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1.
Colloids Surf B Biointerfaces ; 238: 113917, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38615391

ABSTRACT

In this study, the encapsulation and structural characteristics of the self-assembled liposome formed by epigallocatechin gallate (EGCG) and alcohol dehydrogenase (ADH) were studied. According to the results, EGCG significantly increased the catalytic activity of ADH with a 33.33 % activation rate and the liposomes were able to entrap EGCG-ADH with an effectiveness of 88.94 %. The self-assembled monolayers had nanometer-sized particles, and the excellent self-assembled system was demonstrated by the low PDI value and high surface absolute potential. The scanning electron microscope showed that the self-assembled liposome was honeycomb, groove-shaped, and rough. The spectroscopic results showed that EGCG-ADH complex was formed through hydrogen bond, which changed the secondary structure of the liposome, and verified EGCG-ADH liposome system was successfully prepared. In vitro digestion experiments showed that the gastrointestinal tolerance and antioxidant activity of EGCG-ADH liposomes were significantly higher than those of free EGCG-ADH.


Subject(s)
Alcohol Dehydrogenase , Catechin , Liposomes , Liposomes/chemistry , Catechin/chemistry , Catechin/analogs & derivatives , Alcohol Dehydrogenase/chemistry , Alcohol Dehydrogenase/metabolism , Antioxidants/chemistry , Antioxidants/pharmacology , Particle Size , Hydrogen Bonding
2.
Foods ; 12(9)2023 Apr 26.
Article in English | MEDLINE | ID: mdl-37174330

ABSTRACT

The study investigated the effects of different microwave vacuum freeze-drying powers (100-500 W) on the emulsifying properties and structural characteristics of egg white protein, which is of great significance in enhancing the added value of EWP and promoting its application. Emulsification analysis revealed that the emulsification performance was significantly influenced by microwave power and reached its maximum at 300 W. Fourier-transform infrared spectroscopy (FT-IR) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analyses showed that microwave vacuum freeze-drying treatment altered the secondary structure of EWP without changing its peptide structure. Fluorescence measurements indicated that the maximum fluorescence emission intensity decreased, and the maximum emission wavelength shifted towards blue as the power increased. Particle size, zeta potential, scanning electron microscopy (SEM), and differential scanning calorimetry (DSC) analyses showed that the average particle size of EWP reached the minimum value of 1203.66 nm, the absolute value of zeta potential reached the maximum value of 41.35 mV, and the thermal stability was strongest, with a more uniform and loose structure observed at 300 W. Texture profile analysis (TPA) showed that appropriate power treatment significantly enhanced the chewiness and viscoelasticity of egg white protein. Therefore, appropriate power treatment could effectively improve the emulsifying properties and stability.

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