From the Edited Volume


1. Introduction

Polysaccharides and proteins are herbal polymers that room widely provided as functional ingredients for assorted food colloids or emulsion formulations. Bulk of food emulsions are made up with polysaccharide and also protein combinations. They are the necessary ingredients of any food colloid formulation mainly due to their capacity to change product shelf life by varying food structure (Schmidt & Smith, 1992; Schorsch, Jones & Norton 1999). Their communication in the formulation hence finds plenty of applications specifically in brand-new food formulation development. Due to facility formation and also creation the nano or micro structures (aggregation and also gelation behavior) they generally adjust the rheological nature of food colloids i beg your pardon may influence the food product texture and colloidal security (Benichou, 2002; McClements, 2005, 2006, 2007; Dickinson, 2003). Polysaccharide and protein interactions in solution and interfaces have actually been learned by several teams (Dickinson, 2003, 2008; Bos &Van Vliet 2001; Carrera & Rodríguez Patino 2005; Krägel, Derkatch, & Miller, 2008; Koupantis, & Kiosseoglou, 2009; Mackie, 2009). However, in spite of the large advancement made in the current past, polysaccharide and also protein interaction in food hydrocolloids continue to be among the most an overwhelming topics to understand.

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Proteins, gift surface energetic can play major role in the formation and stabilization the emulsions in the presence of polysaccharide, while interacting through electrostatic or hydrophobic-hydrophobic interactions. On the various other hand, polysaccharides gift hydrophilic in nature generally remain in aqueous step thus assist in regulating the aqueous phase rheology prefer thickening, gelling and also acting together stabilizing agents. The formation and deformation that polysaccharide-protein complexes and their solubility depend on various factors like charge and nature of biopolymers, pH, ionic strength and also temperature of the medium and also even the presence of surfactant of the tool (Ghosh & Bandyopadhyay, 2011). If pH that the tool is reduced listed below isoelctric allude (pI) that the protein existing then net positive charge of the protein will come to be prominent i m sorry will communicate with negatively fee polysaccharide to kind stable electrostatic complex. Similarly, if systems pH increased an ext than protein pI, the net an unfavorable charge the protein will often tend to form complicated with positively fee polysaccharides (Xia & Dubin, 1994; Dickinson, 2008; Turgeon, Schmitt & Sanchez, 2007). Generally, chances of weaker complex formation is more when solution pH is practically equal to protein pI, since at that pH selection surface charge of protein becomes virtually zero. However, at really high concentration, likewise charged biopolymers repel every other and also the network repulsion make the mechanism unstable (separate as two distinct phases) i m sorry is well-known as thermodynamic incompatibility. Incompatibility in the mechanism occurs in ~ pH higher than the protein pIand at higher ionic strength (Grinberg & Tolstoguzov, 1997). Thus by varying pH and also ionic strength of the tool one can achieve a regulate on the polysaccharide-protein interactions.

Polysaccharides and also proteins both contribute to the structural and textural properties of food by transforming rheology the food emulsions through their gelling networking mechanism (Dickinson, 1992). Non-covalent interactions in between polysaccharide and also protein in any kind of emulsion formulation pat a major role to readjust the interfacial behavior and also stability that the food colloids. The driving force for this non-covalent interactions is electrostatic interactions, hydrophobic interactions, H-bonding and Van der Waals interactions. Recent literatures also focus on exactly how protein and polysaccharide molecules deserve to be connected together through covalent bond. In ~ pH close come protein pIthis Maillard-type conjugates were offered to improve the colloidal stability and also interfacial structure of protein in specific conditions (Jiménez-Castańo, Villamiel, & López-Fandiňo, 2007; Benichou, Aserin, Lutz & Garti, 2007)). Recent breakthroughs in the field describe interfacial physico-chemical properties of polysaccharide-protein combined systems (Rodríguez Patino & Pilosof 2011). In this chapter, us would like to focus more on polysaccharide and protein non-covalent interaction studies and also their result towards food colloids stability.


2. Nature the polysaccharide-protein complex

Polysaccharide and also protein complicated formation is mostly driven by miscellaneous non-covalent interactions, like electrostatic, H-bonding, hydrophobic, and also steric interactions (Kruif et al 2001). Protein tote +ve or –ve zeta potential based on the pH the the tool (+ve at pH lower than pIand vice-versa). This +ve or –ve electrical charge ~ above the protein chain allude towards the presence of various amino mountain in the protein molecules and their mode of ionization at different pH arrays (Fig. 1). Carboxylate polysaccharides gain deprotonated (become anionic) at a pH range higher than the pKa (Fig. 1). This electric charge on the back bone that protein or polysaccharide chain is responsible because that electrostatic attraction or repulsion between them. Again, visibility of -COOH group on the polysaccharide and -NH3, -COOH teams on the protein chain room the resources of hydrogen bonding in between these two bio-polymers. Extent of both the this hydrogen bonding and also electrostatic communication depends ~ above the solution parameters such together pH, ionic strength, temperature etc. Other than these ionic job on the bio-polymers, few non-polar segments are additionally present top top the bio-polymers, which space responsible because that the hydrophobic staking through each other. Also though equipment parameters are important components to control the different mode of interactions between protein and also polysaccharide, form of proteins/polysaccharides, molecule weight, charge density, and also hydrophobicity of the bio-polymers are likewise play far-reaching role towards the level of complexation between two bio-polymers in ~ a fixed condition.


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Figure 1.

Variation that charge density on the polysaccharide and protein chain at miscellaneous pH ranges.

In general, interactions between proteins and also polysaccharides are quite explored where big numbers of report have been published based on the interactions between oppositely fee “protein-polysaccharide” equipment (Dmitrochenko et al 1989; Bengoechea et al 2011, stone & Nickerson 2012). Back electrostatic attraction is the key driving force for the complexation between protein and also polysaccharide, but it is likewise reported the hydrogen bonding and also hydrophobic interaction plays a secondary role for security of the “protein-polysaccharide” aggregates (McClements, 2006). The extent of hydrogen bonding and hydrophobic interaction also depends on temperature (Weinbreck et al, 2004). In 2009 Nickerson and also co-workers(Liu, Low, & Nickerson, 2009) have reported the pea protein and also gum acacia complex stabilize at short temperature as result of increase in hydrogen bonding interactions and destabilize in ~ high temperature early to decline in hydrogen bonding interactions. Temperature additionally plays critical role to decision the protein conformations (folded or unfolded). In 2007, Pal (Mitra, Sinha & Pal, 2007) and also coworkers have actually reported that human serum albumin unfolds at greater temperature and undergoes in reversible refolding conformations upon cooling (below 600 c). Unravelled conformations of protein expose an ext reactive website (amino acids) come the solvent phase, thus an ext chances of interactions (or binding) v polysaccharide. Binding that anionic polysaccharides (pH~pKa) to the cationic protein (at pHI) an outcome both soluble and insoluble complexes (Magnusson & Nilsson, 2011). Initial binding that polysaccharides (anionic) come the proteins (cationic) cause charge neutralizations, which bring about the formation of insoluble “protein-polysaccharide” aggregates (Schmitt et al, 1998). Further binding that anionic polysaccharides come those neutral aggregates make it successfully anionic, which leads to formation of dissolve complexes. Yet binding that anionic polysaccharides with anionic proteins (pH>pI) are likewise known and also governed through the interactions between anionic reactive website of polysaccharide and tiny cationic reactive website of protein (Fig. 2). Binding the anionic polysaccharides to the cationic next of protein (at pH>pI) result in formation of anionic “protein-polysaccharide” aggregates, hence soluble complexes. Therefore, concentration of polysaccharides and also pH play an important role towards the solubility that “protein-polysaccharide” aggregates.

Two bio-polymers can exist either in a single phase solution or in a step separated systems depending on the nature the bio-polymers, their concentration, and solution conditions. Once two bio-polymers lug opposite charge, climate either lock agglomerates to form soluble complexes (single phase) or insoluble precipitates (2-phase system). Top top the other hand, as soon as two non-interacting bio-polymers blended together, either they exist in a solitary phase system (where two different entities distributes uniformly transparent the medium) or exist together two distinct phases (each phases consist of different bio-polymer). Therefore, in the protein-polysaccharide system, phase separation occurs v two various mechanisms which room associative step separationand segregative phase separation(Tolstoguzov, 2006). Associative phase separationis the aggregation between two oppositely charged bio-polymers (electrostatic attraction driven), leader to the phase separation, where one phase is enriched v two different bio-polymers (coacervation or precipitation) (Fig. 3). Segregative phase separationoccurs either due to solid electrostatic repulsion (between two similarly charged bio-polymers) or because of an extremely high steric exclusion (between two neutral bio-polymers). In this case, at short concentration, two biopolymers can co-exist in a solitary phase conversely, at higher concentration, it starts phase separation. (Fig. 3).


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Figure 3.

Schematic depiction of the possible mode that interaction between polysaccharides and also proteins.


3. Sensible properties that polysaccharide-protein complexes concerned food application

Polysaccharide-protein complexes exhibition a wide selection of exciting properties, such together surface task to stabilize air-water or oil-water interfaces, viscosifying, and gelling properties etc. Viscosifying and gelling capability of polysaccharide-protein complexes aid to acquire gel-like processed food assets without any thermal therapy in the process. The interfacial nature of these complexes help to send stability into the emulsion food products. Also, protein–polysaccharide complexes room able to encapsulate several active ingredients; thus they act as delivery systems for countless bioactives or perceptible molecules in food formulations. This complexes are likewise known to differ bulk/interfacial structures, textures and shelf-life stability of the food colloids. In the following section us will discuss this polysaccharide-protein interaction in light of their useful properties.


3.1. Viscosity of polysaccharide-protein complicated and air-water foam stability

Viscosity and also gelling space the rheological building which counts on the molecular characteristics of the biopolymers, such as their molecule weight, shape, chain flexibility. Other components are the concentration, interaction in between the biopolymers and water, as well as solution parameters like: pH, ionic strength and presence of other components/ligands etc. Interactions in between polysaccharide and protein have been proven to widen the functional properties of every individual biopolymer. Rheological nature of polysaccharide-protein complex lead to brand-new rheological habits different from each individual biopolymer.

Association of two bio-polymers is meant to boost the mass viscosity the the device as reality of larger sizes room formed. The rheological habits of numerous protein–polysaccharide combined systems have actually been studied and ranged indigenous viscous to viscoelastic properties showing elastic habits is reported. The character language polysaccharide-protein complexes increase viscosity and rheology that the system uncovered to be relies on the nature and also structure that polysaccharides. Viscous residential or commercial property of gum acacia-protein coacervates attributes to the globular configuration of the polysaccharide, conversely, the exact same protein with straight pectin results in gel-like system. Beside the nature the the individual bio-polymer systems property and also concentration that bio-polymers are also known to impact the rheology that the system (Dickinson, 2011). For example, it was found that pH play a significant role in the viscosity of the coacervate phase. A preferably viscosity was acquired at pH 4.0, where concentration the whey protein and gum arabic in the coacervate phase was maximum and extent the electrostatic attraction to be highest. This suggests that the electrostatic interactions between whey protein and also gum arabic were responsible because that the extremely viscous actions of the coacervates. Whereas, the exact same composition the whey protein and also gum arabic at pH over protein pI(i.e. Comparatively reduced electrostatic interactions) showed an ext elastic nature than viscous. Ionic strength and protein/polysaccharide ratio is likewise known to play an important role towards the rheology the polysaccharide-protein systems. For example, optimal salt concentrations (0.21 M NaCl) donate the coacervation that β-lactoglobulin v pectin at greater concentration and also produce lot stronger gelatin strength. For far better gelling property, the is essential to regulate the parameters which compelled to form coacervate, because strong associative interaction decrease the solubility of complexes and hence reduced the hydration capacity of the complex, which leads to to decrease in the viscosity (Schmitt & Turgeon, 2011; Kruif, et al 2004).

Viscoelastic nature of polysaccharide-protein complexes likewise play vital role towards the foam stability in variety of food products. In instance of air-water device foam have the right to be define as the wait entrapment by a slim liquid film (water), where this liquid film is stabilized by part surface energetic molecules. Security of the foam increases with the boost in the security of the interfacial fluid film, due to the fact that lower security of this interfacial liquid film have the right to lead to the diffusion of wait entrapped within the foam. Viscosity that this fluid film is one more parameter by which one can manage the diffusion rate of waiting entrapped inside the foam. Therefore, higher stability and also viscosity that the interfacial liquid film leads to lower diffusion of air entrapped within the foam and also increase the foam stability. Schmitt and co-workers have actually studied the air-water interfacial building of β-lactoglobulin-acacia gum complexes at pH 4.2 . The group has reported the although surface activity of the facility is comparable with the pure protein, but complicated forms lot stronger viscoelastic interfacial film v thickness of about 250 Å. Together a result, gas permeability the thin-film stabilized by the complexes was considerably reduced (0.021 cm s -1) compared to pure β-lactoglobulin (0.521 cm s-1). This phenomenon suggests that security of foam (stabilized by protein-polysaccharide complex) is greater compared to the foam stabilized through protein alone.

The likely explanation of the higher foam stability and different interfacial properties of coacervate is the protein-polysccharide complexes room able come re-organize in ~ the user interface by coalescence, creating interfacial microgel. This findings were applied for the ice cream formulation for boosted air bubble stability (Schmitt C, Kolodziejczyk E. 2010). Similarly, gelatin has been replaced by whey protein isolate-gum acacia complexes to improve the bubble security in chilled dairy commodities (Schmitt C, Kolodziejczyk E. 2010). In instance of stabilization by complexes, sports in proportion of biopolymers might be provided to regulate the size of the complexes, for this reason their surface ar activity. In enhancement to that, viscoelastic properties of the air-water interfacial movie is feasible to song by either adsorbing 2 biopolymers all at once or through the sequential adsorption the protein complied with by polysaccharide. Together for example, β-lactoglobulin-pectin complexes are recognized to stabilize the air-water interface. In this case, thickness that the film obtained from the sequential adsorption of protein and polysaccharide was greater (450 Å) than the adsorption that complexes (250 Å) (Ganzelves et al 2008).

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In contrary to air-water foam stability, use of polysaccharide-protein complexes because that the stabilization that oil-water emulsion (Martínez et al 2007) has received much an ext attention. Usage of these polysaccharide-protein hydrocolloids together an emulsion stabilizer will certainly be debated in the following section.