Avances Traducido

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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


3/47

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


4/47

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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6/47

(: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


7/47

Figure +9Protein functionalit &ased on lengthscale of structural ele4ents deter4iningfunctionalit%

()37) Journal of Food Scienceol% 1*, Nr%+), )*+5


Table 2Molecular scale functional

properties of proteins.

Molecular property

0olor %yoglobin@weetness Thaumatinn&ymatic activity 0hymosin


8/47

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


9/47

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.


10/47

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


11/47

(:

ol% 1*, Nr% +), )*+5 Journal of FoodScience ()370

(:Food(he4istr


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.


12/47

$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)


13/47

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


14/47


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


15/47

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


16/47


17/47

(:Food(he4istr

ol% 1*, Nr% +), )*+5 Journal of FoodScience ()375


18/47


(: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.


19/47

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


20/47

c

a

A

@u


21/47

()373 Journal of Food Scienceol% 1*, Nr%+), )*+5


22/47


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 :


23/47

%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


24/47

(:Food(he4istr

$ntroducci&n

@e podrSa argumentar

que las proteSnas sonpolSmeros ms

verstiles de la

biologSa.


25/47

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]


26/47

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.


27/47

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!.


28/47

: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.


29/47

Nuevo $odelo de

Funcionalidad delas !o"e#nas de losAli$en"os

temen al afirmar que

V


30/47

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.


31/47

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.


32/47

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.


33/47

geles, emulsiones, y

espumas son

propiedades

procedentes de

mesoestructuras.


34/47

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.


35/47

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


36/47

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.


37/47

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!.


38/47

%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!.


39/47

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.


40/47

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.


41/47

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. !.


42/47

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


43/47

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.


44/47


45/47

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


46/47

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


47/47

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