Repulsive forces in lecithin glycol lamellar phases.

The repulsive pressure vs. distance for phospholipid bilayers in glycol has been determined from vapor pressure measurements. The magnitude of this pressure is similar to the case when water is present between the lipid bilayers. Hence, an interaction directly corresponding to the previously reported hydration force is shown also for nonaqueous lecithin/solvent systems

Softening of dried Vangueria infausta (African medlar) using maltodextrin and sucrose

Softening of dried Vangueria infausta using maltodextrin and sucrose was investigated experimentally. The pulp of V. infausta was dried in a convective dryer, the influence of drying temperature as well as relationship between water content and water activity were examined. In this study, 48 samples of V. infausta pulp, with and without maltodextrin or sucrose, were dried at air temperatures of 60 and 80°C, at a constant air velocity of 3 m/s, for 0-240 min, and until constant weight. The water content, water activity, hardness and toughness were evaluated throughout the drying process. Samples dried at 80°C exhibited shorter drying times than samples dried at 60°C. The water activity of fruit dried for 240 min at 80°C varied from 0.633 to 0.759, and the fruit was thus safe regarding microbiological spoilage. The hardness and toughness of the dried fruit pulp increased with the reduction in water content, and it was observed that samples of pure pulp became unacceptably hard and tough, when dried to the level needed to obtain microbiological stability. The addition of sucrose as well as maltodextrin has shown to be able to reduce the hardness as well as the toughness of the dried fruit pulp; which can be considered as a strategy to obtain dried fruit pulp with suitable consistency

Effects of feed composition, protein denaturation and storage of milk serum protein/lactose powders on rehydration properties

Whey powder rehydration is expected to be closely linked to both denaturation and lactosylation of the proteins. This study investigated the relation between the forced imbibition rate of spray-dried milk serum protein/lactose powders and the particle morphology and how it is related to the insoluble and lactosylated protein fraction, respectively. Despite extensive variation in protein denaturation, aggregation and lactosylation, only comparably small effects on the forced imbibition rate of the powders and the particle morphology could be observed. A possible explanation for this rather limited effect on the rehydration properties and particle morphology might be that the surface composition of the powder particles is rather similar and dominated by native proteins. These insights have relevance for the formulation of whey powders with improved rehydration properties

Particle morphology and rehydration properties of spray-dried microgels and fractal aggregates with varying fractions of native milk serum proteins

To keep their functional properties, it is crucial that protein aggregates maintain their structure after spray drying and that the powders can be fully rehydrated. In this study, microgels and fractal aggregates were prepared by heating a mixture of milk serum protein concentrate and lactose (40/60; %, w/w) at 85 °C for 15 min by varying the pH. Various fractions of native proteins were added to the systems prior to spray drying. This study showed that microgels and fractal aggregates kept their structure after spray drying and reconstitution. The particle morphology could be correlated to the stiffness of the interface of the feed droplet. The forced imbibition rate showed a negative correlation with increasing amount of aggregated proteins in the powders that seems to be a result of denatured/aggregated proteins present at the surface. These findings are of importance for the formulation of spray-dried powders with improved rehydration characteristics

Impact of surface properties on morphology of spray-dried milk serum protein/lactose systems

This study investigated milk serum protein concentrate/lactose systems with varying ratios and how the morphology of the spray-dried particles of these systems could be described by the surface properties of the feed as well as the protein surface coverage of the particles. An extrapolation of the surface pressure of the feed to 0.3 s, the approximate time for molecular diffusion in an atomised droplet in the spray-dryer, showed a relationship with the particle morphology. At low protein concentrations (<1%), the particles were almost totally smooth. At higher protein concentrations (≥1%), the particles became dented and ridged, and these tended to become deeper and thicker as the protein concentration increased. It is suggested that the surface pressure of the feed at low protein concentrations is the most prominent surface property, whereas the modulus of elasticity seems to be the most prominent surface property for particle surface deformation at higher protein concentrations

Impact of surface properties on morphology of spray-dried milk serum protein/lactose systems

This study investigated milk serum protein concentrate/lactose systems with varying ratios and how the morphology of the spray-dried particles of these systems could be described by the surface properties of the feed as well as the protein surface coverage of the particles. An extrapolation of the surface pressure of the feed to 0.3 s, the approximate time for molecular diffusion in an atomised droplet in the spray-dryer, showed a relationship with the particle morphology. At low protein concentrations (<1%), the particles were almost totally smooth. At higher protein concentrations (≥1%), the particles became dented and ridged, and these tended to become deeper and thicker as the protein concentration increased. It is suggested that the surface pressure of the feed at low protein concentrations is the most prominent surface property, whereas the modulus of elasticity seems to be the most prominent surface property for particle surface deformation at higher protein concentrations

Impact of protein surface coverage and layer thickness on rehydration characteristics of milk serum protein/lactose powder particles

Spray-dried powders were produced from milk serum protein concentrate and lactose in varying ratios, and the rehydration characteristics of the powders were evaluated. The dissolution rate was estimated with a flow-cell based technique, and the external and internal distribution of the powder components were evaluated with X-ray photoelectron spectroscopy and confocal Raman microscopy, respectively. The surface of the powder particles is more or less covered by a thin protein layer. A phase segregation between protein and lactose is observed in the interior of the particle resulting in a protein rich layer in the vicinity of the surface. However, the protein layer in the vicinity of the particle surface tends to become thinner as the bulk protein concentration increases in the powders (from 10 to 60% w/w). The time for the spontaneous imbibition to occur show a linear correlation with the protein surface coverage. The dissolution rate of powders containing 0.1% w/w protein is around 60 times faster than for a powder containing 1% w/w protein but the dissolution rate of powders containing 1% and 100% w/w differ only by a factor of 2. Thus, it is suggested that the outer protein layer becomes denser at the interface as the protein content increases in the powders, thereby causing poorer rehydration characteristics of the powders (especially for low protein concentrations 0.1–1% w/w). This insight has relevance for the formulation of whey protein powders with improved rehydration characteristics

Extraction of β-Glucan from Oat Bran in Laboratory Scale

Effects of various enzymes and extraction conditions on yield and molecular weight of beta-glucans extracted from two batches of commercial oat bran produced in Sweden are reported. Hot-water extraction with a thermostable alpha-amylase resulted in an extraction yield of approximate to 76% of the beta-glucans, while the high peak molecular weight was maintained (1.6 x 10(6)). A subsequent protein hydrolysis significantly reduced the peak molecular weight of beta-glucans (by pancreatin to 908 x 10(3) and by papain to 56 x 10(3)). These results suggest that the protein hydrolyzing enzymes may not be pure enough for purifying beta-glucans. The isolation scheme consisted of removal of lipids with ethanol extraction, enzymatic digestion of starch with alpha-amylase, enzymatic digestion of protein using protease, centrifugation to remove insoluble material, removal of low molecular weight components using dialysis, precipitation of beta-glucans with ethanol, and air-drying