; 24-30.
[58] Markus CR, Olivier B, de Haan EHF. Whey protein rich in α-
lactalbumin increases the ratio of plasma tryptophan to the sum of
the other large neutral amino acids and improves cognitive per-
formance in stress-vulnerable subjects. Am J Clin Nutr 2002; 75:
[59] Nederfors T. Xerostomia and hyposalivation. Adv Dent Res 2000;
14: 48-56.
[60] Tenovuo J. Clinical applications of antimicrobial host proteins
lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy
and safety. Oral Dis 2002; 8: 23-9.
[61] Warner EA, Kanekanian AD, Andrews AT. Bioactivity of milk
proteins: 1. Anticariogenicity of whey proteins. Int J Dairy Technol
2001; 54: 151-3.
[62] Causey J, Thomson K. The whey to intestinal health. Today’s
Dietitian 2003; July: 22-25.
[63] Gibson GR, Roberfroid MB. Dietary modulation of the human
colonic microflora: introducing the concept of prebiotics. J Nutr
1995; 125: 1401-12.
[64] Petschow BW, Talbott RD. Growth promotion of Bifidobacterium
species by whey and casein fractions from human and bovine milk.
J Clin Microbiol 1990; 28: 287-92.
[65] Harper WJ. Biological properties of whey components: a review.
The American Dairy Products Institute, Chicago, 2000.
[66] Warny M, Fatima A, Bostwick EF, et al. Bovine immunoglobulin
concentrate –Clostridium difficile retains C. difficile toxin neutral-
izing activity after passage through the human stomach and small
intestine. Gut 1999; 44: 212-7.
[67] Kilara A, Panyam D. Peptides from milk proteins and their proper-
ties. Crit Rev Food Sci Nutr 2003; 43: 607-33.
[68] Dionysius DA, Milne JM. Antibacterial peptides of bovine lactofer-
rin: purification and characterization. J Dairy Sci 1997; 80: 667-74.
[69] Pihlanto-Leppala A. Bioactive peptides from bovine whey proteins:
opioid and ACE-inhibitory peptides. Trends Food Sci Technol
2000; 11: 347-56.
[70] Florisa R, Recio I, Berkhout B, Visser S. Antibacterial and antiviral
effects of milk proteins and derivatives thereof. Curr Pharm Des
2003; 9(16): 1257-75.
[71] Kitts DD, Weiler K. Bioactive proteins and peptides from food
sources. Applications of bioprocesses used in isolation and recov-
ery. Curr Pharm Des 2003; 9(16): 1309-23.
[72] Korhonen H, Pihlanto A. Food-derived bioactive peptides--
opportunities for designing future foods. Curr Pharm Des 2003;
9(16): 1297-308.
... On the contrary, after casein precipitation, whey proteins are the proteins that are still soluble and consist of nearly 50% β-lactoglobulin, 20% α-lactalbumin (αlac), 10% albumin, and remaining contains lactoferrin with lactoperoxidase [6]. These globular proteins are susceptible to heat denaturation and are more water soluble than caseins [7]. Casein is referred to as a "slow" protein and whey protein as a "fast" protein because casein is digested in the stomach more gradually than whey proteins. ...
... A healthy metabolism depends on whey proteins, which are divided into major and minor protein fractions with varying molecular weights. Major whey proteins include β-lactoglobulin, α-lactalbumin, serum albumin, immunoglobulins, and glycomacropeptide, while minor proteins include lactoperoxidase, lactoferrin, βmicroglobulin, lysozyme, insulin-like growth factor (IGF), γ-globulins and a number of other tiny proteins [7]. There are various components of whey protein which include, β-Lactoglobulin, α-Lactoalbumin, Bovine serum albumin, Properties [5] The functional properties of the proteins in whey are shown in Table II. ...
... Supplementation of whey protein has proven to be highly beneficial [1]. Whey contains biologically active molecules capable of enhancing intestinal health [7]. The best-known benefits of whey protein include its capacity to aid in weight loss, raise lean muscle mass, and improve immunity [2,15]. ...
Full-text available
The popularity of whey protein among athletes and the bodybuilding community has grown significantly. Whey is a by-product of the dairy industry's process for manufacturing cheese. It constitutes only 20% of milk. It contains minerals, water, lactose, protein, and fat. Whey protein is a potent source of many benefits. Its antibacterial, antitoxin, and immunomodulating properties aid in the treatment of many ailments. It also plays an important role in the healing of burns and wounds. It has antioxidant qualities that aid in the battle against HIV. Whey protein promotes muscle growth and strong bones, in addition to improved athletic performance in athletes and bodybuilders. It aids in preventing cancer, cardiovascular diseases, obesity, and type 2 diabetes. Whey protein is a necessary supplement for those who engage in physical activity, like sports and exercise. It also benefits sedentary adults, newborns, expectant moms, and elderly people. However, in spite of its numerous benefits, there are many myths that surround whey proteins and therefore, are considered only for athletes and gym-goers. The present review attempts to cover an overview of whey protein, its components, types, and benefits. It also aims to dispel different fallacies about whey protein by presenting evidence from scientific studies.
... Furthermore, whey protein may undergo proteolysis during gastrointestinal transit to produce antimicrobial peptides. The inhibitory action of LF, -LA, and -LG against type 1 human immunodeficiency virus has been evaluated (HIV-1) (Yalcin, 2006;Chatterton et al., 2006). Due to nausea and appetite loss, cancer patients receiving radiation or chemotherapy often struggle to satisfy their daily nutritional needs. ...
Whey is produced in huge quantities by the dairy industry as a byproduct, and as non-food leads to serious environmental issues due to its high organic matter content. There has been a lot of research done over the last several decades how to use whey in a more sustainable and cost-effective way. The creation of value-adding goods including whey powders, functional meals, edible films and coatings, lactic acid, alcoholic beverages, sports drinks, and other biochemical, bioplastics, and biofuels is the core objective of sustainable whey management. In recent years, researchers have looked at different ways to use whey in a more affordable and ecologically friendly way, with the main goal of turning undesirable end products into useful materials. It is a source of several bioactive ingredients with various physiological and functional characteristics. It also provides an opportunity to food industries to develop functional foods with potential health benefits. Whey’s active components are advantageous because they offer antibacterial and antiviral activities, boost antioxidant activity, support bone and immune system health, improve athletic performance, and prevent cancer and cardiovascular disease. This chapter describes how to use whey and its components sustainably while using integrated processes and refining techniques to create high-value whey-based products. This is done in accordance with many international initiatives for improved planetary health, such as the EU Green Deal and the Sustainable Development Goals (UN, General Assembly. Transforming our world: The 2030 agenda for sustainable development. 2015).
... 4,18 Available prescription and non-prescription treatment modalities cover a wide variety of products that demonstrates the prevalence of the condition and difficulties associated with treating this behavior. 4,14,[19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35] Prescription medications to treat CTA fall into 3 main classes: benzodiazepines (BZDs), tricyclic antidepressants (TCAs) and selective serotonin reuptake inhibitors (SSRIs). 4 One of the most recommended conventional treatments of CTA is alprazolam given 30 minutes to 2 hours before a storm and every 4-6 hours during a storm. ...
Canine thunderstorm aversion (CTA) is a significant challenge to pets, owners, and veterinarians. The objective of this research was to determine if traditional Chinese veterinary medicine (TCVM) treatment with acupuncture, Chinese herbal medicine, basic desensitization and counterconditioning (DSCC) with a behavior modification drug, could lessen the severity of CTA in dogs. A total of 23 dogs that exhibited behaviors typical of thunderstorm aversion were enrolled in the study. At study start, all dogs received a TCVM Pattern diagnosis and were treated with Pattern-specific Chinese herbal medicine and acupuncture points. In addition, owners received DSCC behavior modification protocols and a conventional drug (alprazolam) to be used as needed during thunderstorms. Dogs were examined once a month for 4 months and Chinese herbal medicine formulations and acupuncture treatment adjusted as TCVM Patterns changed. After 120 days of treatment, the mean±SD improvement in overall thunderstorm aversion behaviors in study participants was 77.2%±27.7% (p < 0.0001). This result was significantly greater than 52% (p = 0.002), a reported mean improvement percentage for conventional treatment only, after 4 months. Six of the 7 individual aversion behaviors (panting, pacing, trembling, hiding, excess salivation, excess vocalization) had a significant reduction (range: p =0.046 to p = 0.008) over the course of treatment. The study results demonstrated that integrative management of CTA with TCVM Pattern-specific treatments combined with a conventional rescue drug and behavior modification improves CTA behaviors and suggests greater efficacy than conventional medical management only. Randomized controlled trials are warranted to validate these preliminary findings.
... Among minor proteins are lactoperoxidase, lactoferrin, insulinlike growth factor and γ-globulins [3,4]. Whey proteins are important in terms of both their biological value and their high content of sulfur-containing amino acids [5,6]. The human α-La and oleic acid (OA) complex called human alpha-lactalbumin made lethal to tumor cells (HAMLET) exhibits remarkable apoptotic activity [7][8][9]. ...
Full-text available
Objective: This study aimed to obtain protein derivatives after treatment of whey proteins with hazelnut oil and olive oil and determined their effects on MCF-7 cells. Materials and Methods: Whey proteins obtained from 6% whey powder were treated with hazelnut oil (HO) and olive oil (OO) at a protein to lipid ratio of 1:10 at 60 ̊C for 120 minutes. The protein derivatives formed with whey protein and HO or OO were applied to MCF-7 cancer cells and healthy fibroblasts. The effects of protein derivatives on cell viability, apoptosis, reactive oxygen species (ROS) production, wound healing, cell cycle phase distribution and cell cycle related proteins Akt and p21(Waf1/Cip1) expressions were investigated. Results: Cell viability decreased significantly after 24 h of incubation with WP:OO. The percentage of apoptotic or necrotic cells varied between 5-10% and no statistically significant effect was observed. There was no statistically significant difference in ROS production and colony formation between controls and WP:HO or WP:OO groups. Treatment of cells with WP:OO for 24 h significantly decreased cell migration compared to the control group. G2/M phase was significantly suppressed in WP:OO group compared to the control group. WP:OO also increased the expression of p21(Waf1/Cip1) significantly when compared with the control group. Conclusion: Our results showed that whey protein derivatives applied to MCF-7 cells are cytotoxic and may be useful in breast cancer treatment.
... It also has antibacterial properties in the upper respiratory system, and protects the mucosa of the stomach (Gupta and Prakash 2017). ALA is one of the few proteins that survives pasteurization as it is relatively heat-stable (Yalçın 2006). It is also required for the production of lactose, which is a vital source of energy for newborns (Kassem 2015). ...
Cancer prevalence is rising rapidly around the globe, contributing immensely to the burden on health systems, hence the search for more effective and selective treatments still remains enticing. Whey, as a natural source, has received extensive focus in recent years because of its intriguing applications to health benefits. Growing consumer appreciation of the nutraceutical effects of whey components makes them an attractive field within cancer research. Whey is a valuable source of superior-quality proteins, lactose, vitamins, and minerals that contribute to proper nutrition as well as help hamper illness and even complement certain disease-related therapy prognosis. As a result, industry leaders and dairy producers are devising new ways to valorize it. Great emphasis on cancer prevention and treatment has been given to whey protein (WP) by the scientific community. WP intake has been proven to induce anti-cancer effects in various in vitro and in vivo studies. Nutritionists and dietitians are now enormously endorsing the role of WP in the therapeutic field, notably for cancer cachexia management. However, human intervention studies with WP are in their infancy and remain to be established with different tumor entities to provide valid proof of its ability to act as a coadjuvant in cancer treatment.
... Whey proteins are exceptional, as they include all the important amino acids. The biological characteristics of milk whey and whey proteins are distinct (Yalcin, 2006) depending on their amino acid residues in peptides. Whey protein remains a soluble protein at 4.6 pH after casein precipitation and it comprises β-lactoglobulin (β-la), α-lactalbumin (α-la), bovine serum albumin (BSA), immunoglobulin (Ig), as well as lactoferrin (LF) (Morr & Ha, 1993). ...
Whey protein concentrate-80 (WPC-80) fermented with L. fermentum (KGL4) (37 °C) and S. cerevisiae (WBS2A) (25 °C) was tested for ACE-inhibitory and antioxidant activities over different periods (12, 24, 36 and 48 h). Proteolytic activity (OPA method) was used to optimize the growth conditions (inoculation rate, i.e. at 1.5%, 2.0%, and 2.5% and incubation time, i.e. 12, 24, 36, and 48 h) for peptide production. Results indicated that the highest amount of peptides was obtained at 7.24 mg/mL for KGL4 (37 °C, 48 h) and 8.59 mg/mL for WBS2A (25 °C, 48 h). The whey protein fermentate inhibited the LPS-induced NO production, while enhanced production concentrations of TNF-α, IL-6, and IL-1β. Subsequently, SDS-PAGE, as well as Two-Dimensional (2D) gel electrophoresis methods, were applied for protein purification using water-soluble extracts (WSEs) of WPC-80 fermented by a combination of L. fermentum and S. cerevisiae. On SDS-PAGE, protein bands were observed in the range of 10–55 kDa, whereas on the 2D page, protein spots were in the range of 10–70 kDa. All the 2D spots were analyzed using RPLC/MS. WSEs of 3 kDa and 10 kDa permeates were used in RP-HPLC to identify distinct peptide fractions. The data from LC/MS was also characterized by utilizing ProteinPilot software. Further, different functional groups were also analyzed using FTIR investigation. The research aims to isolate and characterize novel ACE-inhibitory and antioxidative peptides from fermented WPC-80 produced by Lactobacillus fermentum and S. cerevisiae.
Grape marc (GM) is an agri‐food residue from the wine industry valuable for its high content of phenolic compounds. This study aimed to develop an encapsulation system for GM extract (GME) using food‐grade biopolymers resistant to gastric conditions for its potential use as a nutraceutical. For this purpose, a hydroalcoholic GME was prepared with a total phenolics content of 219.62 ± 11.50 mg gallic acid equivalents (GAE)/g dry extract and 1389.71 ± 97.33 µmol Trolox equivalents/g dry extract antioxidant capacity, assessed through ABTS (2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid) assay. Moreover, the extract effectively neutralized reactive oxygen species in Caco‐2 cells, demonstrating an intracellular antioxidant capacity comparable to Trolox. The GME was encapsulated using whey protein isolate and pectin through nano spray drying (73% yield), resulting in spherical microparticles with an average size of 1 ± 0.5 µm and a polydispersity of 0.717. The encapsulation system protected the microcapsules from simulated gastrointestinal digestion (GID), where at the end of the intestinal phase, 82% of the initial phenolics were bioaccessible compared to 54% in the free GME. Besides, the encapsulated GME displayed a higher antioxidant activity by the ferric reducing antioxidant power assay than the free extract after GID. These results show the potential of this encapsulation system for applying GME as a nutraceutical with a high antioxidant capacity and protective effect against cellular oxidation.
This work was conducted to synthesize whey protein nanoparticles (WPNPs) for the coating of zinc citrate (Zn CITR) at three levels and to study their protective role against CCl4 -induced kidney damage and inflammatory gene expression disorder in rats. Seventy male Sprague-Dawley rats were divided into seven groups and treated orally for 4 weeks as follows; the control group, the group treated twice a week with CCl4 (5 mL/kg b.w), the groups received CCl4 plus WPNPs (300 mg/kg b.w); the group received 50 mg/kg b.w of Zn CITR or the three formulas of Zn CITR-WPNPs at low, medium and high doses (LD, MD, and HD). Blood and kidney samples were collected for different assays and histological analyses. The fabricated particles were semispherical, with an average size of 160 ± 2.7, 180 ± 3.1, and 200 ± 2.6 nm and ζ potential of -126, -93, and -84 mV for ZN CITR-WPNPs (LD), Zn CITR-WPNPs (MD), and ZN CITR-WPNPs (HD), respectively. CCl4 significantly increased (p ≤ 0.05) kidney function indices, oxidative stress markers, messenger RNA expression of transforming growth factor-β1, interleukin (IL)-1β, IL-10, IL-6, inducible nitric oxide synthase, and tumor necrosis factor-α and significantly decreased (p ≤ 0.05) renal superoxide dismutase, catalase, and glutathione peroxidase along with the histological changes in the kidney tissues. WPNPs, Zn CITR, and Zn CITR loaded WPNPS showed a protective effect against these complications and Zn CITR-WPNPs (LD) was more effective. WPNPs can be used effectively for coating Zn CITR at a level of 7 mg/g WPNPs to be used as a supplement for the protection of the kidney against different toxicants to enhance immunity and avoid harm of excess Zn.
The world's ever-increasing protein demand for food, feed and other applications require us to seek cheaper, renewable, sustainable proteins, and cereal crops such as millets are emerging as a potent protein source. Millets are group of tiny seeds obtained from annual plants that are widely cultivated in semi-arid and dry land regions of the world. These highly nutritious seeds are rich in protein content, fat and fiber. The main goal of this review is to discuss the distinctive advantageous properties of millet seed proteins and various potential fractionation methods available for extracting them. For instance, in addition to the conventional methods such as Osborne's classical scheme and Landry and Moureaux's scheme that are well adopted for sequential protein fractionation protocols, advanced green technologies such as ultrasonication, microwaves, hydrostatic pressure, etc. have been discussed in depth. We have also described several solvent-based extraction methods that have been established specifically for preparing concentrate from millet protein. The review paper also discusses the current status and potential applications of millet proteins in the food, pharma, nutritional supplement, and bio-based industries.
Full-text available
In recent years there has been a huge increase in consumer interest in products with the reduced fat content and the additional health-promoting properties. The interactions between the fiber and the ingredients of the cheese sauce have not yet been investigated and described. The aim of the research was examination of the effect of pumpkin and kale fibers on physicochemical properties and stability of the processed cheese sauces (PCS) obtained with the whey protein concentrate (WPC80), acid casein (AC) and different fat sources. In samples with the kale (KF) and rapeseed oil (RO) addition an increase in the value of characteristics such as hardness, adhesiveness, product stability (TSI) and surface roughness was observed. The results of measurements of storage (G′) and loss (G″) moduli showed the same upward trend with an increase in the amount of added kale fiber. They were related to the hardness and roughness parameters determined by measure of surface properties using the optical profilometer and the stability examined using Turbiscan. In the PCS with kale fiber addition based on RO an increase in stability (6.41–1.86 TSI) and roughness (2.2–16 qm) values along with the amount of fiber added was observed. Also optical microscopy images present the compacted structure of produced sauces. This article provides results and relevant literature, discussing the impact of different fibers and other ingredients on structure of PCS. In the future, these fibers may replace typical hydrocolloids used in processed cheese sauces production.
Full-text available
In the present review dealing with the antibacterial lactoperoxidase (LP) system, it is shown that the two reactants thiocyanate (SCN⁻) and hydrogen peroxide (H2O2) as well as the catalytic enzyme lactoperoxidase (LP) are widely distributed in nature and that evidence for the activity of the LP system in animals, including man, is accumulating. The in vitro effects on bacterial and animal cells are discussed and the unique action of the LP system on the bacterial cytoplasmic membrane is pointed out. Some practical applications are also presented, with particular emphses on the possibility of utilizing the LP system to preserve the quality of raw, cooled as well as uncooled milk. It is concluded that the addition of minute quantities of SCN⁻ and H2O2 (ca. 12 and 8 ppm, respectively) to secure an optimum activity of the LP system should be harmless to the consumer of milk and milk products treated in this way.
Full-text available
Protein intake that exceeds the recommended daily allowance is widely accepted for both endurance and power athletes. However, considering the variety of proteins that are available much less is known concerning the benefits of consuming one protein versus another. The purpose of this paper is to identify and analyze key factors in order to make responsible recommendations to both the general and athletic populations. Evaluation of a protein is fundamental in determining its appropriateness in the human diet. Proteins that are of inferior content and digestibility are important to recognize and restrict or limit in the diet. Similarly, such knowledge will provide an ability to identify proteins that provide the greatest benefit and should be consumed. The various techniques utilized to rate protein will be discussed. Traditionally, sources of dietary protein are seen as either being of animal or vegetable origin. Animal sources provide a complete source of protein (i.e. containing all essential amino acids), whereas vegetable sources generally lack one or more of the essential amino acids. Animal sources of dietary protein, despite providing a complete protein and numerous vitamins and minerals, have some health professionals concerned about the amount of saturated fat common in these foods compared to vegetable sources. The advent of processing techniques has shifted some of this attention and ignited the sports supplement marketplace with derivative products such as whey, casein and soy. Individually, these products vary in quality and applicability to certain populations. The benefits that these particular proteins possess are discussed. In addition, the impact that elevated protein consumption has on health and safety issues (i.e. bone health, renal function) are also reviewed.
Bioactivities of peptides encrypted in major milk proteins are latent until released and activated by enzymatic proteolysis, e.g. during gastrointestinal digestion or food processing. Activated peptides are potential modulators of various regulatory processes in the living system: Opioid peptides are opioid receptor ligands which can modulate absorption processes in the intestinal tract, angiotensin-l-converting enzyme (ACE)-inhibitory peptides exert an hypotensive effect, immunomodulatory casein peptides stimulate the activities of cells of the immune system, antimicrobial peptides kill sensitive micro-organisms, antithrombotic peptides inhibit aggregation of platelets, mineral binding peptides may function as carriers for different minerals, especially calcium, and several cytomodulatory peptides inhibit cancer cell growth. The multifunctionality of various peptides involves quite different bioactivities. Bioactive peptides can interact with target sites at the luminal side of the intestinal tract, or they could reach any potential site of action in the system to elicit physiological effects. Food-derived bioactive peptides are claimed to be health enhancing components for 'functional foods' that are used to reduce the risk of disease or to enhance a certain physiological function.
Colostrum, a nutrient-rich fluid produced by female mammals immediately after giving birth, is loaded with immune, growth and tissue repair factors. It is a complex biological fluid, which helps in the development of immunity in the newborn. It contains significant quantities of complement components that act as natural anti-microbial agents to actively stimulate the maturation of an infant’s immune system. Bovine colostrum, a raw material for immune milk preparations, can be used to treat or prevent infections of the gastrointestinal tract. It is possible that colostral preparations aimed at specific consumers may play a significant role in healthcare in the future. Besides providing immune support, colostrum has remarkable muscular-skeletal repair and growth capabilities. Studies have shown that colostrum is the only natural source of two major growth factors namely, transforming growth factors alpha and beta, and insulin-like growth factors 1 and 2. These growth factors have significant muscle and cartilage repair characteristics. They promote wound healing with practical implications for trauma and surgical patients. Colostral growth factors have multiple regenerative effects that extend to all structural body cells, such as the gut.
Keywords:Anticariogenicity;Caseinophosphopeptides;Dental caries;Hydroxyapatite;Whey fractions
Cow’s milk is considered as a basic food in many diets, and is rich in a variety of essential nutrients. With today’s sophisticated analytical, biochemical and cell-biological research tools, the presence of many other (minor) compounds with biological activity has been demonstrated. Achievements in separation techniques in the dairy industry and enzyme technology offer opportunities to isolate, concentrate or modify these compounds, so that their application in functional foods, dietary supplements, nutraceuticals and medical foods has become possible. Within the sequence of amino acids of a dietary protein, specific peptides may be located with specific biological activity. Peptides from casein may be used to enhance the solubility of minerals such as calcium and zinc—and hence increase the bioavailability of these minerals—or to reduce the activity of the angiotensin-converting enzyme, which is involved in vasoconstriction and (hence) blood pressure. Immunoglobulins from vaccinated cows may be considered as natural antimicrobials with certain advantages over synthetic antibiotics. Lactoferrin is an example of a minor milk protein that has been studied in great detail: it is becoming increasingly clear that it is important for the nonspecific defence against bacteria, fungi and viruses. Oligosaccharides, glycolipids and glycoproteins containing sialic acid residues may have a role as anti-infectives. Components such as growth factors may also be considered for future product development, because of the economies of scale used in the dairy industry.
Summary Demineralized whey, whey protein concentrates and, to a lesser extent, some other whey protein fractions are key raw materials in infant formula manufacture. An estimate of the amount of whey protein used in infant formulae annually is in the order of 30–40 000 tons. Infant formula development has been a long lasting effort to approach the nutrient composition of human breast milk while using cow's milk as the raw material. This required extensive fractionation of the bovine milk followed by subsequent recombination of specific fractions. Criteria to judge protein quality and define adequate protein quantity in infant formulae have also evolved. Early criteria for protein adequacy were based on Protein Efficiency Ratio (PER) testing in rats and/or nitrogen balance studies. More recently, the approach of essential amino acid scores, based on the amino acid pattern of mature human milk has been put forward. Regulatory authorities such as CODEX, EC Commission and more recently LSRO in its suggestions to FDA in the USA, have issued reference amino acid profiles which are based on the average amino acid composition of human milk. The same authorities have also regulated protein density in infant formulae, accounting for an observed protein mean density of 1.5–1.6 g /100 kcal in mature breast milk. The minimum protein level of cow's milk based infant formulae was fixed at 1.8 g/100 kcal by these authorities. Current infant formulae have however protein densities significantly higher than the minimum of 1.8 g/100 kcal. The higher protein density compensates for the likeliness that the protein in the best of the formulae, is not as ideal for the infant as the protein from breast milk. Even if a complete equivalence may be difficult to reach, efforts continue in the direction of further optimizing the protein quality in terms of essential and semi-essential amino acid profiles. This is the only way to be able to lower the protein content in a formula to levels that are nearer to the low protein density of human milk. Among several possibilities, the increase in the mass proportion of bovine α-lactalbumin is a particularly promising way to achieve this goal.