ABSTRACT
Essential oils (EOs) are liquid extracts derived from various parts of herbal or medicinal plants. They are widely accepted in food packaging due to their bioactive components, which exhibit remarkable antioxidant and antimicrobial properties against various pathogenic and food spoilage microorganisms. However, the functional efficacy of EOs is hindered by the high volatility of their bioactive compounds, leading to rapid release. Combining biopolymers with EOs forms a complex network within the polymeric matrix, reducing the volatility of EOs, controlling their release, and enhancing thermal and mechanical stability, favoring their application in food packaging or processing industries. This study presents a comprehensive overview of techniques used to encapsulate EOs, the natural polymers employed to load EOs, and the functional properties of EOs-loaded biopolymeric particles, along with their potential antioxidant and antimicrobial benefits. Additionally, a thorough discussion is provided on the widespread application of EOs-loaded biopolymers in the food industries. However, research on their utilization in confectionery processing, such as biscuits, chocolates, and others, remains limited. Further studies can be conducted to explore and expand the applications of EOs-loaded biopolymeric particles in food processing industries.
Subject(s)
Anti-Infective Agents , Oils, Volatile , Oils, Volatile/pharmacology , Antioxidants/pharmacology , Food-Processing Industry , Food Packaging/methods , Biopolymers , Polymers , Food IndustryABSTRACT
The iron-chelating peptides from soybean protein hydrolysates (SPH) were investigated using immobilized metal affinity chromatography (IMAC). The results demonstrated that SPH could absorb on the IMAC-Fe(3+) column, while the capability of the binding iron was different in SPH (10-30 kDa), SPH (3-10 kDa), and SPH (1-3 kDa). The highest binding amount on the column occurred with SPH (10-30 kDa). With the IMAC method, the iron-chelating peptides were shown to be formed at pH lower than 5.5, and they were not affected by NaCL with the concentration between 0.1 mol/L and 1 mol/L, while the iron-chelating peptides could be partially disrupted by 0.02 mol/L Na(2)HPO(4) at pH 8.0. Furthermore, the iron-chelating peptides were identified with reversed phase (RP)-HPLC, SDS-PAGE, and MALDI-TOF MS/MS. The binding characteristics of the SPH on IMAC-Fe(3+) and the sequences of the iron-chelating peptides revealed that binding sites between SPH and iron might be the carboxyl groups of Glu and Asp residues.
Subject(s)
Chromatography, Affinity/methods , Glycine max/chemistry , Iron/chemistry , Peptides/chemistry , Plant Proteins/chemistry , Protein BindingABSTRACT
Soybean protein hydrolysates are widely used as functional foods as they have antioxidative properties able to enhance immune responses in humans. The alcalase enzymatic hydrolysates of beta-conglycinin were fractionated by ultrafiltration, and two main fractions, SP1 (<10 kDa) and SP2 (10-20 kDa), were obtained. The effects of these two fractions on the growth, development of epithelial cells, and formation of intercellular tight junctions were tested on an in vitro Caco-2 cell culture system. The inhibitory effects of SP1 and SP2 on the penetration of Salmonella typhimurium into Caco-2 epithelial cells were also examined. The results showed that the addition of >0.05 g/L of SP2 improved epithelial cell growth and that a concentration of 0.5 g/L of SP2 increased intercellular tight junction formation, which resulted in increased of transepithelial monolayer resistance (TER) values. Moreover, a lower S. typhimurium count compared to control was obtained when Caco-2 cells were grown in 0.05 and 0.5 g/L of SP2. These results show that beta-conglycinin hydrolysates play an important role in resisting S. typhimurium penetration into intestinal epithelial cells and that high molecular mass peptides (10-20 kDa) were more effective overall than low molecular mass peptides.
