RESUMEN

Whey protein isolate (WPI) has the potential to be a Pickering stabilizer, but its applications in emulsions are restricted due to its structural susceptibility to external environments. Proanthocyanidin (PAC) is a natural antioxidant polyphenol that can improve protein properties and enhance the stability and longevity of emulsions. In the current work, PACs were employed to bind WPIs, forming a complex to stabilize Pickering emulsion. Fluorescence spectroscopy, infrared spectroscopy, confocal microscopy, quartz crystal microbalance with dissipation monitoring (QCM-D), and antioxidant stability of the emulsion were performed to characterize the structural changes of the protein/polyphenol complexes and their effects on the interfacial properties and stability of the emulsion. Results indicated that PACs and WPIs might bind through hydrogen bonding and hydrophobic interactions, effectively increasing the hydrophilicity of the complexes. QCM-D and emulsion stability showed that adsorption at the oil-water interface of the complexes was the largest, and the stability of the Pickering emulsion was optimal when the concentration ratio of PAC to WPI exceeded 1:1. The antioxidant properties of Pickering emulsions were positively correlated with the addition of PACs. These findings demonstrated that PACs could improve the properties of WPIs and enhance the stability and antioxidant properties of WPI Pickering emulsions.

RESUMEN

Trans-impedance amplifier (TIA) based capacitance-voltage (C-V) readout circuits are widely used in micro-machined gyroscopes' control system. In this work, the noise performance of a TIA and charge sensitive amplifier (CSA) based C-V readout circuit is analyzed in detail. The theoretical derivation and simulation experiments carried out in this paper show that the thermal noise of high value feedback resistors in TIA dominates the output noise of the circuit, while a CSA-based readout circuit can overcome this shortcoming. Then, a CSA-based C-V readout circuit is designed with a 1.8 V transistor on a 180 nm complementary metal-oxide-semiconductor. This C-V-based readout circuit occupies an area of 0.039 mm2, which is smaller than the area of a 0603 package resistor. When 1 V bias voltage (Vb) is added to the capacitors under test, the tested C-V gain of this circuit is as high as 225 dB, and the tested output noise of the circuit is less than 150 nV/Hz. Finally, the fabricated chip achieved a resolution of 840 zF/Hz at Vb as low as 1 V. This CSA-based C-V readout circuit has more advantages in terms of noise and area over the TIA circuit and is more suitable for integration into the interface integrated circuit for micro-gyroscopes.

RESUMEN

Glycosylated protein was obtained by the reaction of whey protein isolate(WPI) with inulin of different polymerization degrees and was used to stabilize a pomegranate seed oil emulsion. The physicochemical and antioxidative properties of the emulsions were assessed, and the impacts of accelerated oxidation on pomegranate seed oil were examined. The interfacial tension of WPI and short-chain inulin (SCI)-glycosylated conjugate (WPI-SCI) gradually decreased with increasing glycosylation reaction time. Emulsions stabilized by WPI-SCI (72 h) were the most stable, with a thick interfacial film on the surface of the droplets. After accelerated oxidation for 72 h, WPI-SCI inhibited the oxidation of oil in the emulsion. GC-IMS results showed that the production of harmful volatile components in oil was inhibited, and the peroxide strength was less than 30 mmol/kg oil. This study contributes to understanding of stable storage of lipids.

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RESUMEN

Trans-impedance amplifier (TIA) based capacitance-voltage (C-V) readout circuit is an attractive choice for micro-machined gyroscope for its simplicity and superior performance. In this work, the noise and the C-V gain characteristics of the TIA circuit are analyzed in detail. Then, a TIA based readout circuit with a C-V gain of about 286 dB is designed, and a series of experiments are conducted to test the performance of the circuit. Both the analysis and test results show that T-network TIA should be avoided as far as possible for its poor noise performance. All results also show that there is a signal-to-noise ratio (SNR) limit for the TIA based readout circuit, and the SNR can only be further improved by filtering. Hence, an adaptive finite impulse response filter is designed to further improve the SNR of the sensed signal. For a gyroscope with a peak-to-peak variable capacitance of about 200 aF, a SNR of 22.8 dB can be achieved by the designed circuit and a SNR of 47 dB can be obtained by further adaptive filtering. Finally, the solution presented in this paper achieves a capacitive sensing resolution of 0.9 aF.

RESUMEN

A glycosylated protein/procyanidin complex was prepared by self-assembly of glycosylated whey protein isolate and proanthocyanidins (PCs). The complex was characterized through endogenous fluorescence spectroscopy, polyacrylamide gel electrophoresis, Fourier infrared spectroscopy, oil-water interfacial tension, and transmission electron microscopy. The results showed that the degree of protein aggregation could be regulated by controlling the added amount of procyanidin, and the main interaction force between glycosylated protein and PCs was hydrogen bonding or hydrophobic interaction. The optimal binding ratio of protein:PCs was 1:1 (w/w), and the solution pH was 6.0. The resulting glycosylated protein/PC compounds had a particle size of about 119 nm. They exhibited excellent antioxidant and free radical-scavenging abilities. Moreover, the thermal denaturation temperature rose to 113.33 °C. Confocal laser scanning microscopy (CLSM) images show that the emulsion maintains a thick interface layer and improves oxidation resistance with the addition of PCs, increasing the application potential in the functional food industry.

RESUMEN

Protein-polysaccharide-polyphenol delivery systems function as a promising tool to deliver bioactive ingredients aiming to improve their solubility and bioavailability. In this study, whey protein isolate (WPI), short-chain inulin (SCI), and cyanidin-3-glucoside (C3G) were first used to stabilize Pickering emulsions. The physicochemical properties and stability of curcumin encapsulated or not in Pickering emulsions were explored. Results showed that glycosylation and C3G reduced surface and interfacial tension on protein surfaces and inhibited the aggregation of emulsion droplets, thereby reducing the emulsion's particle size. WPI-SCI/C3G stabilized Pickering emulsion had the best stability. The CLSM results showed that the WPI-SCI and WPI-SCI/C3G stabilized emulsions were uniformly dispersed, suggesting that glycosylation and the interaction between protein and C3G enhanced the adsorption capacity of the interfacial protein and improved the stability of the Pickering emulsion. The retention rates of curcumin-loaded WPI-SCI- (67.34 %) and WPI-SCI/C3G- (77.07 %) stabilized Pickering emulsions on day 8 of storage were higher than those in WPI- (33.97 %) and WPI/C3G- (37.02 %) stabilized emulsions, and the degradation half-life was also extended from 7 days to >15 days. These findings provide a theoretical basis for the application of WPI Pickering emulsion and indicate a useful means for the delivery of bioactive components.

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The poor water solubility of apigenin limits its application feasibility in food and medicine. To address this issue, this study successfully prepared apigenin-loaded zein composite nanoparticles using the pH-driven self-assembly method. The nanoparticles were stabilized by hydrophilic whey protein isolate and carboxymethyl cellulose. The composite nanoparticles exhibited high potential, small size, and uniform particle size distribution. Circular dichroism and fluorescence spectroscopy results revealed that the nanoparticles showed conformational changes from unfolding to folding during the neutralization process. The main driving forces for the formation of nanoparticles were hydrophobic interaction and hydrogen bonding. Encapsulation efficiency and loading capacity of apigenin were 87.28% and 8.17%, respectively. Compared with single zein, apigenin-loaded zein-whey protein isolate-carboxymethyl cellulose showed better re-dispersibility (92.83%), thermal stability, and in vitro release efficiency of apigenin (65.27%).

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