lioto|os aio |oooamoota| aoo |otogia| |ooo comoooots,

bot| ooti|t|ooa||y aoo |ooct|ooa||y. |oti|t|ooa||y, t|oy aio a

sooico o| oooigy aoo am|oo ac|os, w||c| aio ossoot|a| |oi
giowt| aoo ma|otooaoco. looct|ooa||y, t|oy a|oct t|o
|ys|coc|om|ca| aoo soosoiy iooit|os o| vai|oos ioto|-
oacooos |ooos. |o aoo|t|oo, maoy o|otaiy ioto|os ossoss
soc||c b|o|og|ca| iooit|os w||c| ma|o t|oso como-
ooots otoot|a| |ogioo|oots o| |ooct|ooa| oi |oa|t|-iomot-
|og |ooos. 1|oso ioto|os may a|so a|oct t|o toc|oo|og|ca|
|ooct|ooa||ty o| t|o |otooooo ooo-iooocts. Oo t|o ot|oi
|aoo, |t |s ossoot|a| to a|y oi oovo|o toc|oo|og|os w||c|
iota|o oi ovoo oo|aoco t|o act|v|ty o| b|oact|vo como-
ooots |o |ooo systoms. 1||s iov|ow ait|c|o |ocosos oo t|o
o|octs o| iocoss|og oo t|o iooit|os o| b|oact|vo ioto|os
ooi|voo |iom vai|oos sooicos. A soc|a| om|as|s |s g|voo to
m||| ioto|os as t|o|i |ys|o|og|ca| aoo toc|oo|og|ca| |ooc-
t|ooa||ty |as booo stoo|oo oxtoos|vo|y. # ! l|sov|oi
Sc|ooco lto. A|| i|g|ts iosoivoo
Technological processes used in food manufacture aect
the functional, nutritional and biological properties of
food proteins. On the other hand, proteins may be
added as functional ingredients to foods to emulsify,
bind water or fat, form foams or gels, and alter avor,
appearance, and texture [1]. In recent years, the role of
proteins in the diet as physiologically active components
has been increasingly acknowledged. Such proteins or
their precursors may occur naturally in raw food mate-
rials exerting their physiological action direct or upon
enzymatic hydrolysis in vitro or in vivo. For example, it
has become clear that dietary proteins are a source of
biologically active peptides. These peptides are inactive
within the sequence of parent protein and can be
released during gastrointestinal digestion or food pro-
cessing. Once bioactive peptides are liberated, they may
act as regulatory compounds with hormone-like activ-
ity. Milk proteins are the most important source of
bioactive peptides, though other animal as well as plant
proteins, especially soybean, also contain potential
bioactive sequences [2, 3]. In addition, it is well docu-
mented that a number of amino acids possess specic
physiological properties, both benecial and detrimental
e.g. they participate in many biochemical pathways and
are precursors of active metabolites. The amino acids
which are considered to be physiologically benecial
are, for example, arginine, glutamine, histidine, lysine,
taurine, tyrosine and tryptophan [2]. The best sources of
these amino acids are meat, eggs and dairy products.
On the other hand, a few amino acid derivatives, which
are formed during food processing, such as lysinoala-
nine, d-amino acids and biogenic amines, may cause
undesirable metabolic or even toxic events in the body
[4, 5]. Many dietary proteins may naturally pose as
potential allergens and protein-derived allergenic prop-
erties have been mentioned as possible side-eects of
genetically engineered foodstus [6]. In this respect,
development and application of novel processing and
isolation techniques which aim at minimizing such
health risks will play a crucial role.
Sources of bioactive proteins
\|||
Milk contains two major protein groups, caseins and
whey proteins, which dier greatly with regard to their
physicochemical and biological properties. Caseins,
024-2244''$soo |ioot mattoi Coyi|g|t # ! l|sov|oi Sc|ooco lto. A|| i|g|ts iosoivoo
PI I : S024- 2244 0004-
1iooos |o looo Sc|ooco 8 1oc|oo|ogy ! 0!
Impact of
processing on
bioactive proteins
and peptides
Hannu Korhonen*
Anne Pihlanto-Leppa la ,
Pirjo Rantama ki
and Tuomo Tupasela
Agricultural Research Centre of Finland, Food
Research Institute, 31600 Jokioinen, Finland
(tel.: 358-3-418-8271; fax: 358-3-418-8444;
e-mail: hannu.j.korhonen@mtt.)
Review
Coiiosooo|og aot|oi.
which account for 80% of the total protein in bovine
milk, exist primarily in large complexes termed micelles
[7]. The multiple functional properties of caseinate
derivatives allow them to be used in several food pro-
ducts, e.g. bakery and meat products, soups and toppings
[8, 9]. The caseins are known to exhibit biological
activity, such as carrying of calcium, zinc, copper, iron
and phosphate ions in the body (Table 1). Also, the
caseins act as precursors of a number of dierent
bioactive peptides [10].
The whey proteins, which account for 20% of total
milk protein, represent an excellent source of both
functional and nutritious proteins. The main whey pro-
tein constituents are -lactoglobulin and -lactalbumin,
two small globular proteins that account for some
7080% of total whey protein. Minor whey protein
components include the immunoglobulins (Igs), glyco-
macropeptide, serum albumin, lactoferrin, proteose-
peptones and numerous enzymes [11, 12]. The known
biological properties of these proteins are highlighted in
Table 1. The functional versatility of whey proteins is
well known and reviewed in many articles [1317].
Native -lactalbumin has good emulsifying properties,
but its gelation ability is poor. By contrast, native
-lactoglobulin has excellent gelling and foaming prop-
erties. Whey protein concentrates (WPC) and isolates
(WPI) are nowadays increasingly used by various
industries, though their physicochemical functionality is
quite limited [1820]. There seems to be considerable
scope for expanded utilization of specic whey-derived
proteins, not only in the food industry, but also in the
pharmaceutical, health-related and diagnostic industries
[21, 22].
As shown in Table 2, bioactive peptides are widely
distributed among milk proteins. Many studies have
shown in vitro formation of bioactive peptides from
milk proteins and in some studies in vivo formation has
also been found [3, 23]. In addition to liberation during
digestion in vivo, bioactive peptides may be liberated
during the manufacture of milk products. For example,
hydrolysed milk proteins used for hypoallergenic infant
formulas, clinical diets and as food ingredients, consist
exclusively of peptides. Proteolysis during milk fermen-
tation and cheese ripening leads to the formation of
various peptides. Indeed, casomorphins, ACE-inhibi-
tory peptides and phosphopeptides have been found in
fermented milk products [2426].
Co|ostiom
In bovine colostrum, the protein content is 34 times
higher (up to 150 g/l vs 3040 g/l) than in normal milk.
This is primarily attributed to a high concentration of
whey proteins. Among colostral whey proteins, the Igs
represent up to 75% of total protein in the rst milking
compared with 10% in normal milk [27, 28]. Ig
(immunoglobulin) enriched preparations have been
introduced to the market in many countries as calf milk
replacers [29]. It has been suggested that infant formulas
could be fortied with colostral Igs and lactoferrin (LF)
[30, 31]. Also, preparations containing specic colostral
Igs (antibodies) produced in colostrum by hyper-
immunization of pregnant cows may, in the future, nd
applications in the prevention and treatment of human
microbial diseases [21, 32]. A preventive or therapeutic
ecacy of such products has been demonstrated against
dierent gastrointestinal infections [33]. A few so-called
immune milk products are already on the market in the
USA and Australia. Since bovine colostrum also con-
tains other biologically active compounds such as
Table 1. Biological activity of major milk proteins
Protein Concentration
g/l
Function
Caso|os ; aoo 2 |oo caii|oi Ca, lO
4
, lo, 7o, Co, iocoisois o| b|oact|vo ot|oos
-|actog|obo||o !. kot|oo| caii|oi, |atty ac|os b|oo|og, oss|b|o aot|ox|oaot
-lacta|bom|o !.2 lactoso syot|os|s |o mammaiy g|aoo, Ca caii|oi, |mmooomooo|at|oo, aot|caic|oogoo|c
|mmooog|obo||os A, \ aoo C 0. |mmooo iotoct|oo
C|ycomacioot|oo !.2 Aot|v|ia|, b||oogoo|c
lacto|oii|o ll 0.! Aot|m|ciob|a|, aot|ox|oat|vo, |mmooomooo|at|oo, |ioo absoit|oo, aot|caic|oogoo|c
lactooiox|oaso 0.0 Aot|m|ciob|a|
lysozymo 0.0004 Aot|m|ciob|a|, syooig|st|c o|oct w|t| |mmooog|obo||os aoo ll
lata |iom |oi|oooo '2!
Table 2. Bioactive peptides derived from milk proteins
Bioactive peptides Protein precursor Bioactivity
Casomoi||os - aoo -Caso|o O|o|o agoo|sts
-lactoi||o -lacta|bom|o O|o|o agoo|st
-lactoi||o -lactog|obo||o O|o|o agoo|st
lacto|oiiox|os lacto|oii|o O|o|o aotagoo|sts
Casox|os -Caso|o O|o|o aotagoo|sts
Caso||o|os - aoo -Caso|o Aot||yoitoos|vo
Caso|ato||os -Caso|o, 1iaos|oii|o Aot|t|iombot|c
|mmoooot|oos - aoo -Caso|o |mmooost|mo|aots
l|os|oot|oos - aoo -Caso|o \|ooia| caii|ois
lacto|oii|c|o lacto|oii|o Aot|m|ciob|a|
lata |iom \o|so| aoo Sc|||mmo '.
0 H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319
growth-promoting factors and essential nutrients [12,
3436], research in this eld seems highly promising.
1iaosgoo|c m||| ioto|os
Transgenic animals have been employed as in vivo
experimental models for assessing the ability and
impact of foreign gene expression in a biological sys-
tem. Transgenic mice are most commonly used, while
transgenic sheep, goats, pigs and cows have also been
developed for specic, applied purposes. Transgenic
technology has been applied in these animals with the
purpose of altering the properties of milk by adding a
new protein or recovering the protein for other uses,
such as pharmaceuticals [37, 38]. Studies carried out in
transgenic mice suggest that human lysozyme and -
casein are good candidates for benecially altering
cheese manufacturing properties of milk [39]. Also, there
is a growing interest in employing genetic engineering
for production of human milk proteins, peptides,
growth factors and other bioactive substances [40, 41].
Human milk proteins that have been cloned from a
mammary gland library are -lactalbumin, lactoferrin,
lysozyme, collagen, -casein and -casein [40, 42].
Human lactoferrin [43] and human lysozyme [44] have
been expressed in transgenic mice or cattle with reason-
able expression in the milk but, so far, no in vivo studies
on the functional or physiological properties of such
milks have been reported. On the other hand, human
antithrombin III and 1-antitrypsin from the milk of
transgenic livestock are currently in clinical trials [45].
lgg
A hen's egg consists of 13% protein (shell, 3%; egg
white, 11% and yolk, 17%). Eggs are a rich source of
proteins with dierent physicochemical and biological
characteristics as shown in Table 3 [46]. Egg white pos-
sesses multiple functionalities such as gelation, emulsi-
cation, foaming, water binding and heat coagulation,
which makes it a highly desirable protein in many foods.
These properties of egg white can be attributed to com-
plex interactions among its protein constituents, namely
ovalbumin, conalbumin, lysozyme, ovomucin, globulins
and other minor proteins [47]. Whole egg or egg white
powders are commercially manufactured and used in
many food products and also non-food applications.
Among specic egg proteins, lysozyme can easily be
separated from egg white using crystallization or ion-
exchange resins. Puried lysozyme has shown promise as
a food preservative, e.g. in prevention of late fermentation
of hard cheese and in reduction of pathogenic bacteria
on meat surfaces [46]. Egg immunoglobulins (IgY) can
be enriched and isolated in a highly puried form using
a serial ltration system or ultracentrifugation com-
bined with a chromatographic purication process [48,
49]. IgYs have already found use in immunoassay tech-
niques and may, in the future, nd applications as
ingredients of functional foods and feeds aimed at pre-
venting or curing gastrointestinal infections [50].
Ot|oi sooicos
In addition to milk and egg, bioactive proteins are
found in many other biological materials. Among them,
there are animal proteins such as gelatin and sh muscle
proteins and also plant proteins such as corn -zein, rice
glutelin and prolamin, wheat gluten and soya protein
[51, 52]. The biological activity of most of these proteins
is attributed to specic peptide sequences, which are
freed by enzymatic hydrolysis. In the following, exam-
ples of such bioactive proteins are described. Oshima et
al. [53] isolated nine angiotensin-converting enzyme
(ACE)-inhibitory peptides from bacterial collagenase
digests of gelatin. Also, digestion with mammalian
trypsin and -chymotrypsin produced these peptides. In
the hydrolysates of sh meat obtained by pepsin, trypsin,
chymotrypsin, thermolysin or denazyme AP (a protease
from Aspergillus oryzae), potent ACE-inhibitory peptides
Table 3. Proteins in egg albumen
Protein Amount of
albumen
Isoelectric point Molecular
weight (Da)
Characteristics
Ova|bom|o 4 4. 4,000 l|os|og|ycoioto|o
Ovotiaos|oii|o
cooa|bom|o
!2 6.! 6,000 ||oos mota| |oos
Ovomoco|o !! 4.! 2,000 |o||b|ts tiys|o
Ovomoc|o . ..0 ..!0
6
S|a|oioto|o, v|scoos
lysozymo .4 !0. !4,00 lysos somo bactoi|a
C
2
-C|obo||o 4.0 . .04.!0
4

-C|obo||o 4.0 4.0

Ovo|o||b|toi !. .! 4,000 |o||b|ts soi|oo iotoasos
l|c|o cystat|o |o||b|toi 0.0 .! !2,00 |o||b|ts t||oiotoasos
Ovog|ycoioto|o !.0 . 24,400 S|a|oioto|o
Ovomaciog|obo||o 0. 4. .6.0!0

Stioog|y aot|goo|c
Av|o|o 0.0 !0 6,00 ||oos b|ot|o
lata |iom lioo|og '46
H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319 0
have been detected [51]. Among corn proteins, three
distinct zein classes are distinguished, ; - and -zein.
-zein is a major component of maize endosperm pro-
tein and consists of 7585% of the total zein. It contains
polypeptides of molecular weight of 21,00025,000 and
10,000 Da. When -zein was hydrolyzed with thermo-
lysin, ACE-inhibitory peptides were obtained [54]. In
rice proteins, antihypertensive activity has been demon-
strated in peptides originating from glutelin and prola-
min [55, 56]. Gliadin and glutenin are the main wheat
endosperm storage proteins and form 85% of the
wheat our protein content. When hydrated, gliadin
and glutenin form a colloidal complex known as wheat
gluten [57, 58]. Zioudrou et al. [59] discovered opioid
activity in hydrolysates of wheat gluten. Of all oilseeds,
soyabeans are commercially the most important source
of protein. The protein content (mainly glycinins) of
soyabeans is much higher than that of cereal grains. By
enzymatic hydrolysis of soya proteins, functional ingre-
dients suitable, for example, for whipping or foaming
have been developed [60, 61]. Soyabeans have been
shown to possess anti-carcinogenic properties [62] and
both animal and human studies have demonstrated that
a soya protein diet reduces high plasma cholesterol
levels [2]. The actual mechanism by which soya proteins
might lower blood lipid concentrations in humans
remains, however, to be elucidated.
Impact of processing on bioactive proteins
In the conventional industrial manufacture of various
foodstus, the proteins contained in raw materials are
readily subjected to alterations with regard to their
functional or biological properties. pH changes and
certain chemical treatments aect functional properties
by modifying specically one or more amino acids. For
example, acidic treatments destroy glutamine and
asparagine, whereas alkaline treatments destroy cystine,
serine and threonine, and produce lysinoalanine and d-
amino acids (Table 4) [1, 5]. Other chemical treatments,
such as acylation, glycosylation, phosphorylation,
reductive alkylation, succinylation or lipophilization
may improve functionality of the proteins but they
entail also negative eects due to possible residual che-
micals and modication of amino acids. Chemical
treatments of dietary proteins are, therefore, practised
with caution in the food industry [63, 64].
The most common treatments applied to proteinac-
eous raw materials are dierent heat treatments, fer-
mentation processes and extrusion technology. A novel
technology being introduced currently in the European
food industry is high pressure treatment which is
expected to replace in the future heat treatment prac-
tises in the manufacture of a variety of foodstus. These
methods are discussed hereunder in more detail.
loat tioatmoot
Heating is one of the oldest, most common, and most
widely used methods of modifying proteins, for exam-
ple, to make food proteins more edible. It is also used in
many dierent food products to form protein gels or set
structure. Such food products include yogurt, sausages,
and bread. Depending on the intensity of heat treat-
ment, the nutritive value of proteins may be aected
either in a positive or negative way. Heat is also used to
modify the functional properties of protein ingredients.
Heat denatures proteins and may be used, for example,
Table 4. Physicochemical changes and positive (+) or negative () nutritional eects of process treatment and storage on proteins and
amino acids
Treatment/Condition Physicochemical changes Nutritional eects
lkOClSS||C
loat tioatmoot lioto|o oooatoiat|oo |miovomoot o| |oti|os|c o|gost|b|||ty
koooct|oo o| tiys|o |o||b|toi act|v|ty
lostioct|oo o| |oat-soos|t|vo am|oo ac|os
|otiamo|oco|ai ioact|oos Cioss-||o|agos
koact|oo w|t| sogais lostioct|oo o| |ys|oo
l moo||cat|oo So|ob|||ty k|s| o| ox|oat|oo
Ac|o oi a||a||oo |yoio|ys|s |miovomoot o| o|gost|b|||ty
|osoc||c ot|oo booo bioa|ago
lostioct|oo o| l-soos|t|vo am|oo ac|os
Cioss-||o|agos
|somoi|zat|oo iacom|zat|oo
lozymat|c |yoio|ys|s koact|oo w|t| iotoasos lot|oos '
koact|oo w|t| oxygooasos Ox|oat|oo o| am|oo ac|os t|ioog| |||o oi o|y|ooo| ox|oat|oo
\ombiaoo soaiat|oo lioto|o |iact|ooat|oo lioto|o'ot|oo ooi|c|moot
C|aogo |o am|oo ac|o comos|t|oo '
S1OkACl koact|oo w|t| sogais lostioct|oo o| |ys|oo
liosooco o| oxygoo Ox|oat|oo
koact|oo w|t| o|y|ooo|s Ox|oat|oo
lata moo||oo |iom l|oot '
!0 H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319
to improve water-binding ability and emulsication. On
the other hand, heating usually decreases the solubility
of proteins due to their aggregation or coagulation.
Heat denaturation temperatures of dierent dietary
proteins vary from 60 to 90

C [65]. Accordingly, the

activity of bioactive proteins is reduced by dierent heat
treatments. At a standard pasteurization temperature of
72

C for 15 s, the bioactive whey proteins retain most of

their activity [5, 12]. Although most thermal denatura-
tion is irreversible in nature, certain proteins may
undergo reversible denaturation when the thermal
inuence is removed. For example, the thermal dena-
turation of -lactalbumin is primarily a reversible
process with 8090% renaturation at pH values above
3.3. Below pH 3.3, the ability of the protein to return to
the native conformation is reduced. The reversibility of
-lactalbumin is calcium dependent, the regeneration
being reduced when a chelator that binds endogenous
Ca
2+
is added [65].
During heat treatment, the lysine residues of proteins
can react with reducing carbohydrates of the same food
system resulting in the so-called Maillard or non-
enzymatic browning reaction [5]. Depending on the
intensity of heat treatment, this reaction aects the sen-
sory properties (aroma, avour and appearance) of the
product and reduces its nutritional value as the bioa-
vailability of lysine is reduced. Ingestion of Maillard
reaction products may also induce detrimental eects at
the cellular level in the body [5]. Milk is highly sensitive
to the Maillard reaction because of its high levels of
lactose and lysine-rich proteins. Standard pasteurization
of milk does, however, not cause any destruction of
lysine and the UHT treatment destroys less than 2% of
lysine. In can sterilization of milk destroys 1015% of
available lysine. During the storage of milk powders,
the evolution of lysine blockage depends on water
activity and temperature. In model studies, it has been
shown that up to 5060% of lysine can be blocked dur-
ing long-term storage with no browning development
[5]. In milk and infant formulas, the lysine loss has a
limited nutritional eect, as they contain much more
lysine than the recommended level for adults and
infants. A number of compounds have been demon-
strated to inhibit the Maillard reaction. In milk pro-
ducts, active sulfhydryl groups of whey proteins inhibit
heat-induced browning. Also, high pressure treatment
can inhibit the Maillard reaction in milk [66].
loimootat|oo
Natural or controlled fermentation has been exploi-
ted by mankind for thousands of years to preserve dif-
ferent foodstus and to retain or alter their nutritive or
sensory properties. Typical examples of fermented pro-
ducts are ripened cheese varieties, fermented dry sau-
sages, and fermented soya bean (tofu), cereal (bread)
and vegetable (sauerkraut) products. The fermentation
process involves usually natural or added microorgan-
isms (starter cultures), e.g. lactic acid bacteria, which
during their growth hydrolyse sugars and proteins
available in their surrounding medium. As a result,
peptides with dierent amino acid sequencies and single
amino acids are formed. The degree of proteolysis is
highly dependent on the bacterial species involved and
physical conditions of fermentation [67]. The peptides
and amino acids derived from proteins during fermen-
tation often change the functional, rheological, sensory
and biological properties of the fermented product.
Recently, it has been established that during milk
fermentation, bioactive peptides are formed from milk
proteins. Nakamura et al. [25] isolated two ACE-inhi-
bitory peptides Val-Pro-Pro and Ile-Pro-Pro, from sour
milk. ACE- inhibitory activity was also found in ripened
cheese types. This activity increases during cheese
maturation, but decreases when the proteolysis exceeds
a certain level [26]. Caseinophosphopeptides can be
formed during cheese ripening due to plasmin and
microbial protease activity [68, 69]. Laeneur et al. [70]
showed that -casein hydrolysed by lactic acid bacteria
has immunomodulatory activity which could be related
to interaction with monocyte-macrophage and T-helper
cells. Su tas et al. [71] showed that caseins hydrolysed
with a probiotic Lactobacillus GG strain and digestive
enzymes generate compounds with specic suppressive
or stimulatory eects on human lymphocyte prolifera-
tion in vitro. Further, Rokka et al. [72] identied several
known bioactive peptides with ACE-inhibitory, opioid
or immunomodulatory activities from the casein hydro-
lysates used in the above study. These results suggest
that during fermentation of milk with probiotic bac-
teria, peptides with distinct bioactivities can be formed.
Such peptides may contribute to the well-documented
health-promoting properties of fermented dairy pro-
ducts and probiotic lactic acid bacteria [7376]. Some
possible actions of fermented milks in vivo are described
in Fig. 1.
||tia ||g| iossoio
Ultra high pressure (UHP) processing is a non-thermal
process in which foods are subjected to high isostatic
pressures of 1001000 MPa at room temperature.
UHP processing can aect protein conformation and
lead to protein denaturation, aggregation or gelation,
depending on the protein system, the applied pressure,
the temperature and the duration of the pressure
treatment. Low pressures usually induce reversible
changes such as dissociation of protein-protein com-
plexes, the binding of ligands and conformational changes
[66]. Pressures higher than 500 MPa induce, in most
cases, irreversible denaturation. The UHP process also
inactivates microorganisms and, therefore, this techni-
que provides an alternative to heat treatments. On the
other hand, there are, considerable dierences in protein
H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319 !!
denaturation and aggregation induced by high pressure
compared with heat. The use of high pressure to modify
the functionality of food proteins was recently reviewed
by Heremans et al. [66] and Messens et al. [77]. Refer-
ence is made hereunder to these reviews. Although
blood plasma and egg white proteins are known to be
sensitive to heat and readily form gel networks at mod-
erate operating temperatures, at 80

C (30 min), no
gelation occurs if these proteins are pressurized for
30 min at a pressure of 400 MPa. This stability may be
positively correlated with the high amount of disulde
bonds stabilizing the three-dimensional structure of
both proteins. Again, -lactoglobulin appears far more
sensitive towards pressure than ovalbumin and bovine
serum albumin (BSA). UHP process has been shown to
destabilize casein micelles in reconstituted skim milk.
The size distribution of the spherical casein micelles
changed from &200 nm to 120 nm after pressurization.
Subsequent heating of skim milk at 30

C and at
atmospheric pressure restored the original size distribution.
In another study [78], the antigenicity of whey protein
hydrolysates treated with high pressure was found to be
lower than that of heat-treated hydrolysates. Mussa and
Ramaswamy [79] studied the kinetics of microbial
destruction and changes in physico-chemical character-
istics of fresh raw milk caused by UHP treatment which
was conducted at 200400 MPa for various holding
times (5120 min). The treatment led to an ecient
destruction of microorganisms and a prolonged shelf-
life of milk up to 18 days at 5

C and 12 days at 10

C. It
was concluded that UHP processing of milk may be a
useful alternative for extending the shelf-life with qual-
ity advantages. Other potential applications of UHP
treatment on milk include low-temperature inactivation
of enzymes and stabilization of fermented dairy pro-
ducts, improved coagulation of milk, and the manu-
facture of dairy gels and emulsions with novel textures
[77]. Furthermore, studies have been undertaken on the
eects of UHP treatment on meat proteins myosin and
metmyoglobin, egg white, ovalbumin and soya proteins.
Additional experimental research on protein model sys-
tems and real food products is required to understand
the potential of this technology in the restructuring of
food proteins and stabilizing their biological activities.
lxtios|oo
At present, the major technique for texturization of
plant proteins is thermoplastic extrusion. In the extru-
sion process, the raw material is exposed to high pres-
sure (10,00020,000 kPa), high temperature and shear
forces. Extrusion is applied in the manufacture of
instant and snack foods, in particular. Starting materi-
als are usually protein isolates, concentrates and ours.
During extrusion, disulphide bonds play an important
role in protein interactions. Mei and Tung [80] observed
that the solubility of wheat proteins decreased and both
aggregation and fragmentation occurred during the
extrusion process. Proteins aggregated mostly through
non-specic hydrophobic interaction and inter-
molecular disulphide bond formation. Glutenins and
Fig. 1. loss|b|o in vivo |ooct|oos o| iob|ot|c |oimootoo m|||s.
!2 H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319
gliadins were mainly responsible for the aggregation.
Tae [81] studied eects of extrusion on the functional
properties of co-precipitated proteins originating from
soy our and wheat gluten. As compared to native pro-
teins, extruded proteins had signicantly improved
viscosity, gelation and foaming stability. Hu et al. [82]
observed that among the extrusion parameters, the
temperature used had the greatest impact on the nutri-
tional quality of wheat, rice and soyabean proteins.
Addition of soyabean improved signicantly protein
quality and stability of rice and wheat extrudates. In
animal studies, it has been shown that extruded grains
lower serum and liver cholesterol levels as compared to
raw grain diet or control diet based on casein [83]. Fur-
ther research is required to verify these ndings and to
establish the eects of extrusion on the bioactive prop-
erties of dietary proteins.
Processing options modulating functionality
Stioctoio|ooct|oo io|at|oos||s
The functional properties of proteins in a food matrix
are highly inuenced by their molecular structure, pro-
tein interactions with other components, e.g. water,
other proteins, carbohydrates, lipids and ions, as well as
the conditions of processing. Apart from sensory prop-
erties, typical functions of proteins in food systems
include adhesion and cohesion, emulsication, gelation,
foaming, texturization, water, lipid and avor binding
and retention. These functionalities are described in
detail in recently published books and review articles
and will not be discussed further in this review [64, 84
88].
lozymat|c moo||cat|oo o| ioto|os
Proteins can be hydrolysed with acid, alkali or
enzymes to yield peptides or, eventually, amino acids.
For example, acid hydrolysis is being used to produce
hydrolysed vegetable proteins, which have meaty avor
proles. Alkali treatments are used in the production of
gelatin. Various enzymatic hydrolytic treatments, how-
ever, have become the most important tools for
modifying the functionality of dietary proteins [60, 84,
89]. Enzymatically modied proteins have long been
available in many conventional foods such as ripened
cheese and fermented soya protein products. Moreover,
pure protein hydrolysates have been shown to have
valuable dietetic properties and high nutritional value
[90]. Modication of milk proteins by enzymatic treat-
ments is described in more detail below.
\|oy ioto|o |yoio|ysatos
The most commonly used enzymes in the production
of whey protein hydrolysates are pepsin, trypsin and
chymotrypsin. Also, plant-originated papain and some
bacterial and fungal proteases have been used in studies
reviewed by Lahl and Braun [91], Panyam and Kilara
[92] and Nielsen [60]. The ability of enzymes to hydro-
lyse whey proteins is highly variable. Pepsin digests
-lactalbumin and denatured, but not native -lacto-
globulin [93]. Trypsin hydrolyses -lactalbumin slowly
but -lactoglobulin remains almost undegraded [94].
Chymotrypsin hydrolyses readily -lactalbumin but -
lactoglobulin is degraded slowly. Liske and Konrad [95]
demonstrated that BSA and -lactoglobulin were
hydrolysed by papain but -lactalbumin was resistant.
However, -lactalbumin was hydrolysed completely at
acidic pH when calcium binding was absent [97]. Enzy-
matic modication of milk proteins by controlled pro-
teolysis can alter their functional properties over a wide
pH range and other processing conditions [63, 91]. The
hydrolysis of peptide bonds can increase the number of
charged groups and hydrophobicity, decrease molecular
weight, and modify molecular conguration [97]. Chan-
ges in functional properties are greatly dependent on the
degree of hydrolysis. The most common changes in
functionality of whey proteins are an increase in solubi-
lity and a decrease in viscosity. When the degree of
hydrolysis is high, hydrolysates often tolerate strong
heating without precipitating, and solubility is high even
at pH 3.54.0. Hydrolysates also have far lower viscos-
ity than intact proteins. The dierence is especially
striking in solutions with a high protein concentration.
Other eects are altered gelation properties, enhanced
thermal stability, increased emulsifying and foaming
abilities and decreased emulsion and foam stabilities
[95, 98, 99].
A||oigoo|c ot|oos
Milk, egg, soya and wheat proteins may provoke
allergic reactions in sensitized people [6]. Processing
may alter the content and/or properties of these aller-
gens, reducing or increasing the allergenicity of the
starting material. In earlier studies, conicting results
were obtained with regard to the eect of heat treatment
on the allergenicity of whey proteins. Standard pasteur-
ization of milk does not seem to cause any signicant
reduction of the antigenicity of milk proteins, while milk
sterilization may even exacerbate allergic reactions
[100]. It has been postulated that heat treatment and
homogenization of milk, due to mechanical disintegra-
tion of casein micelles and milk fat globules, increase
the ability of milk proteins to elicit allergic reactions in
sensitized persons [101, 102]. Further studies have,
however, not been carried out to substantiate this
hypothesis. In contrast, many studies have shown that
the allergenicity of milk proteins, in particular that of -
lactoglobulin, can be reduced substantially if the pro-
teins are hydrolysed with pepsin or trypsin or using
combinations of proteolytic enzymes [60, 103, 104].
Heat treatment or high-pressure treatment prior to
hydrolysis increases the DH (degree of hydrolysis)
value, further reducing antigenicity of whey proteins
H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319 !
[105, 106]. The hydrophilic amino acids, such as lysine,
arginine, glutamate, and aspartate residues seem to play
important roles in allergenic peptides. The antigenicity
of such peptides can probably be lowered further by
using proteases specic for these amino acid residues.
On the other hand, it has been reported that peptides
consisting of four amino acids only can cause an allergic
reaction in consumers allergic to milk, even though
these small peptides will not be able to sensitize a person
[107]. Partially or extensively hydrolysed milk proteins
have found increasing use in hypoallergenic infant for-
mulas and dietetic products [6, 108110]. The problems
related to enzymatic hydrolysis of proteins are the pro-
duction of a high amount of free amino acids, a bitter
taste and an increase of the formula osmolarity [111].
Current research in this eld is focusing on technologi-
cal reduction in whey of the amount of -lactoglobulin
which is considered the major allergen because it is
absent in human milk. On the other hand, infant for-
mulas enriched with -lactalbumin are being developed
to mimic human milk as it is rich in this protein [64].
||oact|vo ot|oos
A lot of scientic interest has focused on physiologi-
cally active peptides derived from food proteins. These
peptides are inactive within the sequence of the pre-
cursor protein and can be released by enzymatic pro-
teolysis. Milk proteins are a rich source of bioactive
peptides; both casein and whey proteins have been
found to act as precursors of bioactive peptides [3, 64,
36]. Opioid peptides (exorphins) are receptors of opioid
ligands with agonistic or antagonistic activities. These
peptides can be released by the digestion of bovine
casein and whey proteins [112, 113]. -casein opioid
peptides (-casomorphins) have been detected in the
duodenal chyme of minipigs [114] and in the human
small intestine [115] as a consequence of in vivo diges-
tion. Casein of other species like ovine, bualo and
human milk can be regarded as precursors of exorphins
since they contain the amino acid sequences character-
istic for exogenous opioid peptides [116]. Exorphins can
be found also from wheat gluten proteins and their dif-
ferent classes of saline-soluble gliadin and glutein. The
sequences of these peptides have not yet been deter-
mined [59, 117]. Angiotensin-converting enzyme (ACE)
acts on blood pressure regulation and inhibition of this
enzyme can exert an antihypertensive eect. ACE-inhi-
bitory peptides have been isolated from enzymatic
digest of food proteins. Oshima et al. [53] reported that
collagen and gelatin digests contain ACE-inhibitory
peptides. Enzymatic digestion of casein produces ACE-
inhibitory peptides; also fermentation of milk produces
ACE-inhibitory peptides [25, 118, 119]. Some of these
identied ACE-inhibitory peptides have also been
shown to have an antihypertensive eect in vivo [25,
120]. ACE-inhibitory peptides have also been found
from whey, sh and maize protein digests [51, 121].
Immunomodulating casein peptides have been found to
stimulate the proliferation of human lymphocytes and
the phagocytic activities of macrophages [122]. Anti-
microbial peptides from lactoferrin have been shown to
kill sensitive microorganisms [123]. Casein phospho-
peptides can form soluble organophosphate salts and
may function as carriers for dierent minerals, espe-
cially calcium. Bovine
s1
;
s2
and -casein contain
phosphorylated regions which can be released by enzy-
matic hydrolysis and specic phosphopeptides have
been identied in the intestinal contents of minipigs
after ingestion of a diet containing casein [114]. There is
commercial interest in the production of bioactive pep-
tides with the purpose of using them as active ingre-
dients in functional foods. The development of
technology for industrial-scale production of such pep-
tides is currently in progress [124].
||ttoi ot|oos
It has long been known that peptides and amino acids
can produce many types of taste sensation [63]. A pro-
blem in the use of proteolysis for improving function-
ality and nutritional value has been the formation of
bitter peptides, which are formed, for example, from -
lactoglobulin [60]. Bitterness is generally related to the
hydrophobicity of the amino acids in the peptides. In
earlier studies, activated charcoal, various resins, glass
bre and hexyl sepharose were applied for the elimina-
tion or reduction of bitter peptides from the hydro-
lysates. Also, the plastein reaction which can occur
when a protein hydrolysate is incubated with a protease,
is able to debitter protein hydrolysates [60]. Other
methods used for reducing or eliminating bitterness are
selective chromatographic separation, masking and
enzymatic treatment [125, 126].
|ovo| |iact|ooat|oo toc|o|qoos o| b|oact|vo ioto|os
The rapid development of membrane and gel ltra-
tion techniques in the 1970s provided new possibilities
for a large-scale concentration of whey proteins and the
manufacture of whey protein concentrates and isolates
[127131]. Also, manufacture of demineralized whey
powders has become possible on a large scale through
application of dialtration or ion exchange chromato-
graphy. Techniques for the isolation of individual whey
proteins on a laboratory scale by salting-out, ion-
exchange chromatography and/or crystallization has
been available for a long time. Owing to the unique
functional and biological properties of many of the
whey proteins, a need has arisen to develop novel,
gentle methods for their enrichment or isolation on a
large scale [10, 132]. To this end, pilot and industrial-
scale technological methods have been developed for
isolation, in a puried form, of several individual
whey proteins, such as -lactalbumin, -lactoglobulin,
!4 H. Korhonen et al./Trends in Food Science & Technology 9 (1998) 307319
lactoperoxidase, lactoferrin, glycomacropeptide and
immunoglobulins [133140]. Also, methods for fractio-
nation of micellar whole casein and selective separation
of -casein have been developed [124]. For isolation or
enrichment of milk proteins combinations of membrane
separation and chromatographic techniques, such as
microltration, ultraltration, reverse osmosis, nanol-
tration, gel ltration and ion-exchange chromatography
have been applied [131, 141]. Recently, an ion-exchange
membrane technique has been employed successfully
for separation of lactoferrin and lactoperoxidase
from cheese whey [142]. A potential future method for
large scale fractionation and enrichment of bioactive
peptides is a membrane bioreactor based on serial
ultraltration membranes with dierent cut-o values
[124, 143]. Also, further research is needed on the
extraction and purication of the three casein fractions
and other minor whey proteins, such as polypeptide
growth factors, complement factors, enzymes and
transgenic proteins.
Safety implications of bioactive proteins
The development of functional foods is likely to entail
the increased use of dierent protein sources known to
contain bioactive components. These protein compo-
nents may be natural constituents of plant or animal
origin or genetically modied or transferred from
another source. The introduction into the diet of func-
tional foods supplemented with these compounds may
raise the issue that such food products might cause
allergies. Although the bioactive proteins or peptides
described in this article are not known to possess spe-
cic allergic or toxic eects, their addition to any dif-
ferent food system warrants careful consideration about
potential health risks. Specically, their interactions
during processing or storage with other proteins, sugars
and lipids need to be researched with a view to possible
formation of toxic, allergenic or carcinogenic sub-
stances. Some concern has been raised that the transfer
of proteins from one food source to another by genetic
modication could lead to the appearance of a major
food allergen in a normally allergen-free product. In this
respect, analytical methodologies need to be developed
to detect the presence of such allergens.
Further development and research needs
The occurrence of many natural bioactive proteins or
their precursors in animal and plant proteins is now well
established. There are, however, a great number of sci-
entic and technological issues to be solved before these
substances can optimally be exploited for human nutri-
tion and health. Below is a list of the most important
future research needs related to bioactive proteins:
. Basic research on potential bioactivity of minor
proteins of milk, egg, vegetables, cereals, and fruits.
. Technological functionality of bioactive proteins,
e.g. lactoferrin, immunoglobulins, egg proteins
and bioactive peptides.
. Interactions of bioactive proteins/peptides/amino
acids with other food components during proces-
sing and eects of these interactions on bioactivity.
. Eects of conventional and novel processing tech-
nologies on the bioactivity of the proteins.
. Development of novel fractionation and purication
methods for bioactive proteins and their hydro-
lysates.
. Basic research on transgenic production of bioac-
tive proteins and potential side-eects, e.g. aller-
genicity and toxicity of such proteins.
. Evaluation of ecacy of bioactive proteins in ani-
mal model and human clinical studies per se and in
food systems.
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