Construction of resveratrol and quercetin nanoparticles based on folic acid targeted Maillard products between Jiuzao glutelin isolate and carboxymethyl chitosan: Improved stability and function.

Advanced targeted nanoparticles (NPs) were designed to enhance the targeted delivery of resveratrol (RES) and quercetin (QUE) by utilizing carboxymethyl chitosan (CTS) and Jiuzao glutelin isolate (JGI) conjugates. Briefly, RES and QUE were encapsuled within CTS-JGI-2 (CTS/JGI, m/m, 2:1). The carrier's targeting properties were further improved through the incorporation of folic acid (FA) and polyethylenimine (PEI). Moreover, the stability against digestion was enhanced by incorporating baker yeast cell walls (BYCWs) to construct RES-QUE/FA-PEI/CTS-JGI-2/MAT/BYCW NPs. The results demonstrated that FA-PEI/CTS-JGI-2/MAT/BYCW NPs could improve cellular uptake and targeting property of RES and QUE through endocytosis of folic acid receptors (FOLRs). Additionally, RES-QUE successfully alleviated LPS- and DSS-induced inflammation by regulating NF-κB/IkBa/AP-1 and AMPK/SIRT1signaling pathways and reducing the secretion of inflammatory mediators and factors. These findings indicate FA-PEI/CTS-JGI-2/MAT/BYCW NPs hold promise as an oral drug delivery system with targeted delivery capacities for functional substances prone to instability in dietary supplements.

Thermomechanically micronized sugar beet pulp: Emulsification performance and the contribution of soluble elements and insoluble fibrous particles.

In this work, thermomechanically micronized sugar beet pulp (MSBP), a micron-scaled plant-based byproduct comprised of soluble elements (∼40 wt%) and insoluble fibrous particles (IFPs, ∼60 wt%), was used as a sole stabilizer for oil-in-water emulsion fabrication. The influence of emulsification parameters on the emulsifying properties of MSBP was investigated, including emulsification techniques, MSBP concentration, and oil weight fraction. High-speed shearing (M1), ultrasonication (M2), and microfludization (M3) were used to fabricate oil-in-water emulsions (20% oil) with 0.60 wt% MSBP as stabilizer, in which the d4,3 value was 68.3, 31.5, and 18.2 µm, respectively. Emulsions fabricated by M2 and M3 (higher energy input) were more stable than M1 (lower energy input) during long-term storage (30 days) as no significant increase of d4,3. As compared to M1, the adsorption ratio of IFPs and protein was increased from ∼0.46 and ∼0.34 to ∼0.88 and ∼0.55 by M3. Fabricated by M3, the creaming behavior of emulsions was completely inhibited with 1.00 wt% MSBP (20% oil) and 40% oil (0.60 wt% MSBP), showing a flocculated state and could be disturbed by sodium dodecyl sulfate. The gel-like network formed by IFPs could be strengthened after storage as both viscosity and module were significantly increased. During emulsification, the co-stabilization effect of the soluble elements and IFPs enabled a compact and hybrid coverage onto the droplet surface, which acted as a physical barrier to endow the emulsion with robust steric repulsion. Altogether, these findings suggested the feasibility of using plant-based byproducts as oil-in-water emulsion stabilizers.

Valorizing protein-polysaccharide conjugates from sugar beet pulp as an emulsifier.

Inspired by the emulsion stability of sugar beet pulp pectin, the hydrophobic protein fraction in sugar beet pulp (SBP) is expected to feature high interfacial activity. This work retrieved alkaline extracted protein-polysaccharide conjugates (AEC) from partially depectinized SBP by hot alkaline extraction. AEC was protein-rich (57.20 %), and the polysaccharide mainly comprised neutral sugar, which adopted a rhamnogalacturonan-I pectin-like structure. The hydrophobic polypeptide chains tangled as a dense 'core' with polysaccharide chains attached as a hydrated 'shell' (hydrodynamic radius of ~110 nm). AEC could significantly decrease the oil-water interfacial tension (11.58 mN/m), featuring superior emulsification performance than three control emulsifiers, especially the excellent emulsifying stability (10 % oil) as the emulsion droplet size of 0.438 and 0.479 µm for fresh and stored (60 °C, 5 d) emulsions, respectively. The relationship of molecular structure to emulsification was investigated by specific enzymic modification, suggesting the intact macromolecular structure was closely related to emulsifying activity and that the NS fraction contributed greatly to emulsifying stability. Moreover, AEC was highly efficient to stabilize gel-like high internal phase emulsions (oil fraction 0.80) with low concentration (0.2 %) and even high ionic strength (0-1000 mM). Altogether, valorizing AEC as an emulsifier is feasible for high-value utilization of SBP.

Interfacial and emulsification properties of sono-emulsified grape seed oil emulsions stabilized with milk proteins.

Emulsions were designed under low frequency ultrasound (20 kHz) at energy densities of 11.7-117.0 J/mL using grape seed oil and milk protein solutions containing different casein to whey protein ratios of 80:20, 60:40, 50:50 and 40:60. An increase in energy densities produced emulsions with a smaller droplet size and narrow size distribution at all milk protein ratios. However, the minimum sono-energy density required to produce stable emulsions varied depending on the ratio of caseins (CN) and whey proteins (WP) in the continuous phase. In addition, the composition of the interfacial layer was dependent on the composition of the milk proteins in the continuous phase. The interfacial layer was predominantly covered by the CN and CN-WP aggregates in the presence of equal or greater amounts of caseins than whey proteins (80:20, 60:40 and 50:50), while WP aggregates and CN-WP aggregates were the primary constituents of whey protein-rich emulsions (40:60).

Heat stability and acid gelation properties of calcium-enriched reconstituted skim milk affected by ultrasonication.

The aggregation of proteins after heating of calcium-fortified milks has been an ongoing problem in the dairy industry. This undesirable effect restricts the manufacture of calcium rich dairy products. To overcome this problem, a completely new approach in controlling the heat stability of dairy protein solutions, developed in our lab, has been employed. In this approach, high intensity, low frequency ultrasound is applied for a very short duration after a pre-heating step at ⩾70 °C. The ultrasound breaks apart whey/whey and whey/casein aggregates through the process of acoustic cavitation. Protein aggregates do not reform on subsequent post-heating, thereby making the systems heat stable. In this paper, the acid gelation properties of ultrasonicated calcium-enriched skim milks have also been investigated. It is shown that ultrasonication alone does not change the gelation properties significantly whereas a sequence of preheating (72 °C/1 min) followed by ultrasonication leads to decreased gelation times, decreased gel syneresis and increased skim milk viscosity in comparison to heating alone. Overall, ultrasonication has the potential to provide calcium-fortified dairy products with increased heat stability. However, enhanced gelation properties can only be achieved when ultrasonication is completed in conjunction with heating.

The influence of milk composition on pH and calcium activity measured in situ during heat treatment of reconstituted skim milk.

The pH and calcium activity of reconstituted skim milk solutions (9-21% w/w milk solids non-fat) on heating and after cooling were studied as a function of milk pH prior to heating (pH 6.2-7.2 at 25 degrees C) and added calcium complexing agents (phosphate or EDTA). The pH decreased as the temperature was raised from 25 to 90 degrees C and the magnitude of the pH decrease was greater with increase in initial pH at 25 degrees C before heating or milk concentration. The pH decrease on heating from 25 to 90 degrees C in skim milk solutions with added calcium complexing agents was lower than that of milk without the addition of these salts. The calcium activity decreased on heating from 25 to 60 degrees C. The magnitude of the change decreased with increase in initial pH at 25 degrees C before heating and milk concentration. The decrease in calcium activity on heating from 25 to 60 degrees C for skim milk solutions with added calcium complexing agents was lower than that of milk solutions without the addition of calcium complexing agents. The changes in pH and calcium activity on heating milk were largely reversible after cooling the milk. The results suggested that the pH and calcium activity at high temperatures are a function of the milk composition. Knowledge of the initial pH prior to heating alone is not sufficient for predicting the changes that occur during heating.