The recent surge in environmental awareness and consumer demand for stable, healthy, and safe foods has led the packaging and food sectors to focus on developing edible packaging materials to reduce waste. Edible films and coatings as a modern sustainable packaging solution offer significant potential to serve as a functional barrier between the food and environment ensuring food safety and quality. Whey protein is one of the most promising edible biopolymers in the food packaging industry that has recently gained much attention for its abundant nature, safety, and biodegradability and as an ecofriendly alternative of synthetic polymers. Whey protein isolate and whey protein concentrate are the two major forms of whey protein involved in the formation of edible films and coatings. An edible whey film is a dry, highly interacting polymer network with a three-dimensional gel-type structure. Films/coatings made from whey proteins are colorless, odorless, flexible, and transparent with outstanding mechanical and barrier properties compared with polysaccharide and other-protein polymers. They have high water vapor permeability, low tensile strength, and excellent oxygen permeability compared with other protein films. Whey protein-based films/coatings have been successfully demonstrated in certain foods as vehicles of active ingredients (antimicrobials, antioxidants, probiotics, etc.), without considerably altering the desired properties of packaging films that adds value for subsequent industrial applications. This review provides an overview of the recent advances on the formation and processing technologies of whey protein-based edible films/coatings, the incorporation of additives/active ingredients for improvement, their technological properties, and potential applications in food packaging.

In 2018, the worldwide consumption of meat was 346.14 million tonnes, and this is expected to increase in the future. As meat consumption increases, the use of packaging materials is expected to increase along with it. Petrochemical packaging materials which are widely used in the meat processing industry, take a long time to regenerate and biodegrade, thus they adversely affect the environment. Therefore, the necessity for the development of eco-friendly packaging materials for meat processing, which are easily degradable and recyclable, came to the fore. The objective of this review is to describe the application of natural compound-derived edible films with their antioxidant and antibacterial activities in meat and meat products. For several decades, polysaccharides (cellulose, starch, pectin, gum, alginate, carrageenan and chitosan), proteins (milk, collagen and isolated soy protein) and lipids (essential oil, waxes, emulsifiers, plasticizers and resins) were studied as basic materials for edible films to reduce plastic packaging. There are still high consumer demands for eco-friendly alternatives to petrochemical-based plastic packaging, and edible films can be used in a variety of ways in meat processing. More efforts to enhance the physiological and functional properties of edible films are needed for commercial application to meat and meat products.

The whole genome sequence of Lactiplantibacillus plantarum DJF10, isolated from Korean raw milk, is reported, along with its genomic analysis of probiotics and safety features. The genome consists of 29 contigs with a total length of 3,385,113 bp and a GC content of 44.3%. The average nucleotide identity and whole genome phylogenetic analysis showed the strain belongs to Lactiplantibacillus plantarum with 99% identity. Genome annotation using Prokka predicted a total of 3235 genes, including 3168 protein-coding sequences (CDS), 59 tRNAs, 7 rRNAs and 1 tmRNA. The functional annotation results by EggNOG and KEGG showed a high number of genes associated with genetic information and processing, transport and metabolism, suggesting the strain’s ability to adapt to several environments. Various genes conferring probiotic characteristics, including genes related to stress adaptation to the gastrointestinal tract, biosynthesis of vitamins, cell adhesion and production of bacteriocins, were identified. The CAZyme analysis detected 98 genes distributed under five CAZymes classes. In addition, several genes encoding carbohydrate transport and metabolism were identified. The genome also revealed the presence of insertion sequences, genomic islands, phage regions, CRISPR-cas regions, and the absence of virulence and toxin genes. However, the presence of hemolysin and antibiotic-resistance-related genes detected in the KEGG search needs further experimental validation to confirm the safety of the strain. The presence of two bacteriocin clusters, sactipeptide and plantaricin J, as detected by the BAGEL 4 webserver, confer the higher antimicrobial potential of DJF10. Altogether, the analyses in this study performed highlight this strain’s functional characteristics. However, further in vitro and in vivo studies are required on the safety assurance and potential application of L. plantarum DJF10 as a probiotic agent.

Milk protein is a well-known precursor protein for the generation of bioactive peptides using lactic acid bacteria. This study investigated the antioxidant activity of bovine casein hydrolysate after fermentation with Bifidobacterium longum KACC91563 using the 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) assay and total phenolic content (TPC). The antioxidant activities of the 24-h and 48-h hydrolysates were higher than that of the 4-h hydrolysate (2,045.5 and 1,629.3 μM gallic acid equivalents, respectively, vs. 40.3 μM) in the ABTS assay. In contrast, TPC values showed activities of 43.2 and 52.4 μM gallic acid equivalents for the 4-h and 24-h hydrolysates, respectively. Three fractions (≥10 kDa, ≥3 but 10 kDa and 3-10 kDa fractions, respectively). Through liquid chromatography-electrospray ionization-tandem mass spectrometry analysis, 2 peptides, VLSLSQSKVLPVPQK and VLSLSQSKVLPVPQKAVPYPQRDMPIQA, containing the fragment VLPVPQ that has antioxidant properties, were identified in the <3kDa fraction after 24h of hydrolysis. The present study demonstrates the possibility of antioxidant peptide production from bovine casein using Bifidobacterium longum.