Starch-protein interplay varies the multi-scale structures of starch undergoing thermal processing.

Background Egg white proteins (EWPs) are an excellent source of essential amino acids for human nutrition. Also, egg white is commonly used in food processing because of its numerous technological functionalities. Processing can influence the EWPs digestibility and thereby amino acid bioavailability. A better understanding of processing effects on EWPs digestibility enables improving the nutritional value of EWP products. Scope and approach This review elucidates the impact of diverse processing methods on EWPs at molecular level (individual molecules), supramolecular level (aggregated state), and macroscopic level (gelled state). Key findings and conclusions Heat, high pressure, ultrasound, pulsed electric fields, and adsorption at interface can unfold native EWPs, causing exposure of hydrolysis sites and improvement of protein digestibility at molecular level. However, the Maillard glycation of EWPs may restrict the access of digestive enzymes to the proteins and reduce their digestibility. The Maillard reaction can also lower the IgE-binding capacity of ovalbumin, which could potentially reduce allergenicity. At supramolecular level, protein-protein interactions between the unfolded EWPs lead to the formation of aggregates with different morphologies, depending on the pH and ionic strength. The accessibility of digestive enzymes to the cleavage sites of heat-induced spherical aggregates is lower compared to the linear counterparts. However, gels formed from the linear aggregates show high resistance to digestion owing to the dense network of these gels. A combination of processes can increase the impact of digestibility. For instance, quick production of specific bioactive peptides can be achieved by applying enzymatic treatment to EWPs under high pressure.

Effects of thermal, non-thermal and emulsification processes on the gastrointestinal digestibility of egg white proteins

Effect of emulsifying salts replacement with polymerised whey protein isolate on textural, rheological and melting properties of acid casein model processed cheeses

Biopolymers are natural macromolecules that can be utilized for the fabrication of eco-friendly products with the goal of sustainable development. They are highly biocompatible, environmentally benign, and starting reagents/modifiers in many reactions. The physical and mechanical properties of bio-macromolecules/polymers are not up to the mark for direct industrial applications, especially in packaging and product formulations. So they are supposed to undergo a certain degree of modifications or new innovative routes are devised to formulate value-added industrial-grade biopolymers. Mostly, additional co-polymeric units, clay, nanomaterials, and other additives (crosslinkers or initiators) are incorporated during the fabrication process. The available functional groups, modifiable hydrocarbon chains, and unsaturated units make these biomacromolecules or polymers make them one of the reactive reactants or suitable backbones in various polymeric chains for different applications. The surpassing utilization of biopolymers in the biomedical and food packaging industry makes them phenomenal as well as a prime topic in the R&D sector. Also, they play a key role in lowering the overall carbon footprint, particularly in the packaging industry. Due to the global population demands and adverse environmental effects of petrochemicals, biopolymers have gained much attention in every alternate industry, but far more notable in food industries for producing value-added products with commercial importance. They are generally considered to be safe (GRAS) with appropriate appearance, texture, taste, and smell. Further, the nutritional and sensory values of the products can be tuned based on the decided application of the material. Biodegradability gives significant value to all biopolymer-based products for direct human application (in vivo or in vitro). The application in the sector of drug delivery and food sector generates international demand for such polymers. The biopolymers can improve consumers’ expectations, experiences, and simultaneously help in maintaining an ecological balance. This chapter highlights various applications of renewable biopolymers in the food industry. The most relevant biopolymers with high potential in food packaging, food design, functional food ingredient, encapsulation, and food manufacturing have been discussed. Moreover, the information related to the source of biopolymer, types, applications, and future potential in the food industry altogether would provide a better outlook. 

The Scope of Biopolymers in Food Industry

Proteins are essential to human health with enormous food applications. Despite their advantages, plant and animal proteins often exhibit limited molecular flexibility and poor solubility due to hydrogen bonds, hydrophobic interactions, and ionic interactions within their molecular structures. Thus, there is an urgent need to modify the rigid structure of proteins to enhance their stability and functional properties. Ultrasound‐assisted ionic liquid (UA‐IL) treatment for developing compound modification and producing proteins with excellent functional properties has received interest. However, no review specifically addresses the interactions between UA‐ILs and proteins. Hence, this review focused on recent research advancements concerning the effects and potential reaction mechanisms of UA‐ILs on the physicochemical properties (including particle size; primary, secondary, and tertiary structure; and surface morphology) as well as the functionality (such as solubility, emulsifying properties, and foaming ability) of proteins. Moreover, the safety evaluation of modified proteins was also discussed from various perspectives, such as acute and chronic toxicity, genotoxicity, cytotoxicity, and environmental and microbial toxicity. This review demonstrated that UA‐IL treatment‐induced protein structural changes significantly impact the functional characteristics of proteins. This treatment approach efficiently promotes protein structure stretching and spatial rearrangement through cavitation, thermal effects, and ionic interactions. As a result, the functional properties of modified proteins exhibited an obvious enhancement, thereby bringing more opportunities to utilize modified protein products in the food industry. Potential future directions for protein modification using UA‐ILs were also proposed.

How does ultrasound‐assisted ionic liquid treatment affect protein? A comprehensive review of their potential mechanisms, safety evaluation, and physicochemical and functional properties

Whey Protein Structure and Denaturation and Interactions with Other Food Components

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Whey Protein Structure and Denaturation and Interactions with Other Food Components