Protein/polysaccharide intramolecular electrostatic complex as superior food-grade foaming agent

High-performance foaming agents are widely required in the food industry. In this study, the relationship between electrostatic interaction of whey protein isolate (WPI)/alginate (ALG) and the resultant foaming properties were investigated systematically. The phase diagram of WPI/ALG was established in terms of protein/polysaccharide mixing ratio (r) and pH. The results show that the foaming capacity of WPI/ALG complexes is almost the same across different regions of the phase diagram, while the foam stability varies significantly. At pHs 7.0 and 0.5 where no electrostatic complexation occurs, the foam stability is found to decrease monotonically with decreasing r. At pH 4.0 and particular mixing ratios, i.e., r = 1 and 2, intramolecular soluble complexes are formed and the particular WPI/ALG complexes yield the best foam stability, as compared to other electrostatic complexes or individual components. The half-life (t1/2) of the foams stabilized by the intramolecular electrostatic complexes is as long as 4000 s at a very low WPI/ALG concentration of 0.1% w/w. The foaming properties are in line with the foam viscosity, interfacial adsorption behavior and microstructures of the complexes observed at the air-water interface. This demonstrates that the protein/polysaccharide intramolecular electrostatic complex, more specifically at the stoichiometry, could potentially act as a superior foaming agent in the food industry

Effect of arabinogalactan protein complex content on emulsification performance of gum arabic

The emulsification properties of the standard (STD), matured (EM2 and EM10) and fractionated gum arabic samples via phase separation induced molecular fractionation were investigated to find out how the content of arabinogalactan protein (AGP) complex affects the resulting emulsion properties. Phase separation and the accompanying molecular fractionation were induced by mixing with different hydrocolloids including hyaluronan (HA), carboxymethyl cellulose (CMC), and maltodextrin (MD). Increase of AGP content from 11 to 28% resulted in the formation of emulsions with relatively smaller droplet sizes and better stability. Further increase in the AGP content to 41% resulted in the formation of emulsions with larger droplets. In spite of the larger droplets sizes, these emulsions were extremely stable. In addition, the emulsions prepared with GA higher AGP content better stability in the presence of ethanol. The results indicate that AGP content plays a vital role in emulsion stability and droplet size

Interfacial and emulsifying properties of the electrostatic complex of β-lactoglobulin fibril and gum Arabic (Acacia Seyal)

Formation, interfacial and emulsifying properties of the electrostatic complex of β-lactoglobulin fibril (BLGF) and gum Arabic Acacia Seyal (AS) were investigated. Necklace-like soluble complex could be formed at pH 3.5, and its charge and interfacial properties depended on the BLGF content. With appropriate amount of BLGF (< 9.09 wt.%), the formed complex possessed a good dispersibility and surface activity. When excessive BLGF (9.09∼50 wt.%) existed, surface charge of the complex was gradually neutralized and aggregation occurred. Homogeneous oil-in-water emulsions could be stabilized by the complex and the droplet size decreased with increasing BLGF content. Higher content of BLGF (9.09∼50 wt.%) was detrimental for emulsification due to the aggregation of complex, and the formed emulsion tended to flocculate. Compared with AS, the complex formed emulsions were much more stable against heating (90 ℃, 30 min) and salting (200 mM NaCl) environments, and the emulsions were stable during long-term storage (46 days). Proposed mechanisms for the adsorption of BLGF/AS complex at the oil-water interface. Pure AS (i) could adsorb at the oil-water interface but formed a loose film due to its poor surface activity and insufficient adsorption amount. With addition of a small amount of fibrils (ii), soluble electrostatic complexes are formed and they can be adsorbed at the interface to formed a dense viscoelastic film due to the surface activity of the BLGF. With a higher content of fibrils (iii), surface charge of the complex tended to be neutralized, causing the aggregation. Because the presence of protein fibrils, they could also adsorb at the oil-water interface to produce a viscoelastic film. However, with a bigger size and irregular shape, the aggregates were difficult to array at the interface as densely as the soluble complex

Understanding the multi-scale structure and digestion rate of water chestnut starch

Using combined techniques and two comparisons (maize and cassava starches), this work concerns the multi-scale structure and digestion rate of water chestnut tuber starch. Among the starches, the water chestnut starch showed altered hierarchical structural features and a relatively low digestion rate. The underlying mechanism on the reduced digestion rate of water chestnut starch was discussed from a hierarchical structural view. Specifically, compared with maize starch, the water chestnut starch contained no pores on the granule surface, with the thickened crystalline lamellae, the increased lamella ordering, and the elevated content of crystallites. Such structural features probably increased the bulk density of molecule assembly in starch and thus could hinder the diffusion of enzyme molecules in starch matrixes. Consequently, the absorption of enzyme to the starch glucan chains could be retarded, resulting in a reduced enzyme hydrolysis rate of starch chains. The relatively large amylose molecules of water chestnut starch also tended to reduce the starch digestion rate, associated with the enhanced molecule interactions such as that between starch chains. In addition, the further reduction in the digestion rate of cassava starch could be also ascribed to the variations in the multi-scale structural features

Effects of temperature and solvent condition on phase separation induced molecular fractionation of gum arabic/hyaluronan aqueous mixtures

Effects of temperature and solvent condition on phase separation-induced molecular fractionation of gum arabic/hyaluronan (GA/HA) mixed solutions were investigated. Two gum arabic samples (EM10 and STD) with different molecular weights and polydispersity indices were used. Phase diagrams, including cloud and binodal curves, were established by visual observation and GPC-RI methods. The molecular parameters of control and fractionated GA, from upper and bottom phases, were measured by GPC-MALLS. Fractionation of GA increased the content of arabinogalactan-protein complex (AGP) from ca. 11% to 18% in STD/HA system and 28% to 55% in EM10/HA system. The phase separation-induced molecular fractionation was further studied as a function of temperature and solvent condition (varying ionic strength and ethanol content). Increasing salt concentration (from 0.5 to 5 mol/L) greatly reduced the extent of phase separation-induced fractionation. This effect may be ascribed to changes in the degree of ionization and shielding of the acid groups. Increasing temperature (from 4oC to 80oC) also exerted a significant influence on phase separation-induced fractionation. The best temperature for GA/HA mixture system was 40oC while higher temperature negatively affected the fractionation due to denaturation and possibly degradation in mixed solutions. Increasing the ethanol content up to 30% showed almost no effect on the phase separation induced fractionation