Food Hydrocolloids xxx (2016) 1e8

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Food Hydrocolloids
journal homepage: www.elsevier.com/locate/foodhyd

Hydrocolloid-food component interactions

Zhiming Gao a, b, Yapeng Fang a, b, *, Yiping Cao a, Hua Liao a, Katsuyoshi Nishinari a, b,
Glyn O. Phillips a
a
Glyn O. Phillips Hydrocolloid Research Centre, School of Food and Pharmaceutical Engineering, Faculty of Light Industry, Hubei University of Technology,
Wuhan, 430068, China
b
Hubei Collaborative Innovation Centre for Industrial Fermentation, Hubei University of Technology, Wuhan, 430068, China

a r t i c l e i n f o a b s t r a c t

Article history: Hydrocolloids can greatly influence the structure and functionalities of modern foods, mainly due to
Received 23 June 2016 their interactions with other components present in complex food matrices. This review outlines three
Received in revised form main categories of hydrocolloid-food component interactions: hydrocolloid-ion, hydrocolloid-small
30 August 2016
molecule, and hydrocolloid-hydrocolloid interactions. Examples are given to illustrate the impact of the
Accepted 31 August 2016
Available online xxx
interactions on the structure, stability, functional properties of foods, and their utilizations in food
technologies such as separation/purification, gelation, emulsification, and encapsulation etc.
© 2016 Published by Elsevier Ltd.
Keywords:
Hydrocolloid
Food component
Interaction
Structure
Functionality

1. Introduction interactions are ubiquitously present between macromolecules,

Today, the consumer is becoming increasingly fastidious in
demanding food products with improved quality and functionality.
Traditional approaches to improve food quality and functionality,
by simply exploring the physicochemical and nutritional/functional
properties of individual food components, have reached a ceiling.
On the other hand, scientists have realized that food is a typical soft
matter system containing multi-components, multi-phases and
multiple length scales (Mezzenga, Schurtenberger, Burbidge, &
Michel, 2005; Ubbink, Burbidge, & Mezzenga, 2008; van der
Sman, 2012). A more profound exploration of food quality and
functionality needs the use of soft matter approaches. Specifically,
it should be realized on the basis of a better understanding of food
component interactions and a controlled food structuring over
multiple length scales.
Food products contain complex and variable components such
as water, carbohydrates, proteins, lipids, minerals, colorants, fla-
vors, and other functional substances. In such systems, molecular
* Corresponding author. Glyn O. Phillips Hydrocolloid Research Centre, School of
Food and Pharmaceutical Engineering, Faculty of Light Industry, Hubei University of
Technology, Wuhan, 430068, China.
E-mail address: fangypphrc@163.com (Y. Fang).
small molecules and ions, and have different interactivities
including electrostatic interaction, hydrogen bonding, hydrophobic
interaction, coordination force, and p-p stacking etc. These in-
teractions usually have dual effects on quality and functionality of
foods. They can cause undesired properties such as reduced solu-
bility and stability, but also can enhance the quality and function-
ality of foods (A. R. Patel, 2013).
Hydrocolloids, particularly the naturally occurring macromo-
lecular proteins and polysaccharides, constitute the major cate-
gories of food structuring agents and play critical roles in conferring
food structure and stability. Broadly speaking, starch is also a type
of polysaccharides, which however is often considered separately
due to its special role as an energy store. These hydrocolloids are
now widely used in the food industry to perform a number of
functions including thickening and gelling aqueous solutions, sta-
bilizing foams, emulsions and dispersions, inhibiting ice and sugar
crystal formation and the controlled release of flavors, etc
(Williams & Phillips, 2009). Interactions of hydrocolloids with
other food components present in food formulation dictate their
molecular assembly over multiple length scales and consequently
the final structure of food products, thus having great impacts on
the texture, nutritional and functional aspects of foods (Fig. 1) (Ai
et al., 2015).
Here, we outline three main categories of hydrocolloids-food

http://dx.doi.org/10.1016/j.foodhyd.2016.08.042
0268-005X/© 2016 Published by Elsevier Ltd.

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2 Z. Gao et al. / Food Hydrocolloids xxx (2016) 1e8
Fig. 1. Hydrocolloids as structuring agents contribute to the texture, nutritional and
functional properties of foods.
components interactions including hydrocolloids-ions (salts, min-
erals etc.), hydrocolloids-small molecules (colorants, flavors, fatty
acids, vitamins, phytochemicals etc.), and hydrocolloids-
hydrocolloids (proteins, polysaccharides etc.) interactions. Exam-
ples, particularly those from our studies, are given to illustrate how
the interactions are explored and utilized by food technologists to
control the quality and functionality of foods.
2. Hydrocolloids-ions interactions
Mineral elements are present in relatively low concentrations in
foods, but they play key functional roles. They are either inherently
contained in food materials or introduced during processing and
cooking. For instance, calcium is inherently present in milk. It is
essential for structuring casein micelles and is the major source of
calcium intake in our daily life. In contrast, sodium is mainly
introduced into foods during cooking or processing. It is a deter-
mining factor for the taste and shelf life of foods, but high intake is
related to chronic diseases such as cardiovascular diseases. Mineral
elements exist in many different chemical forms in foods, including
compounds, complexes and free ions. Among these, free ions are
the most reactive species due to high solubility (Damodaran,
Parkin, & Fennema, 2008), and therefore readily interact with hy-
drocolloids through electrostatic interactions or coordination, etc.
Monovalent ions such as Hþ, Naþ, Kþ and I have been reported
to interact with hydrocolloids through specific and non-specific
interactions. These ions constantly surround protein and poly-
saccharide molecules in solution, forming a layer of “ion atmo-
sphere” and affecting the solubility, rheological and gelling
properties of proteins and polysaccharides via electrostatic inter-
action or hydration effect (Cao, Fang, Nishinari, & Phillips, 2016). Hþ
ions at low pHs often cause the protonation of carboxylic groups
(pKaz3.5), and induce a weak gel formation in polysaccharides
carrying carboxylic groups, such as in pectin (Strom, Schuster, &
Goh, 2014), alginate (Elliott, Steckbeck, Murray, & Erk, 2013), hya-
luronan (Luan, Wu, Zhang, & Wang, 2012) and carboxymethyl
cellulose etc (Hakert, Eckert, & Muller, 1988). Hydrogen bonding
and/or hydrophobic interaction between the polysaccharide chains
after protonation were considered to be the driving force for
network formation (Y. Fang et al., 2009; Strom et al., 2014). Both Kþ
and I ions were reported to bind specifically to the helical state of
k-carrageenan, promoting and stabilizing double helix formation
(Djabourov, Nishinari, & Ross-Murphy, 2013; Viebke, Borgstrom,
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j.foodhyd.2016.08.042
Carlsson, Piculell, & Williams, 1998). The difference is that Kþ ions
facilitate the subsequent aggregation of the double helices and thus
gelation, while I ions tend to prevent them (Ikeda & Nishinari,
2001).
Multivalent ions such as Mg2þ, Ca2þ, Ba2þ, Fe2þ, Cu2þ, Zn2þ, Fe3þ
and Al3þ have the ability to form complexes with polysaccharides,
proteins and lipids. Due to their multivalency, they can bind to
multiple oxygens simultaneously and function as cross-linkers for
polysaccharides and proteins (Damodaran et al., 2008). The most
typical example is the interaction between Ca2þ and polyuronate
alginate and pectin. Two sequences of Ca-active sites on alginate
(i.e., guluronate units) or pectin (i.e., galacturonate units) chains
coordinate with Ca2þ ions, forming dimers that resemble “egg-box”
(Fang, Al-Assaf, Phillips et al., 2007; Fang, Al-Assaf, Sakata, Phillips,
Schultz, & Monnier, 2007). The egg-box structure acts as cross-
linking junction zones, leading to Ca-induced gel formation of
alginate or pectin. The “egg-box” model was developed over 40
years ago. Nevertheless, the dynamic process of structural evolu-
tion of egg-box structures was elucidated only recently. Based on
dilute solution characterization using complementary techniques
(Fang, Al-Assaf, Phillips et al., 2007; Fang, Al-Assaf, Sakata et al.,
2007), the binding of Ca2þ ions to alginate was found to involve
distinct multiple steps, namely, monocomplexation, dimerization,
and lateral aggregation (Fig. 2). In particular, the dimerization step
was rather critical, only occurring when the stoichiometry of egg-
box dimer was reached (i.e., Ca/guluronate ¼ 0.25). Borgogna
et al. later proposed a tilted egg-box model (Borgogna, Skjak-Braek,
Paoletti, & Donati, 2013), and argued that the cross-linking of
alginate chains by Ca2þ occurred even when Ca/guluronate < 0.25.
Two alginate chains were held together by loosely bound Ca2þ ions
(Fig. 2), and formed tilted contact points that differed from the
classical egg-box arrangement. The so-called tilted egg-box might
represent a transient state of the cross-linking of monocomplexes,
and should by no means disprove the multiple step mechanism,
particularly, the monocomplexation step. Comparative studies
were conducted on alginate and pectin in terms of their difference
in Ca binding (Y. P. Fang et al., 2008). The dimerization process of
pectin was found to be much less critical than that of alginate, due
to the random distribution of binding sites along pectin chain. A
progressive “dotting” growth of pectin dimers was suggested in
contrast to the critical “zippering” growth of alginate dimers.
Elucidation of the interaction mechanisms of polyuronates with
Ca2þ allows better control of the gelling behavior of alginate and
pectin. An effective way of tuning the gelling kinetics and gel
properties of polyuronates was developed by using low molecular
weight oligoguluronates (GB) (DP < 50) prepared by selective acid
hydrolysis and precipitation (Jorgensen, Sletmoen, Draget, &
Stokke, 2007; Sletmoen, Draget, & Stokke, 2010). Depending on
the Ca concentration regime, GB either inhibited (0.25 < R < 0.6) or
promoted (R > 0.6) the gelation of alginate (Fig. 3a) (Liao et al.,
2015). The inhibitory effect arose from a competitive binding of
GB with alginate for Ca, whereas the promotive effective was due to
an enhanced lateral aggregation of alginate under the mediation of
GB dimers. The modulatory effect of GB on low methoxy pectin was
quite different from that on alginate (Fig. 3b). Interestingly, GB was
found to promote the gelation of low methoxy pectin in low Ca
concentration regime (R < 0.25) where egg-box dimers were not
yet formed. This was presumably attributed to the role of GB as a
cross-linker to bridge two pectin chains, by formation of mixed
tilted egg-box structure with pectin. Since GB was effective in
altering calcium binding behaviors and gel network structure of
polyuronates, it could be potentially used to modify macroscopic
properties, e.g., water holding capacity, of alginate and pectin gels
(Nakauma et al., 2016).
Carrageenans also have diverse binding behaviors with
 Z. Gao et al. / Food Hydrocolloids xxx (2016) 1e8 3

Fig. 2. Binding of Ca2þ to alginate: multiple step mechanism (left) proposed by Fang et al. and tilted egg-box mechanism (right) proposed by Borgogna et al. (Borgogna et al., 2013).
Reproduction with permission from ACS.

Fig. 3. Modulation of the gel elasticity of alginate (ALG) (a) and low methoxy pectin (LMP) (b) by addition of oligoguluronate (GB). G'sat is the saturated storage modulus of ALG or
LMP gels induced by Ca-EDTA under the hydrolysis of GDL. R is the molar ratio of calcium to guluronate/galacturonate unit ([Ca]/[G]), where [G] includes the contributions both from
GB and ALG or LMP.

multivalent ions, which vary according to the number of sulphate
groups carried by a repeating unit. k-Carrageenan, carrying one
sulphate group in a repeating unit, exhibited specific binding with
monovalent cations such as Kþ, Csþ and Rbþ. In comparison, i-
carrageenan, which has two sulphate groups in a repeating unit,
was more sensitive to divalent cations such as Ca2þ (Djabourov
et al., 2013). Intriguingly, our recent study showed that l-carra-
geenan with three sulphate groups in a repeating unit bound spe-
cifically to trivalent cations including Fe3þ and Al3þ (Fig. 4). Direct
addition of the trivalent ions into l-carrageenan solution caused
solid precipitation, while slow diffusion by dialysis induced weak
gel formation (Fig. 4a). ITC analysis gave an exact stoichiometry of
1:1 (M3þ/repeating unit), and a binding constant of 8.1  103 and
5.6  103/M for Al3þ and Fe3þ, respectively. In view of their ability to
bind to multivalent cations, i-carrageenan and l-carrageenan could
be potentially used to sequester prooxidant metal ions, thus
inhibiting lipid oxidation in lipid-containing foods.
Proteins exhibited even richer interactions with ions, due to the
presence of specific binding sites in protein hierarchical structures.
As aforementioned, the interaction of calcium with casein mole-
cules is fundamentally important for the structuring of casein mi-
celles and the colloidal stability of milks (de Kruif, Huppertz, Urban,

Fig. 4. Weak gel formation of 1% l-carrageenan induced by dialysis against 10 mM AlCl3 at pH 2.3 (a); ITC isotherm for titration of 30 mM AlCl3 into 0.05% l-carrageenan in 5 mM
pH 2.3 phosphate buffer (b).

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4 Z. Gao et al. / Food Hydrocolloids xxx (2016) 1e8
& Petukhov, 2012). Ions have a significant influence on the aggre-
gation, gelation and emulsification of proteins (Nishinari, Fang,
Guo, & Phillips, 2014), and thus are important for production of
protein-based foods. For instance, the traditional approach to
making tofu utilizes the interaction of soy proteins with calcium
sulphate, which causes the cross-linking and coagulation of the
proteins. Proteins after amyloid fibrillation were shown to have
increased binding ability with metal ions, particularly with transi-
tional metal (e.g., Cu2þ, Fe3þ, and Zn2þ) (Guzzi, Rizzuti, Labate,
Zappone, & De Santo, 2015). This has led to interesting applica-
tions such as heavy metal removal for water purification and nano-
catalysis (Bolisetty & Mezzenga, 2016; Rufo et al., 2014), based on
food-grade fibrillar proteins. In spite of the structural similarity of
protein fibrils with amyloids causing amyloidosis diseases, the
complete digestion of b-lactoglobulin fibrils in simulated gastric
fluids has been confirmed (Bateman, Ye, & Singh, 2010).
3. Hydrocolloids-small molecules interactions
Food contains numerous small molecules, including colorants,
flavors, fatty acids, vitamins, biosurfactants, and phytochemicals.
These small molecules are either hydrophilic or hydrophobic, and
possibly interact with hydrocolloids through hydrogen bonding
and/or hydrophobic interaction. The interactions significantly alter
the organoleptic, functional and nutritional properties of foods.
Colorants or pigments are often added into food products to
create color effects. The presence of hydrocolloids can cause sta-
bilization or destabilization of colorants, and change their optical
properties. In beverages, gum arabic was found to destabilize azo
colorants (sunset yellow, azorubine, and allura red) and cause
precipitation. Our study demonstrated that the instability origi-
nated from the interaction between gum arabic and azo colorants,
mediated or bridged by divalent alkaline earth metals such as Mg2þ
and Ca2þ (Fang, Al-Assaf, Phillips et al., 2007; Fang, Al-Assaf, Sakata
et al., 2007). On the other hand, for example, alginate and pectin in
jam or jelly products were found to improve the physical and
chemical stabilities of anthocyanin (Hubbermann, Heins,
Stoeckmann, & Schwarz, 2006). This was possibly due to the exis-
tence of molecular binding between anthocyanin and the poly-
uronates (Fernandes, Bras, Mateus, & de Freitas, 2014).
Hydrocolloids were also used intentionally to tune the coloring or
optical properties of colorants. By exploring the hydrophobic
interaction with zein, water-insoluble colorant curcumin and
water-soluble colorant indigocarmine were co-incorporated into
colloidal zein particles using anti-solvent precipitation method (A.
R. Patel, Heussen, Dorst, Hazekamp, & Velikov, 2013). This gave a
series of color blends of different mixing ratios, exhibiting tunable
colors in yellow-green-blue range.
Flavor is one of the most important attributes determining the
acceptance of foods by the consumer. The interactions of hydro-
colloids with flavor compounds significantly influence flavor
retention, release and perception. Although the major effect of
hydrocolloids seems to be a limitation on flavor diffusion by vis-
cosification (Godshall, 1997), there exist a range of reversible and
irreversible interactions between hydrocolloids and flavors
(Guichard, 2002). Proteins were well known to form covalent
binding with aldehydes. They could also bind flavors reversibly
through hydrophobic pockets. These properties were successfully
used to decrease odor perception or mask off-flavors in certain food
products. Polysaccharides can also modify flavor release and
perception. Starch is one of the most studied polysaccharides
regarding its ability to bind flavors (Guichard, 2002). The formation
of amylose-flavor inclusion complexes has been well demonstrated
by X-ray diffraction.
Phytochemicals, such as polyphenols, flavonoids, carotenoids,
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and phytosterols, are food supplements with numerous health
benefits. Their interactions with hydrocolloids have been
frequently used to overcome solubility, stability and bioavailability
issues of the phytochemicals (McClements, Decker, Park, & Weiss,
2009). Caseins were found to form complexes with lipophilic cur-
cumin through hydrophobic interaction. Curcumin were efficiently
entrapped in the core of casein nanoparticles, leading to 4 decades
increase in water solubility and a significant improvement in bio-
logical activity as evaluated by antioxidant and cell proliferation
assays (Pan, Zhong, & Baek, 2013). The hydrophobic interaction was
also used for synthesis of zein-curcumin colloidal nanoparticles by
anti-solvent precipitation approach. The particles were stable
against gastro-intestinal conditions, and exhibited excellent
mucoadhesion property (A. Patel, Hu, Tiwari, & Velikov, 2010). The
interactions of hydrocolloids with phytochemicals can also signif-
icantly modify the functionalities of hydrocolloids. Patel et al.
demonstrated a colloidal complexation between methylcellulose
and tannic acid, driven by hydrophobic interaction and hydrogen
bonding (Patel, Ten-Hoorn, Hazekamp, Blijdenstein, & Velikov,
2013). The complexation resulted in loss of thermoreversible gel-
ling property, improvement of emulsifying property, and
enhancement of foam-stabilizing property of methylcellulose.
Another example from our study showed that the addition of a
small amount of epigallocatechin gallate (EGCG) induced a ther-
moreversible gelation of tamarind seed xyloglucan (TSX) (Nitta,
Fang, Takemasa, & Nishinari, 2004). Hydrogen bonding between
EGCG and TSX played a crucial role in the formation of gel junction
zones.
Other biologically relevant small molecules such as fatty acids,
bile acids and vitamins were also found to exhibit diverse in-
teractions with hydrocolloids. Using electron paramagnetic reso-
nance (EPR), we revealed a binding of free fatty acids with gum
arabic (Y. Fang, Al-Assaf, Phillips, Nishinari, & Williams, 2010),
which was driven by hydrophobic interaction and ionic hydrogen
bonds (Fig. 5). The interaction was attributed to the presence of
protein moieties in gum arabic. This binding phenomenon might
explain the role of gum arabic retarding lipid digestion, since gum
arabic at the lipid interface could prevent the transport of lipolysis
product fatty acids. Similarly, polysaccharide b-glucan was found to
have dynamic interactions with bile salts (Mikkelsen et al., 2014),
which might be related to its role in lowering the blood plasma
cholesterol level in humans. With regards to proteins, Livney et al.
reported that b-lactoglobulin and casein can serve as natural
Fig. 5. Broadening of EPR spectra of 5-DSA with increasing gum arabic concentration,
revealing the binding of gum arabic with fatty acid.
 Z. Gao et al. / Food Hydrocolloids xxx (2016) 1e8 5

nanovehicles for hydrophobic nutraceuticals, i.e., u-3 poly- the phase separation induced molecular fractionation can be used
unsaturated fatty acid and vitamin D (Haham et al., 2012; Zimet & to separate/purify functional components from polydisperse
Livney, 2009). This merit was due to the hydrophobic binding of the hydrocolloids.
nutraceuticals to proteins, enhancing water dispersibility and Segregative phase separation was also used to design micro-
providing protection against oxidation. Diarrassouba et al. (2015) structure, texture and mechanical properties of food products.
reported that self assembly structures of b-lactoglobulin and egg Depending on phase volume ratio, segregative phase separation
white lysozyme developed using electrostatic interaction could can result in totally different microstructures, varying from
efficiently entrap vitamin D3, and serve as a potential food-grade dispersed microstructure to bicontinuous microstructure. This was
vehicle for bioactives in the formulation of food products. well illustrated by Schorsch et al. using micellar casein-locust bean
gum systems (Fig. 7) (Schorsch, Clark, Jones, & Norton, 1999). The
4. Hydrocolloids-hydrocolloids interactions different microstructures yielded totally different mechanical
properties.
Hydrocolloids-hydrocolloids interactions here refer to the non- Associative phase separation occurs between two hydrocolloids
covalent interactions between food macromolecules, including where heterotypic interaction is enthalpically more favorable than
proteins, polysaccharides and starches. Since they are the major homotypic interactions. This type of phase separation leads to the
structuring agents of food products, their interactions profoundly enrichment of two hydrocolloids in one phase, leaving the other
affect food structural formation and consequently their texture, phase depleted. Associative phase separation often happens be-
stability and functionalities. In many cases, individual hydrocolloid tween two oppositely charged hydrocolloids, e.g., an ionic poly-
cannot provide required properties and consistency in food for- saccharide and a protein. Protein/polysaccharide associative phase
mulations, and combination of hydrocolloids is employed. When separation is also known as complex coacervation, where electro-
two hydrocolloids are mixed, it is unusual for each to behave static interaction is the prevalent primary interaction that governs
exactly in the same way as it would be in the absence of the other phase behaviors. There have been many attempts to understand
hydrocolloid. Due to the low entropy gain during mixing of hy- protein/polysaccharide complex coaveration at the molecular level
drocolloids, phase separation is more often observed than to elucidate its detailed mechanism and structural transitions. A
compatible mixture. Thermodynamically compatible mixture only common picture is that the complexation occurs as a two-step
exists under specific conditions such as at very low concentrations,
or when the two hydrocolloids are indeed chemically and struc-
turally very similar. Depending on the nature of interactions, phase
separations between hydrocolloids can be classified into “segre-
gative” and “associative” types (Cao et al., 2015).
Segregative phase separation occurs between two hydrocolloids
where heterotypic interaction is enthalpically less favorable than
homotypic interactions. This type of phase separation leads to the
enrichment of each hydrocolloid in separate phases. Segregative
phase separation often happens between two similarly charged
hydrocolloids, two neutral hydrocolloids, or one charged hydro-
colloid and one neutral hydrocolloid. A typical example is that
between gum arabic and sugar beet pectin. Since both hydrocol-
loids are negatively charged and thus repulsive each other, their
mixing led to phase separation into two layers, the upper layer
being sugar beet pectin-rich phase and the lower layer being gum
arabic-rich phase (Fig. 6a). Interestingly, molecular fractionation of
gum arabic was found accompanying the phase separation (Fig. 6b)
(Mao et al., 2013). With increasing the phase separation extent, that
is, VU/VL, the content of arabinogalactan-protein complex (AGP)
increased by more than two-fold in the gum arabic-rich phase. This
Fig. 7. Phase diagram and microstructures of micellar casein-locust bean gum systems
provided a promising way to the preparation of high-AGP gum at 5  C. Casein phase was stained and appears as bright. Reproduction with permission
arabic with enhanced emulsifying functionality. It is expected that from Elsevier (Schorsch et al., 1999).

Fig. 6. Segregative phase separation of gum arabic and sugar beet pectin (a); Plot of AGP content in gum arabic against phase separation extent as characterized by the ratio of the
volumes of upper phases to lower phases VU/VL (b).

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Fig. 8. Volume-weight mean diameter D [4,3] of freshly prepared CLA emulsions as a function of the concentration of whey protein isolate/gum arabic intramolecular soluble
complexes (a); Normalized oxygen consumption rate R/Sv for CLA emulsions stabilized with different concentrations of whey protein isolate/gum arabic intramolecular soluble
complexes at 40  C with (dot column) and without (blank column) exposure to light (b). R is the oxygen consumption rate, and Sv stands for the specific surface area of CLA
emulsions.

process upon changing pH. Intramolecular soluble complexes are
first formed, followed by intermolecular complexes and insoluble
complexes (Weinbreck, de Vries, Schrooyen, & de Kruif, 2003;
Weinbreck, Rollema, Tromp, & de Kruif, 2004). The formation of
insoluble complexes results in either a liquid-liquid phase separa-
tion (coacervation) or a precipitation depending on the charge
density of the polysaccharide. In a previous study, we established
the phase diagram of protein/polysaccharide complexation in
terms of pH and mixing ratio. Detailed structural transition during
complex coacervation was elucidated, which included five states:
(I) a stable region of mixed individual soluble polymers, (II) a stable
region of intramolecular soluble complexes, (III) a quasi-stable re-
gion of intermolecular soluble complexes, (IV) an unstable region of
intermolecular insoluble complexes, and (V) a second stable region
of mixed individual soluble polymers (Li, Fang, Al-Assaf, Phillips,
Yao, et al., 2012).
Protein/polysaccharide complex coacervation has been widely
used to confer structure and stabilize food products and provide
desired functionalities. For instance, gelatin/pectin electrostatic
complexes were used to create hydrogel particles with similar di-
mensions and functional attributes as starch granules for the design
of low-calorie and low-starch foods (Wu, Degner, & McClements,
2014). The electrostatic complexes between whey protein and
gum arabic were used to microencapsulate different flavor oils, and
were successfully incorporated into cheese products for controlled
flavor release (Weinbreck, Minor, & De Kruif, 2004; Yeo, Bellas,
Firestone, Langer, & Kohane, 2005). Complex coacervation was
also employed to isolate proteins from their mixtures by virtue of
different protein surface charge density. This, for example, resulted
in a separation of bovine serum albumin with 90% purity from a 1:1
mixture with a second protein b-lactoglobulin, by complexation
with hyaluronic acid (Du, Dubin, Hoagland, & Sun, 2014). More
recently, Bosnea et al. found that the encapsulation of lactic acid
bacteria using whey protein isolate/gum arabic electrostatic com-
plexes could significantly improve the probiotic viability against
adverse conditions, and therefore has potential to deliver live
probiotics in low pH foods or fermented products (Bosnea,
Moschakis, & Biliaderis, 2014).

Fig. 9. Electrostatic complexation of type B gelatin/k-carrageenan as affected by the conformational ordering of k-carrageenan upon cooling in the presence of different salts: (a) KCl
and (b) Me4NI. k-carrageenan and gelatin molecules are illustrated in black and red, respectively. The blue and green dots represent Kþ cations and I anions, respectively. (For
interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

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 Z. Gao et al. / Food Hydrocolloids xxx (2016) 1e8
Due to the combined hydrophilic and hydrophobic properties,
protein/polysaccharide electrostatic complexes were seen as novel
emulsifiers and foaming agents, exhibiting excellent interfacial
activities. Using bovine serum albumin/sugar beet pectin as a
model mixture, the correlation between protein/polysaccharide
phase diagram and emulsifying functionality was established (Li,
Fang, Al-Assaf, Phillips, & Jiang, 2012). It was shown that within
the particular region of intramolecular stable complexes, the pro-
tein/polysaccharide mixture exhibited greatly improved emulsion
stability. This was attributed to the cooperative adsorption of pro-
tein and polysaccharide at the interface of emulsion droplets.
Furthermore, the protein/polysaccharide intramolecular complexes
were found to be efficient in stabilizing polyunsaturated fatty acids
both physically and chemically (Yao et al., 2016). At an optimal
emulsifier concentration, whey protein isolate/gum arabic intra-
molecular soluble complexes produced fine and stable conjugated
linoleic acid (CLA) emulsions that could withstand acceleration test
at elevated temperatures. The resultant CLA emulsions showed
much better stability against oxidation, in comparison with those
produced with individual protein or polysaccharide (Fig. 8).
In view of its enormous applications in food technologies, it is
crucial to be able to tune protein/polysaccharide electrostatic
complexation by external parameters such as temperature.
Recently, we found that in type B gelatin/k-carrageenan system the
electrostatic complexation was significantly enhanced by reducing
the temperature till above the coil-helix transition temperature of
gelatin (Wang et al., 2015). This was due to the formation of
extensive hydrogen bonds between the galactose-sulphate resi-
dues in k-carrageenan and the proline residues in gelatin. More-
over, temperature-induced conformational ordering exerted
pronounced effects on the electrostatic complexation of protein
and polysaccharide. The effects could be decomposed into specific
ionic binding and chain stiffening (Fig. 9) (Cao et al., 2016). At the
initial stage of conformational ordering (Step I), electrostatic
complexation could be either dissociated (e.g. Kþ, Fig. 9a) or pro-
moted (e.g. I, Fig. 9b) due to specific binding of differently charged
ions to k-carrageenan. With further progress of conformational
ordering and propagation of k-carrageenan helices (Step II), the
effect of chain stiffening dominated, leading to the dissociation of
electrostatic complexation. Conformational transition of poly-
saccharide therefore seemed to be an effective means to tune the
extent of protein/polysaccharide electrostatic complexation.
Vice versa, protein/polysaccharide electrostatic complexation
was shown to strongly affect the conformational transition of
polysaccharide (Fig. 10). The enthalpy change associated with the
Fig. 10. Enthalpy change DH associated with the conformational ordering of k-carra-
geenan, as affected by the electrostatic complexation with type B gelatin (circle) and b-
lactoglobulin (square) at different mixing ratios. pH ¼ 4.70; KCl ¼ 50 mM; k-carra-
geenan concentration was fixed at 0.15 wt%.
Please cite this article in press as: Gao, Z., et al., Hydrocolloid-food component interactions, Food Hydrocolloids (2016), http://dx.doi.org/10.1016/
j.foodhyd.2016.08.042
7
conformational ordering of k-carrageenan, that is, the extent of
coil-to-helix transition, decreased markedly upon complexation
with increasing amount of type B gelatin and b-lactoglobulin.
Therefore, protein/polysaccharide electrostatic complexation could
be used to control the conformational transition of polysaccharide
and thus its gelling and viscoelastic properties. Using b-lactoglob-
ulin and its hydrolysates, we demonstrated that the influence of
protein/polysaccharide electrostatic complexation on poly-
saccharide conformational transition largely relied on protein
molecular weight (data not published). b-lactoglobulin hydroly-
sates with Mw > 2000 Da suppressed the conformational transition
of k-carrageenan, while those with Mw < 1000 Da tended to pro-
mote and stabilize it. Since protein hydrolysis is a rather common
technique in food processing, electrostatic complexation with
different protein hydrolysates appears as a promising approach to
tuning the gelation and gel properties of polysaccharide.
5. Conclusions
As the major food structuring agents, hydrocolloids are indis-
pensible in the design of food structure and functionality that are
demanded by the consumer of the modern society. Their in-
teractions with other food components coexisting in food matrices
allow increased flexibility for food research and development. This
review covered systematically the interactions of hydrocolloids
with ions, small molecules (colorants, flavors, fatty acids, vitamins,
biosurfactants, and phytochemicals etc.) and macromolecules
(proteins, polysaccharides). Emphasis was put on how to utilize the
interactions to overcome undesired properties in food formulation
and to enhance food quality and functionality for food products.
Acknowledgements
This study was financially supported by the National Natural
Science Foundation of China (31671811, 31501430, 31322043,
31171751), the Program for New Century Excellent Talents in Uni-
versity (NCET-12-0710), and the Projects from Hubei Provincial
Department of Science and Technology (2014BHE004,
2012FFA004), Hubei Provincial Department of Education
(T201307), and Wuhan Science and Technology Bureau
(2015070504020218).
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