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.

The techno-functional properties of ovomucin as a gel-forming agent and its biological properties are well-known. The aim of the present study was to investigate antioxidant activity in ovomucin hydrolysate using radical scavenging assays. Electrophoresis showed that ovomucin isolated from whole egg was well separated. Ovomucin hydrolysis was carried out using microbial protease according to different incubation times. These ovomucin hydrolysates exhibited 85% antioxidant activity as measured by the 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) assay after a 2 h incubation with protease and retained 90% activity until 24 h. At an incubation time of 4 h, the activity of ovomucin hydrolysates reached approximately 90%, corresponding to 115 μM gallic acid equivalent, regardless of the proteases used. The partially purified fraction of the hydrolysate by ultrafiltration and reverse-phase high-performance liquid chromatography was collected and then analyzed by liquid chromatography electrospray ionization mass spectrometry. Two peptides, LDEPDPL and NIQTDDFRT, in this fraction were identified. The antioxidant activities of these two synthesized peptides were measured to be 51.8 and 24.7% by the 2,2-diphenyl-1-picrylhydrazyl assay.