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UNIVERSIDAD NACIONAL DEEL CALLAO
FACULTAD DE INGENIERIA PESQUERA Y DE ALIMENTOSESCUELA PROFESIONAL DE INGENIERIA DE ALIMENTOS
Nuevo Modelo de Funcionalidad de las
!o"e#nas de los Ali$en"os
Cu!so% Avances en Ciencia & Tecnolo'#a de Ali$en"os(
Docen"e% D!) In'( Ole'a!io Ma!in(
Alu$no% Ro$e!o Valve!de *avie!(
CALLAO-BELLAVISTA
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JFS Special Issue: 75 Years of Advancing FoodScience, and Preparing for the Next 75
Food Protein Functionalit!A Ne" #odel$% Allen Foegeding
A&stract: Proteins in foods serve dual roles as nutrients and structural building blocks. The concept of protein function-ality
has historically been restricted to nonnutritive functionssuch as creating emulsions, foams, and gelsbut this places sole
emphasis on food quality considerations and potentially overlooks modifications that may also alter nutritional quality or
allergenicity. A new model is proposed that addresses the function of proteins in foods based on the length scales!
responsible for the function. Properties such as flavor binding, color, allergenicity, and digestibility are e"plained based on
the structure of individual molecules# placing this functionality at the nano$molecular scale. At the ne"t higher scale,
applications in foods involving gelation, emulsification, and foam formation are based on how proteins form secondary
structures that are seen at the nano and microlength scales, collectively called the mesoscale. The macroscale structure
represents the arrangements of molecules and mesoscale structures in a food. %acroscale properties determine overall
product appearance, stability, and te"ture. The historical approach of comparing among proteins based on forming and
stabili&ing specific mesoscale structures remains valid but emphasis should be on a common means for structure formation
to allow for comparisons across investigations. 'or applications in food products, protein functionality should start withidentification of functional needs across scales. Those needs are then evaluated relative to how processing and other
ingredients could alter desired molecular scale properties, or proper formation of mesoscale structures. This allows for a
comprehensive approach to achieving the desired function of proteins in foods.
'e"ords: foam, gel, protein, protein functionality, sol
ntroduction(t could be argued that proteins are biology)s most versatile
polymers. The other main biological polymerspolysaccharides
and nucleic acid polymers *+A and +A!are structurally re-
stricted because being composed of ust a few monomers limits the
chemical properties that can be imparted in the final struc-ture. (n
contrast, proteins with / amino acids have the ability to take on a
range of structures that provide catalytic activity en-&ymes!,
building material for tissues collagen!, and mechanisms for
movement myosin and actin!, to name a few of the numerous
biological functions. The history of proteins has been eloquently
covered in a book by 0harles Tanford and 1acqueline eynolds
titled 2+ature)s obots Tanford and eynolds //3!.4 As the name
implies, proteins are molecules that play an active role in biology
and the concept of activity is usually e"pressed as bio-logical
function. The central dogma of protein chemistry is that the
sequence of amino acids determines the 5 dimensional struc-ture,
and the 5-dimensional structure determines the biological function
0reighton 3665!. This is fitting for biological functions whereprotein structure is the result of evolutionary pressure to survive and
be passed on to the ne"t generation. A fascinating e"-ample of this is
the umami receptor in hummingbirds evolving to essentially become
a sweetness receptor, allowing hummingbirds to adapt to a different
food source 7aldwin and others /38!. Proteins take on a broader
functionality role in foods. They can function in foods by an
e"tension of their biological activity, by
MS 20151269 Submitted 7/27/2015, Accepted 9/21/2015. Auto! i" #it$ept. of %ood, &iop!oce""ing ' (ut!ition Science", (o!t )a!olina State*ni+., .. &o 762, aleig, (.). 27695-762, *.S.A. $i!ect inui!ie" toauto! %oegeding 3-mail4 allenfoegedingnc"u.edu.
being building blocks for food structures that biology had notintended, or they can bind a variety of small molecules and altertheir availability during ingestion.
9ne e"ample of proteins functioning in foods as an e"tension of their
biological "t!uctu!e and functionis en&ymes. The ability of en-&ymes to
cataly&e reactions can produce desirable meat tenderness altered withproteolytic en&ymes! or undesirable fruit browning caused by
polyphenol o"idase! changes in food. (n other cases, the polyme! and
colloidal p!ope!tie" of proteins are manipulated to pro-duce desirable
food structures, as is the situation with dairy foods. The biological
function of casein micelles is not to make cheese or yogurt# however,
the colloidal and polymer properties of casein micelles allow for the
production of a wide range of dairy prod-ucts. 'inally, protein surfaces
have different degrees of polarity and potential binding "ite" for small
molecules such as flavor compounds and polyphenols 'ran&en and
:insella 36;8# 9)0onnell and 'o" //3# 7andyopadhyay and others
/3!. This binding could alter the ability to perceive a flavor einers
and others ///! or could be used to decrease loss of a bioactive
polyphenol
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Ne" food protein functionalit 4odel % % %
assessment. (tbuilds and e"pandson a previousevaluation of pro-tein functionality'oegeding and*avis /33!.
6nderstanding
o" ProteinsFunction in aFood fro4 the8asis of FoodStructure
Proteins are
generally part of a
comple" structure in
foods that
determines hedonic
properties and may
contribute to the
bioavailability of
nutrients and other
bioactive
compounds. @ome
e"amples of foods
and properties
associated with
proteins are seen in
Table 3. ach food
property can be
e"plained by
structural elements
according to scale
'igure 3 and Table
3!. 'rom this
perspective, %ood"t!uctu!e is the
combined
representation of a
food starting with
the molecules, the
primary structures
formed from the
molecules, and the
overall structure
observed by the
consumer 'igure
3!. The molecula!
"cale /nm! is the structure
of the individual
molecule. (n
proteins, this
encompasses
primary, secondary,
tertiary and, when
applicable,
quaternary structure
0reighton 3665!.
The mac!o"copic
le+el is the highest
level and represents
the overall
organi&ation of
molecules and
substructures in a
food. This
structural level is
observed when
viewing food and
evaluated when
eating.
(ntermediate
between molecular
and macroscopic
scales is the
me"o"cale. This
has also been
referred to as
microscale due to
features with si&es
in the range of
micrometers, but
me"o meaning
2middle or
intermediate4
from ancient
Breek for
2middle4! is more
accurate as nanosi&e structures can
also be involved.
@tructures viewed
at the microscale
have historically
been the focus of
2food structure
analysis,4 for
e"ample see
review by =eerte
/38!, but a more
recent and
comprehensiveapproach to food
structure is to take
on the perspective
of soft matter
physics and view
structures across
length scales
Cbbink and others
//?# van der
@man /3!.
'oods can be
defined on a soft
matter physics
length-scaleperspective as a
collection of
molecules
molecular scale!
assembled into
various
mesostructures
mesoscale! that
are assembled into
the overall food
structure
macroscale!.
=edonic sensationsof a foodthose
associated with
appearance, taste,
a
r
T
h
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the biological
mesostructures for
e"ample,
myofilaments and
sarcomeres! and
how physiological
events occurring
during conversion of
muscle to meat alter
those
mesostructures. This
often requires in "itu
investigations to
under-stand
structural changes
associated with meat
tenderness. 'orma-
tion of processed
meats such as a hot
dog$frankfurter is a
different matter.
%yofibrillar
proteins are
e"tracted
dispersed! from
their biological
structures and
form interfacial
films around
dispersed fat
droplets
colloidal$polymer
mesostructure!
and, upon heating,
a gel network
colloidal$polymer
mesostructure! is
formed that traps
the dispersed fat
phase 'oegeding
and amsey 36?;!.
(n processed
meats, proteinfunctionality is
related to the
ability of muscle
proteins to form
and stabili&e
colloidal
structures. =ow-
ever, post-mortem
events may alter
the proteins and$or
the ability to
e"tract the proteins
from the biologicalstructures for use
in forming
colloidal
structures.
A contrast to
meats would be
milk and milk
products. The bi-
ological structure
of milk is actually
a colloidal
dispersion of pro-
teins whey and
casein micelles!
and fat globules in
a true solution
serum phase!
containing salts,
lactose, and other
compounds. 0a-
sein micelles are
naturally dispersed
in milk and
stabili&ed against
aggregation by
steric and
electrostaticmechanisms that
are also used to
stabili&e synthetic
c
o
T
h
P
e
ol% 1*, Nr% +), )*+5 Journal of Food Science()37+
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(:Food(he4istr
:
oo
e4
sr
Ne" food protein functionalit4odel % % %
Table 1Properties of foods associated
with proteins and their related structural
element.
topic by stating that
2The possession of
these characteristics
by a much lower-
priced product made
from whey, either
naturally or as the
result of permissible
physical or chemicaltreatment, would
result, therefore, in its
e"tended use4 Peter
and 7ell 365/!. This
type of investigation
continues today with
additional
motivations beyond
lower cost! of dietary
restrictions gluten
free or vege-tarian!
and a more
sustainable ingredient
source, to name a few
goals. 7ased on the
food structure model
'igure 3!, successful
substitution of one
protein for another
changing the
moleculscale!
is based on the ability
of various proteins to
form the same
mesostructures. (n
other words, Peter
and 7ell worked on
the hy-pothesis that if
they could show how
to produce wheyprotein foams with
properties similar to
egg white foams, then
whey pro-teins could
be substituted for egg
white. This is a
logical yet often
incomplete approach
that will be discussed
in subsequent
sections.
@cientists have
used both top down
and bottom up
approaches to
understand protein
functionality, and this
has produced con-
fusion on the precise
meaning of p!otein
functionality.
*ifficulties
Structural elements by scale
Food Food property Molecules Mesostructures Macrostructure
@keletal meat Te"ture %yofibrillar proteins and @arcomere, connective Amount and location of connective tissuecollagen tissue and muscle fibers
0olor %yoglobinDater holding %yofibrillar proteins and @arcomere, connective Amount and location of connective tissue
collagen tissue and muscle fibers0heese Te"ture 0aseins and whey proteins mulsion, Bel Phase volumes of emulsion and gel# gel
structure# emulsion droplet si&e%elting and flow 0aseins and whey proteins Bel Phase volume and structure of gel
Tofu Te"ture @oy proteins Bel Bel structureDater holding @oy proteins Bel Bel structure
7everages Te"ture Earious proteins @ol @i&e and shape of solid particlesmouthfeel!
0larity Earious proteins @ol @i&e and shape of solid particles7read and 0akes Te"ture Earious proteins 'oam, mulsion Phase volume of foam and emulsion# bubble
foam! and droplet emulsion! si&e
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Figure +9Protein functionalit &ased on lengthscale of structural ele4ents deter4iningfunctionalit%
()37) Journal of Food Scienceol% 1*, Nr%+), )*+5
Ne" food protein functionalit4odel % % %
Table 2Molecular scale functional
properties of proteins.
Molecular property
0olor %yoglobin@weetness Thaumatinn&ymatic activity 0hymosin
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Food(he4istr
in applying the term
2functionality4 to
food proteins and
food applications
were addressed by
Pour-l 36?3! in
stating that 2+o
subect in the generalarea of food
chemistry and
technology has
suffered more from
inconsistency,
confusion, and
ambiguity than the
field of
functionality.4 Pour-
l 36?3! proposed a
list of food types and
associated protein
functionalities. @ome
of the so-called
functionalities
mentioned by Pour-l
36?3! are directly
related to molecular
or mesoscale
structures that can be
characteri&ed by a
range of chemical and
physical properties
associated with
molec-ular structure
color and comple"
formation! or formation and
stabili&ation of
colloidal
mesostructures. The
colloidal systems
cov-ered are sol
solid dispersed in
liquid!, emulsion
liquid dispersed in a
liquid!, foam gas
dispersed in a liquid!,
and a gel continuous
solid network
surrounded by a
fluid!. 9ther
functionalities were a
bit more ambiguous
and dependent on
specific empirical
tests solubility, fat
holding capacity,
liquid holding
capacity, and water
absorption!. (n
addition, some were
associated with
sensory per-ceptionof macroscale
structures hardness,
chewiness, cohesion,
and adhesion!. (f a
protein has a
function, and the
function is due to
chemical$physical
aspects of the
protein structure or
mesostruc-tureformed, then there
should be a way to
assay that function.
=all 366F!
proposed that
protein functionality
can be analy&ed by
methods that cover
solubility, viscosity,
gelation, foam
formation and
stabili&ation,
emulsion formation
and stabili&ation,
water and fat
holding properties,
and surface
hydrophobicity.
These can be
grouped into
molecular
hydrophobicity and
viscosity!, molec-
ular and
mesostructure
solubili ty of a
powdered protein!,and mesostructure
gel, foam,
emulsion, and fat
and water holding!
scale properties.
This is generally
valid as a point of
comparison that is
independent of a
specific food
application.
=owever, these tests
must cover a range
of solution
conditions protein
concentra-tion, p=,
ions, and ionic
strength! to be
robust enough to
cover a broad range
of food
applications. The
advantage of this
approach is that
there are numerous
physical and
chemical tests thatcan be use to
characteri&e
molecular and
m
e
#
A
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The model consistsof 5 structuralscales andfunctionalpropertiesassociated witheach structuralscale.
Molecula! "cale
properties are those
that can be
e"plained primar-ily
on protein structure
considerations.@ome e"amples of
molecu-lar scale
properties are seen
in Table .
n&ymatic activity,
binding of proteins
to biological
receptors, color, and
binding of ligand
compounds for
e"ample, flavor
compounds or
polyphenols! are the
result of specific
properties of protein
structure. These
func-tions are
analogous to
biological structureG
function
relationships and
amenable to a broad
range of physical,
chemical, and
molec-ular biology
tools that are used to
determine howproteins func-tion in
biology. 'or
e"ample, a
molecular docking
computational tool
can be used to
evaluate how
ligands flavor
compounds or
polyphenols! bind to
proteins rickson
and others //8!.
There are molecularproperties that have
a direct impact on
health and nutrition.
Proteins are the
source of amino
acids and bioactive
pep-tides# therefore,
it is essential that
modifications that
reduce these
contributions be
avoided.
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stabili&e colloidal
mesostructures is a
good way to
compare !elati+e
functionality among
proteins, or the
result of protein
modification, but
may miss a critical
element needed to
perform in a specific
food product. (f
there were
standardi&ed
conditions for
forming colloidal
structures, then the
properties of those
structures could be
considered an
ine!ent
functionality of a
protein.
The final level is
the mac!o"cale,
which accounts forall elements
comprising a food.
The science of soft
matter physics is
based on the
premise that the
behavior of soft
matter materials
can-not be predicted
from molecular
constituents and
originates from
mesostructuresCbbink and others
//?# van der @man
/3!. The
macrostructure can
be viewed as the
amount and spatial
dis-tribution of
definable
mesostructures and
molecules. (t can be
very simple, as in a
gelatin gel, or the
comple" structures
found in ice cream,
cakes, or cheese, to
name a few.
'urthermore, there
are
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(:
ol% 1*, Nr% +), )*+5 Journal of FoodScience ()370
(:Food(he4istr
Ne" food protein functionalit4odel % % %
Table 3Locations and properties of proteins
in colloidal systems relatie to formation and
stabili!ation.
"olloidal system "ontinuous phase #ispersed phase $nterface
@ol Eiscosity relative to a second Protein aggregate si&e, shape, and +Adispersed phase density
'oam Eiscosity, formation of a network, +A Protein film thickness, gasinteraction with interface permeability# surface properties
electrostatic or steric stabili&ation!#and rheological properties
mulsion Eiscosity, formation of a network, +A Protein film thickness# surfaceinteraction with interface properties electrostatic or steric
stabili&ation!# dispersed phasepermeability# and rheologicalproperties
Solid continuous phase Li%uid continuous phaseBel 0ontinuous gel network of Eiscosity and interactions with the +A
characteristic strand thickness, gel network connectivity, and phase volume
+A, indicates not applicable.
some foods whereprocessing producesan initial 2green4structure, but thetarget structure isthe result of slowchanges duringaging, such as incheese. Productslike cheese requirean aging process toallow for slow
transitions at themolecular andmesoscales toproduce the desiredmacroscalestructure.
#acroscaleStructure 8asedon For4ing andSta&iliing the
Appropriate#esostructures
As seen in Table 3,processed foods that
rely on proteins for
food structure can be
modeled as one or a
combination of the
ba-sic colloidal
structures of sol,
emulsion, foam, or
gel. This has led to
producing and
stabili&ing said
colloidal structures as
being a pri-mary
focus in measuring
protein functionality.
%oreover, forming
and stabili&ing
colloidal structures
have a solid
foundation in the-
oretical and
e"perimental science
for e"ample,
*ickinson 366#
7irdi //6! that
provides useful
models to determine
mechanisms
responsible for
formation and
stability in foods
*ickinson 366#
Dalstra //5!. ach
colloidal structure has
various elements.
@ols, foams, and
emulsions have a
di"pe!"ed pa"e
surrounded by a
contin-uou" pa"e
and the inte!face
where the phases
meet. Proteins canfunction as being the
dispersed phase sol!,
forming an interfacial
film emulsion or
foam! or as part of
the continuous phase
sol, emulsion, or
foam! Table 5!. This
means that several
parameters need to be
determined when
evaluating protein
functionality, even ina simple colloidal
system.
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$4ulsions9ne of the most
common approaches
for evaluating protein
functionality in an oil-
in-water emulsion is to
compare several
proteins at
concentrations where
there is sufficient
protein to coat oil
droplets and minimal
remaining in the
dispersed phase. (f one
protein produces
smaller droplets, does
it have a higher
emulsifying abilityH
Ies, if your goal is to
ust produce small
droplets. =owever,
most emulsions have
to be stable for an
e"tended time, so the
sta-bility of the system
is often more
important than the
initial physical state
that is, droplet si&e
distribution!. *o small
droplets make for a
more stable emulsionH
Ies, if the
destabili&ation
mechanism is ust
based on the creaming
rate of the oil droplets
as described by the
@tokes)
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such as other
surfactants or sugars.
'or e"ample,
increasing sucrose
concentration in egg
white foams will
increase the
interfacial dilatational
elasticity of egg
white protein films
and foam stability
Iang and 'oegeding
/3/, /33!.
Therefore a key
functional property,
forming a protein
film with high
dilatational elasticity,
depends on inherent
properties of the
protein and how other
ingredients modify
them. This would
suggest that a
p!ima!y functionality
to compare amongproteins is properties
of an airGwater
interfacial film from
a standard aqueous
solutionwith
application to a
specific food
formulation requiring
accounting for
additional
constituents. This is
evident when
comparing the ability
of egg white proteins
or whey proteins to
be used in making
angel food cakes. A
complete replacement
of egg white with
equal amounts of
whey protein
produces a cake that
collapses upon
baking Pernell and
others //!. 7oth
proteins have
relatively similar
abilities to form wet
foams Iang and
'oegeding /3/,
/33! and have
similar structural
transitions when
heated 7erry and
others //6!. They
differ when flour and
sugar are folded into
the foam to make the
cake batter. Thisinitiates
destabili&ation in the
whey protein foam
and has minimal
effect on the egg
white foam 7erry
and others //6!. (n
this case, the critical
difference in protein
functionality is not
observed until a
mesostructure is
()372 Journal of Food Scienceol% 1*, Nr%+), )*+5
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Ne" food protein functionalit 4odel % % %
mi"ed with otheringredients to formthe batter collection of mesostructures andmolecules to formthemacrostructure!.
SolsProtein-
containing
beverages can be
considered sols,
with the dispersed
solid phase being
protein aggregates.
7everages designed
for meal
replacement or
workout recovery
contain other
ingredi-ents thatmay affect protein
interactions. The
effect of nonprotein
ingredients need to
be accounted for
when determining
how a protein will
function is a given
beverage. A
functional concept
that is used
regarding beverages
is 2thermal
stability.4 This
evokes the notion of
comparing protein
denaturation
temperatures
molecu-lar scale!,
but in reality it is the
stability of a
colloidal sol of
protein aggregates
mesoscale! that
determines
producing a
satisfactory productand shelf life.
*enaturation and
aggregation are
some-what linked,
but there are
e"ceptions as with
-lactalbumin that
denatures at F8 K0
but with minimal
aggregation
%cBuffey and
others //>!. An
acceptable quality
beverage is one that
after thermal
processing has
protein aggregates
that create the
desired clarity,
viscosity, and
mouthfeel.
@tructures
produced from
pro-tein
aggregation
molecular scale
interactions
producing
mesoscale
structures! will
depend on p=,
ionic strength, type
of ion, and pro-tein
concentration, in
addition to other
molecules such as
sugars +icolai
and *urand /35!.
Protein
functionality in a
beverage can berepresented based
on a state diagram
that shows
relationships
between or more
vari-ables. Dith the
goal of producing a
fluid, a general
approach is to use a
fi"ed thermal
process and vary the
solution conditions
to determine criticalconcentrations to
produce a stable sol.
This has been done
for -lactoglobulin
Ako and others
//6! and whey
protein isolate
Dagoner and
others /3>!. As
seen in 'igure ,
this allows for a
comparison of
&ones of stability
based on forming a
soland the sol
region can be
further subdivided
to show proper-ties
such as solubility.
The state diagram
approach is
applicable to
F
i
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comparison of
relative stability
among various
protein ingredients
or could be used to
determine the
stabili&ing$destabili&
ing effect of other
beverage
components for
e"ample, salts and
polyphe-nols!.
=owever, as with
the e"ample of
emulsions, this only
shows conditions
relevant to
formation of a sol
after thermal
processing, and
further analysis is
need to determine
shelf stability. @helf
life is based in part
on the protein
particle phaseremaining dispersed
and not forming a
precipitate, gel, or -
phase system over
time. At the
molecular scale,
most proteins are 3
to a few nanometers
in diameter and
sedimentation would
be so slow as to not
be a factor with a
shelf life of up to ayear or . Therefore,
forming a visible
precipitate or gel
network will depend
on the si&e and
amount of
aggregates formed
during thermal
processing and their
propensity to
undergo secondary
aggregation at
storage temperatures
yan and others
/35!. (n theory,
these elements
should be
predictable based on
how molecular
structure ability to
form intermolecu-lar
interactions during
thermal processing!
determines the type
of mesostructure
particle! formed.
The desiredmesostructure par-
ticle! is small in
si&e, had a density
approaching that
of the contin-uous
phase, and has a
higher amount of
repulsive than
attractive surface
forces to inhibit or
prevent secondary
aggregation.
;els
'orming aprotein gel
network can be
considered under
the same conte"t
as sol formation.
(n both cases, the
primary concern is
at the molecular
scale in factors that
favor interprotein
aggre-gation. They
differ in that the
goal of forming a
stable sol is tominimi&e
aggregation while
gelation requires
directed
aggregation of
proteins into a 5-
dimensional gel
network. The
mesostruc-ture of
the gel network
will determine
macroscopic
physical prop-erties of the gel
van der
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(:Food(he4istr
ol% 1*, Nr% +), )*+5 Journal of FoodScience ()375
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Ne" food protein functionalit 4odel % % %
(:Food(he4istr
loss from soyprotein gels underdeformationCrbonaite andothers /38!. Aunique challengewith physicalproperties of foodgels is that thereare numerousmethods available
to determine waterholding,rheological orfractureproperties#however, therelevance toperception duringconsumption maybe more comple".That requires anunderstanding ofhow foodmolecules andstructures areperceived byhumans.
Interfacing"ith u4anPhsiolog
There are several
molecula! functional
p!ope!tie" that are
important to
consumers regarding
hedonic and health
aspects of proteins.
Proteins are
nonvolatile, so
aromas associated
with protein ingre-
dients are due to
aroma compounds
that are either
present in the
ingredient or formed
upon storage. This is
more a characteristic
of the overall
ingredient andshould not be
considered a
property of the
protein per se.
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7/26/2019 Avances Traducido
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f
l
(
T
h
such as color,
sweetness,
en&ymatic activity,
and ligand binding
are observed at the
molecula! "cale
and should be
predictable directly
from protein
structure. These
properties should
be invariant from 3
manufacturer to
another and could
be found in a
master list based on
common assays.
@ince food protein
ingredients contain
a mi"-ture of
proteins, the
molecular scale
properties of the
ingredient would be
the proportionate
sum of theindividual proteins.
At the ne"t
structural level,
forming and
stabili&ing sols,
emulsions, foams,
and gelsand their
physical and
sensory properties
depend on
forming specific
me"o"cale
structures. Themain challenge at
this level is creating
standardi&ed
conditions for
forming the
structures that do
not inherently favor
one protein over
another. (n
comparing
proteins, the one
that forms a
stronger gel or
more stable foam
may depend on p=,
therefore
comparing across
p= and protein
concentration is
needed. 9nce
standard conditions
for formation are
established, then a
range of tests to
assess structure and
structural stability
can be used. 9necautionary note is
that processing
equipment becomes
outdated and
conditions should be
based on
engineering
principles that are
independent of
specific equipment.
Also, methods to
assess how
structures are
transformed during
oral processing are
needed.
The mac!o"cale
structure, which
determines the
overall properties of
the food, is created
by one or several
mesoscale
structures. As
illustrated with angel
food cakes, protein
function-ality
differences may not
appear until themesostructures are
mi"ed and processed
in the final stage of
food production.
An analogy can be
drawn with
determining the
bioactivity of a
polyphenol. An
isolated molecule
can show chemical
activity, say
antio"idant activityor binding to a
protein of interest,
which can be
conclusively shown
at the molecular
scale. The activity in
a biological system
can move from cell
culture, to rodent
studies, and finally
to human studies.
ach level of
increased
comple"ity provides
another potential
barrier to it
producing the
bioactivity predicted
from the molecular
structure.
Protein
functionality should
start with defining the
length scale and
structural basis for the
properties of interest.
Those defined at themolecula! "cale are
inherent to protein
structure and can be
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c
a
A
@u
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()373 Journal of Food Scienceol% 1*, Nr%+), )*+5
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Ne" food protein functionalit 4odel % % %
Author(ontri&utions
.A. 'oegedingis the solecontributor to thearticle.
-eferencesAberle *, 'orrest 10,
Berrard *, %ills D.//3. Principles of meatscience. 8th ed. *ubuqe,(owaM :indal l$=untPublishing 0ompany.
Ako :, +icolai T, *urand *,7rontons B. //6. %icro-
phase separation e"plainsthe abrupt structuralchange of denaturedglobular protein gels onvarying ionic strength orthe p=. @oft %atter >M8/55G83.
Antmann B, Ares B,@alvador A, Earela P,'is&man @. /33."ploring and e"plainingcreaminess perceptionMconsumers) underlying
concepts. 1 @ens @tudFM8/G;.
Audebrand %, opers %-=,iaublanc A. /35.*isappearance of intermolecular beta-sheetsupon adsorption of beta-lactoglobulin aggregatesat the oil-water interfacesof emuls ions . 'ood=ydrocoll 55M3;?G?>.
7aldwin %D, Toda I,+akagita T, 9)0onnell%1, :lasing :0, %isakaT, dwards @E, M 66G55.
7andyopadhyay P, BhoshA:, 0handrasekhar B./3. ecentdevelopments on
polyphenol-proteininteractionsM effects on teaand coffee taste,antio"idant properties andthe digestive system. 'ood'unct 5M >6GF/>.
7arbana 0, Pere&J %*./33. (nteraction of -lactalbumin with lipidsand possible implicationsfor i ts emuls ifying
propertiesa review. (nt*airy 1 3M ;;G83.
7eecher 1D, *rake %A,>5-F/.
7erry T:, Iang N,'oegeding A. //6.'oams prepared fromwhey protein isolate andegg white proteinM .0hanges associated withangel food cakefunctionality. 1 'ood @ci;8M F6-;;.
7irdi :@. //6. =andbookof surface and colloidalchemistry. 5rd ed. 7ocaaton, '.
*ickinson . 366. Anintroduction to foodcolloids. 9"ford, C:M9"ford Cniversity Press.*ickinson . /3.muls ion gels M thestructuring of soft solidswith protein-stabili&ing oil
droplets. 'ood
=ydrocoll ?M8G83.
rickson 1A, 1alaie %,obertson *=, /.
'oegeding A, *avis 1P./33. 'ood proteinfunctionalityM acomprehensiveapproach. 'ood=ydrocoll >M3?>5GF8.
'oegeding A, amsey@. 36?;. heologicaland water-holding
properties of gelledmeat batters containingiota carrageenan, kappacarrageenan or "anthangum. 1 'ood @ci>M>86G >5.
'oegeding A, Einyard01, ssick B, Buest @,0ampbell 0. /3>.Transforming structural
breakdown into sensoryperception of te"ture. 1Te"ture @tud 8FM3>G;/.
'ran&en :
-
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%cBuffey %:, pting :5M53?G6/.
+icolai T, *urand *. /35.0ontrolled food proteinaggregation for newfunctionality. 0urr 9pin0olloid (nterf @ci 3?M86->F.
9)0onnell 1, 'o" P'. //3.@ignificance andapplications of phenoliccompounds in the
production and quality ofmilk and dairy productsM areview. (nt *airy 133M3/5G/.
Pascua I, :oc =, 'oegedingA. /35. 'ood structureMroles of mechanical
properties and oralprocessing in determiningsensory te"ture of softmaterials. 0urr 9pin0olloid (nterf @ci 3?M58G55.
Pernell 0D, ->3.Peter P+, 7ell D. 365/.
+ormal and modifiedfoaming properties ofwhey-protein and egg-albumin solutions. (ndustng 0hem M338-?.
Poms , :lein 0G>.
Tanford 0, eynolds 1.//3. +ature)s robots ahistory of proteins.9"ford, C:M 9"ford Cni-versity Press.
Taylor A1, . Cbbink
1, 7urbridge A, %e&&enga
. //?. 'ood structure and
functionalityM a soft matter
perspective. @oft %atter8M3>F6G?3.
Cdenigwe 00, Aluko ./3. 'ood-protein-der ived bioact ive
peptidesM production,process-ing, andpotential healthbenefits. 1 'ood @ci;3M33G8.
Crbonaite E, de 1ongh==1, van der .
Eisschers D, 1acobs
%A, 'rasne lli 1,=ummel T, 7urgering%, 7oelruk A%.//F. 0ross-modalityof te"ture and aroma
pe
Da
D
a
Ian
Ian
-
7/26/2019 Avances Traducido
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(:Food(he4istr
$ntroducci&n
@e podrSa argumentar
que las proteSnas sonpolSmeros ms
verstiles de la
biologSa.
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7/26/2019 Avances Traducido
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e"tensiUn de su
actividad biolUgica,
por
siendo componentes
de estructuras de
alimentos que la
biologSa no habSan
previsto, o pueden
unirse a una variedad
de molWculaspequeYas y alterar su
disponibilidad
durante la ingestiUn.
Cn eemplo de
proteSnas que
funcionan en los
alimentos como una
e"tensiUn de su
estructura y funciUn
biolUgica es en&imas.
el instituto de tecnolog?a de ali4entos
mailto:[email protected]:[email protected] -
7/26/2019 Avances Traducido
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aYadir con la
intenciUn de formar
estructuras coloidales
especSficas, pero
tienen un efecto
secundario no
deseado. Por
eemplo, en las
bebidas que
contienen proteSnas
de suero se austa el
p= a un p= de 5. a
5.> para aumentar laestabilidad coloidal
del sol de proteSnas,
pero tambiWn imparte
astringencia
indeseable 7eecher
y otros //?!. Cn
obetivo ideal serSa
tener una Vetiqueta
funcionalidadV en un
ingrediente proteSna
alimentaria que
proporciona medidas
de la eficacia del
ingrediente serSa enuna gama de
aplicaciones de
alimentos.
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pueden estar
implicados.
structuras vistos en
la microescala
histUricamente han
sido el foco de
Vanlisis de la
estructura del
alimentoV, por
eemplo vWase la
revisiUn de =eerte
/38!, pero un
enfoque ms recientey completo de la
estructura del
alimento es para
asumir la perspectiva
de la fSsica y ver las
estructuras de
materia blanda a
travWs de escalas de
longitud Cbbink y
otros //?# van der
@man /3!.
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:itabatake //3# 0
Akir y otros /3!.
l papel de
mesoestructuras se
puede ilustrar
adicionalmente por
los eemplos de la
leche y los productos
crnicos.
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Nuevo $odelo de
Funcionalidad delas !o"e#nas de losAli$en"os
temen al afirmar que
V
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n otras palabras,
Peter y 7elltrabaaron en el
hipUtesis que si
pudieran mostrar
cUmo producir
espumas de proteSna
de suero con
propiedades
similares a las de
huevo espumas
blancas, a
continuaciUn, suero
de leche pro-
proteSnas podrSan ser
sustituidos por laclara de huevo. ste
es un enfoque lUgico,
aunque a menudo
incompleto que ser
discutido en las
secciones siguientes.
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rodeado por un
fluido!. 9tras
funcionalidades eran
un poco ms
ambiguo y depende
de las pruebas
empSricas especSficas
solubilidad,
capacidad de
retenciUn de grasa,
capacidad de
retenciUn de lSquido,
y la absorciUn deagua!. Adems,
algunos se asociaron
con sensorial la
percepciUn de las
estructuras
macroescala dure&a,
masticabilidad,
cohesiUn y
adherencia!. @i una
proteSna tiene una
funciUn y la funciUn
es debido a aspectos
fSsicos quSmicos $ de
la estructura de laproteSna o
mesostructura
formado, entonces
debe haber una
manera de ensayo
que funciUn. =all
366F! propone que
la funcionalidad de la
proteSna se puede
anali&ar por mWtodos
que cubren la
solubilidad, la
viscosidad, la
gelificaciUn, laformaciUn de espuma
y de estabili&aciUn,
la formaciUn de
emulsiUn y
estabili&aciUn, el
agua y propiedades
de sueciUn de grasa,
y la hidrofobicidad
de la superficie.
stos se pueden
agrupar en molecular
hidrofobicidad y
viscosidad!,
%olecular ymesoestructura
solubilidad de una
proteSna en polvo!, y
mesoestructura gel,
espuma, emulsiUn, y
la grasa y retenciUn
de agua! Propiedades
de escala. sto es
vlido en general
como un punto de
comparaciUn que es
independiente de una
aplicaciUn de
alimento especSfico.@in embargo, estas
pruebas deben cubrir
una gama de
condiciones de
soluciUn
concentraciUn de
proteSnas, p=, iones,
y la fuer&a iUnica!
para ser lo
suficientemente
robusta como para
cubrir una amplia
gama de aplicaciones
de alimentos.
-
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proteSna. sto se
logra mediante la
definiciUn de la
funcionalidad en
base a la
funcionalidad que
determina la escala
estructural crStica
'igura 3!.
l modelo consta de
5 escalas
estructurales ypropiedades
funcionales
asociados a cada
escala estructural.
-
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geles, emulsiones, y
espumas son
propiedades
procedentes de
mesoestructuras.
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Puede ser muy
simple, como en un
gel de gelatina, o las
compleas estructuras
que se encuentran en
los helados, pasteles,
o queso, para
nombrar unos pocos.
Adems, hay algunos
alimentos cuando el
tratamiento produce
una estructura inicial
VverdeV, pero su
estructura de destino
es el resultado de
cambios lentos
durante el
enveecimiento,
como por eemplo en
el queso.
-
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formando unapelScula interfacialemulsiUn o espuma!o como parte de lafase continua sol,emulsiUn o espuma!Tabla 5!. stosignifica que varios
parmetros necesitanser determinados enla evaluaciUn de lafuncionalidad de la
proteSna, incluso enun sistema coloidalsencillo
+mulsiones
Cno de los mWtodos
ms comunes para la
evaluaciUn de la
funcionalidad de la
proteSna en una
emulsiUn de aceite en
Agua es comparar
varias proteSnas a
concentraciones
donde hay suficiente
gotitas de aceite para
la capa de proteSna y
mSnima que queda en
la fase dispersa. @i
una proteSna produce
gotas ms pequeYas,
]tiene una capacidad
emulsionante
superiorH @S, si su
obetivo es
simplemente
producir pequeYasgotas. @in embargo,
la mayorSa de las
emulsiones tienen
que ser estable
durante un tiempo
prolongado, por lo
que la estabilidad del
sistema es a menudo
ms importante que
el estado fSsico
inicial es decir, la
distribuciUn de
tamaYo de las
gotitas!.
=acen pequeYas
gotas de una
emulsiUn ms
estableH @S, si el
mecanismo de
desestabili&aciUn
sUlo se basa en la
tasa de formaciUn de
la crema de las
gotitas de aceite
como se describe en
la
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compleos y no se ha
descrito para Wl una
prueba simple o
propiedad fSsica.
Tomemos por
eemplo la capacidad
de deformar un
huevo blanco de
merengue estable.
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de suero produce un
pastel que se hunde
tras la cocciUn
Pernell y otros
//!. Ambas
proteSnas tienen
capacidades
relativamente
similares para formar
espumas hXmedas
Iang y 'oegeding
/3/, /33! y tienen
transiciones
estructurales
similares cuando se
calienta 7erry y
otros //6!. @e
diferencian cuando la
harina y el a&Xcar se
doblan en la espuma
para hacer la masa
del pastel. sto inicia
la desestabili&aciUnde la espuma de
proteSna de suero y
tiene un efecto
mSnimo sobre la
espuma de clara de
huevo 7erry y otros
//6!. n este caso,
la diferencia
fundamental en la
funcionalidad de la
proteSna no se
observa hasta una
mesoestructura quees un me&clado con
otros ingredientes
para formar la masa
colecciUn de
estructuras meso y
las molWculas para
formar la
microestructura!.
-
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%cBuffey y otros
//>!. Cna bebida de
calidad aceptable es
uno que, despuWs del
proceso de cocciUn
tiene agregados de
proteSnas que crean
la claridad, la
viscosidad, y
sensaciUn en la boca
deseada. structuras
producidas a partir
de la agregaciUn de
pro-proteSna
interacciones
moleculares escala
que producen
estructuras de
mesoescala!
dependern de p=,
fuer&a iUnica, el tipo
de iones y la
concentraciUn de
pro-proteSna, ademsde otras molWculas
tales como a&Xcares
+icolai y *urand
/35!.
-
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mayorSa de las
proteSnas son de a
unos pocos
nanUmetros de
dimetro y
sedimentaciUn serSa
tan lento como para
no ser un factor con
una vida Xtil de hasta
un aYo o . Por lo
tanto, la formaciUn
de una red de
precipitado o gelvisible depender en
el tamaYo y la
cantidad de
agregados formados
durante el
procesamiento
tWrmico y su
propensiUn a sufrir
agregaciUn
secundaria a
temperaturas de
almacenamiento
yan y otros /35!.
n teorSa, estoselementos deben ser
predecibles en
funciUn de cUmo la
estructura molecular
capacidad de formar
interacciones
intermolecular
durante el
procesamiento
tWrmico! determina el
tipo de
mesoestructura
partScula! formado.
-
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a F` w $ v, a p= ;!
produo soles, geles
homogWneos, micro-
fase separada geles,
o precipita como la
concentraciUn de
+a0l se incrementa
de /,/3 a 3 % Ako y
9T=-@ //6!. l
diagrama de estado
que presenta la
relaciUn entre la
concentraciUn de+a0l y la
concentraciUn de
proteSnas a un p= de
;,/ muestra una
concentraciUn
mSnima para la
gelificaciUn de
alrededor de ` w $
v# sin embargo, esto
puede variar con un
cambio en el p=.
Cn enfoque integral
para una proteSna
individual serSagenerar diagramas de
estado que cubren
una amplia gama de
valores de p= y las
concentraciones de
proteSna ,los puntos
crSticos, y luego
evaluar cUmo otros
factores, tales como
ingredientes
aYadidos, cambiar
los puntos crSticos en
el diagrama de
estado.%acroescala
propiedades
asociadas con los
geles incluyen
apariencia
transparente u
opaco!, la firme&a
fuer&a $
deformaciUn!, fuer&a
la fuer&a para
provocar la fractura!,
y la retenciUn de
agua. stos son
pertinentes a laapariencia y la
estabilidad del
producto alimenticio
y, posiblemente,
asociados con la
percepciUn sensorial
de la te"tura
@&c&ensiak //#
Pascua y otros /35!.
@e relacionan con
elementos en
molecular y
mesoscales van
Eliet //# van den7erg y otros //;a,
b!. Cn eemplo
reciente es el
halla&go de que la
escala de longitud
micrUmetro
mesoestructura! es
el agua una factor
mas determinante
por la pWrdida de los
geles de proteSna de
soa bao
deformaciUn
Crbonaite y otros
/38!.
Cn desafSo Xnico,con propiedades
fSsicas de los geles
de alimentos es que
hay numerosos
mWtodos disponibles
para determinar de
retenciUn de agua,
las propiedades
reolUgicas o para
fracturas# sin
embargo, la
relevancia a la
percepciUn durante el
consumo puede serms complea. sto
requiere una
comprensiUn de
cUmo las molWculas y
estructuras de
alimentos son
percibidos por los
seres humanos.
$nterfa! con
Fisiolo)a umana
=ay varias
propiedadesfuncionales
moleculares que son
importantes para los
consumidores en
relaciUn con los
aspectos hedUnicos y
de salud de las
proteSnas.
-
7/26/2019 Avances Traducido
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de la funcionalidad
de la proteSna. @in
embargo, como se
mencionU
anteriormente, los
compuestos de sabor
de uniUn es una
forma en que las
proteSnas pueden
alterar el aroma
general de un
alimento. !.
-
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se pueden austar a
las transformaciones
especSficas durante el
preprocesamiento
oral. n estos
eemplos , 3 factor
clave es la
coalescencia de las
gotitas de aceite
durante el
procesamiento oral.
sto sugiere que,
adems de lacomprensiUn de
cUmo formar y
estabili&ar
mesoestructuras
coloidales,
propiedades que son
esenciales para la
aceptaciUn del
consumidor en la
compra, las
transformaciones en
la mesoestructura
durante el
procesamiento porvSa oral deben ser
entendidos con
respecto a que
suscitan sensaciones
de te"tura
'oegeding y otros
/3>!.
bseraciones
Finales
-
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ilustra con pastel de
ngel, no pueden
aparecer diferencias
proteSna de funciUn-
lidad hasta que los
mesoestructuras se
me&clan y se
procesan en la etapa
final de la
producciUn de
alimentos.
Cna analogSa sepuede e"traer con la
determinaciUn de la
bioactividad de un
polifenol. Cna
molWcula aislada
puede mostrar
actividad quSmica,
por eemplo la
actividad
antio"idante o uniUn
a una proteSna de
interWs, que puede
ser demostrado de
forma concluyenteen la escala
molecular.
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rickson 1A, 1alaie %,obertson *=, /.
'oegeding A, *avis 1P./33. funcionalidad de la
proteSna alimentariaM unenfoque integral. 'ood=ydrocoll >M 3?>5-3?F8.
'oegeding A, amsey@. 36?;. . ->3.
Peter P+, 7ell D. 365/.normal y propiedadesespumantes modificadas desoluciones de albXmina dehuevo, proteSna de suero y.
(ndust ng 0hem M 338-33?.
Poms , :lein 0
-
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clases quSmicas. (mpactode la proteSna en la
percepciUn del olor de lavainillina y eugenol. -3>.
@ammis 1. luso de diagramas de estado
para predecir la estabilidad
coloidal de las bebidas deproteSna de suero de leche.
1 Agric 'ood 0hem F5M855>-88.
Dalstra P. //5.'isicoquSmica de losalimentos. +ew Iork, +IM%arcel *eckker, (nc.
Iang N, 'oegeding A.
/3/. fectos de lasacarosa en proteSna declara de huevo y proteSnade suero espumasM factoresque determinan las
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