Cocoa Nanoparticles to Improve the Physicochemical and Functional Properties of Whey Protein-Based Films to Extend the Shelf Life of Muffins

A novel nanocomposite whey protein-based film with nanoemulsified cocoa liquor (CL) was prepared using one-stage microfluidization to evaluate the emulsion properties and the effect of CL on the film properties by response surface methodology (RSM). The results indicated that the number of cycles by microfluidization had a significant effect (p < 0.05) on the particle size and polydispersity of the nanoemulsion, with a polyphenol retention of approximately 83%. CL decreased the solubility (<21.87%) and water vapor permeability (WVP) (<1.57 g mm h−1 m−2 kPa−1) of the film. FTIR analysis indicated that CL modified the secondary protein structure of the whey protein and decreased the mechanical properties of the film. These results demonstrate that applying the film as a coating is feasible and effective to improve the shelf life of bakery products with a high moisture content. This nanocomposite film is easy to produce and has potential applications in the food industry.

Effects of Fermentation on the Quality, Structure, and Nonnutritive Contents of Lentil (Lens culinaris) Proteins

Protein digestibility, secondary protein structure components, sugars, and phenolic compounds were analysed to investigate the effect of fermentation on the quality, structure, digestibility, and nonnutritive contents of lentil (Lens culinaris) proteins (LPs). Fermentation was carried out using water kefir seed. The initial pH of the unfermented LPs (6.8) decreased to pH 3.4 at the end of the fermentation on day 5. Protein digestibility increased from 76.4 to 84.1% over the 5 days of fermentation. Total phenolic content increased from 443.4 to 792.6 mg of GAE/100 g after 2 days of fermentation, with the sums of the detected phenolic compounds from HPLC analysis reaching almost 500 mg/100 g. The predominant phenolic compounds detected in fermented LPs include chlorogenic and epicatechin, while traces of rutin, ferulic acid, and sinapic acid were observed. Fermentation played a major role in the changes of the components in the secondary protein structure, especially the percentage of α -helices and random coils. In addition, the reduction in α -helix: β -sheet ratio with the increase in protein digestibility was related to the prolongation of the fermentation time. The model used in this research could be a robust tool for improving protein quality, protein degradation, and nonnutritive nutrients using water kefir seed fermentation.

Seven SNPs in the Coding Sequence of Leptin Receptor Gene in Long-term Selected Japanese Quail Lines

The objective of this study was to identify SNPs in the coding sequence of the leptin receptor gene and to test for their possible association with 20 economically advantageous traits in 15 generations of 2 selected (HBW and LBW) and a control of japanase quail. A 350-bp part of the leptin receptor coding region was amplified and sequenced and understood that the fragment contained 7 SNPs (GenBank:KP674322.1-KP674328.1) that were detected in 5 loci (T3216C, T3265C, T3265G, C3265G, T3303C, A3311G, and T3347C) in a total of 30 individuals. The T3216C and T3303C SNPs located at the end of the codon were synonymous and did not affect the presence of proline. However, phenylalanine, leucine and valine were produced when the T3265C, T3265G and C3265G SNPs, respectively, were present. Glutamine or arginine was produced when the A3311G SNP was A or G, respectively, and serine was produced when the T3347C SNP was C. Although codons and amino acid sequences changed due to the second SNP, the secondary protein structure was not changed. However, the fourth and fifth SNPs changed both the amino acid sequences and secondary protein structure. Pairing the SNP loci with phenotypic traits created haplogroups. When all individuals were evaluated together, some of the differences between the haplogroups were statistically significant (p<0.05; p<0.01). These results showed that both the sequence and structure of the leptin receptor gene could be altered by long-term selection. However, to achieve a more precise understanding of the role of leptin, entire coding sequences of leptin and the leptin receptor should be studied.