Effect of Essential Oils from Lemongrass and Tahiti Lime Residues on the Physicochemical Properties of Chitosan-Based Biodegradable Films.

This work aimed to evaluate the impact of adding two essential oils (EO) from lemongrass (LEO) and Tahiti lime (TLEO) on the physical, mechanical, and thermal properties of chitosan-based biodegradable films. Six film formulations were prepared: two controls with chitosan concentrations of 1% and 1.5% v/w, two formulations combining the two chitosan concentrations with 1% LEO v/v, and two formulations combining the two chitosan concentrations with 1% TLEO v/v. The films' morphological, water affinity, barrier, mechanical, and thermal properties were evaluated. The films' surface showed a heterogeneous morphology without cracks, whereas the cross-section showed a porous-like structure. Adding EO to the films promoted a 35-50% decrease in crystallinity, which was associated with an increase in the elasticity (16-35%) and a decrease in the tensile strength (9.3-29.2 MPa) and Young's modulus (190-1555 MPa) on the films. Regarding the optical properties, the opacity of the films with TLEO increased up to 500% and 439% for chitosan concentrations of 1% and 1.5%, respectively. While the increase in opacity for the films prepared with LEO was 357% and 187%, the reduction in crystallinity also reduced the resistance of the films to thermal processes, which could be explained by the reduction in the enthalpy of fusion. The thermal degradation of the films using TLEO was higher than those where LEO was used. These results were indicative of the great potential of using TLEO and LEO in biodegradable films. Likewise, this work showed an alternative for adding value to the cultivation of Tahiti lime due to the use of its residues, which is in accordance with the circular economy model. However, it was necessary to deepen the study and the use of these essential oils in the preparation of biodegradable films.

Impact of Lipid and Protein Co-oxidation on Digestibility of Dairy Proteins in Oil-in-Water (O/W) Emulsions.

Enrichment of polyunsaturated fatty acids (PUFAs) is a growing trend in the food industry. However, PUFAs are known to be susceptible to lipid oxidation. It has been shown that oxidizing lipids react with proteins present in the food and that as a result polymeric protein complexes are produced. Therefore, the aim of this work was to investigate the impact of lipid and protein co-oxidation on protein digestibility. Casein and whey protein (6 mg/mL) based emulsions with 1% oil with different levels of PUFAs were subjected to respectively autoxidation and photo-oxidation. Upon autoxidation at 70 °C, protein digestibility of whey protein based emulsions containing fish oil decreased to 47.7 ± 0.8% after 48 h, whereas in the controls without oil 67.8 ± 0.7% was observed. Upon photo-oxidation at 4 °C during 30 days, mainly casein-based emulsions containing fish oil were affected: the digestibility amounted to 43.9 ± 1.2%, whereas in the control casein solutions without oil, 72.6 ± 0.2% of the proteins were digestible. Emulsions containing oils with high PUFA levels were more prone to lipid oxidation and thus upon progressive oxidation showed a higher impact on protein digestibility.

Identification of modified lysozyme peptides upon photo-oxidation by LC-TOF-MS.

Protein oxidation can have major implications on the quality and safety of foods, but the majority of methods to evaluate oxidative damage lack specificity. Therefore, this study aimed to identify specific markers for protein oxidation. A well-characterized protein, lysozyme, was modified by photo-oxidation and subsequently hydrolyzed prior to peptide analysis by LC-TOF-MS. A semiquantitative analysis of the peptides indicated that from the seven peptides containing sensitive amino acids, two peptides (HGLDNYR and WWCNDGR) were highly affected upon photo-oxidation and have the potential to serve as markers for protein oxidation. Site-specific modifications enabled the description of the degradation pathway of several lysozyme peptides but also indicated that the surrounding amino acids and the 3D structure of the protein have an impact on the induced modifications. It is therefore advisable to evaluate protein oxidation on the intact protein.