Optimization of lycopene spray drying encapsulation in basil seed gum: Boosting bioavailability and mayonnaise stability.

This study aimed to improve lycopene stability and bioavailability in food products. Lycopene, a potent antioxidant, often has poor stability and undesirable organoleptic properties. Therefore, the impact of basil seed gum (BSG) concentration and spray drying inlet temperature (IT) on the physicochemical, bioaccessibility, and antioxidant properties of encapsulated lycopene emulsion (ENL) was investigated using Central Composite Design (CCD)-Response Surface Methodology (RSM).

High internal phase emulsion stabilized by soy protein isolate-Rutin complex: Rheological properties, bioaccessibility and in vitro release kinetics.

High internal phase emulsions (HIPEs) are promising carrier materials for encapsulating and delivering hydrophobic bioactive compounds. By strategically adjusting the composition, particle size, or charge of HIPEs, it is possible to enhance both their stability and the bioaccessibility of hydrophobic polyphenols encapsulated within them. In this study, different soy protein isolate (SPI)-rutin (SPI-R) complexes (formed under various preheating temperatures) were used to stabilize HIPEs, while the particle size, and charge of HIPEs was further adjusted through different homogenization rates.

Soy protein isolate-catechin complexes conjugated by pre-heating treatment for enhancing emulsifying properties: Molecular structures and binding mechanisms.

This study aimed to investigate the impact of different pre-heating temperatures (ranging from 40 °C to 80 °C) on the interactions between soy protein isolate (SPI) and catechin to effectively control catechin encapsulation efficiency and optimize the emulsifying properties of soy protein isolate. Results showed that optimal heat treatment at 70 °C improved catechin encapsulation efficiency up to 93.71 ± 0.

Structural and Gel Textural Properties of Soy Protein Isolate When Subjected to Extreme Acid pH-Shifting and Mild Heating Processes.

Changes in the structural and gel textural properties were investigated in soy protein isolate (SPI) that was subjected to extreme acid pH-shifting and mild heating processes. The SPI was incubated up to 5 h in pH 1.5 solutions at room temperature or in a heated water bath (50 or 60 °C) to lead to protein structural unfolding, followed by refolding at pH 7.

Contributions of fat content and oxidation to the changes in physicochemical and sensory attributes of pork dumpling filler during frozen storage.

This study was conducted to evaluate the contributions of fat addition levels and storage duration at -18 °C to the oxidation and physicochemical changes of frozen pork dumpling filler. With an increase in the fat addition, thiobarbituric acid-reactive substances and carbonyl production increased (P < 0.05), the transition temperatures (Tmax) shifted to lower temperatures, and the total enthalpy (ΔH) of protein denaturation reduced (P < 0.