Encapsulation of food protein hydrolysates and peptides using protein, polysaccharide and lipid carriers is needed to enhance their biostability and bioavailability for application as health-promoting functional food ingredients and nutraceuticals.

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Enzymatic hydrolysis of whey proteins increased the reducing capacity and decreased reactive sulfhydryl (SH) content of the peptides. Hydrolysis yielded Maillard reaction products and the carbonyl compounds depleted SH by nucleophilic reaction.

Prebiotics enhance immune response through the modulation of intestinal microbial activities, production of short chain fatty acids (SCFA), direct interaction with toll‐like receptors and mucin production. These non‐digestible food components are known to be resistant to enzymatic hydrolysis by digestive enzymes and are utilized as carbon source for the growth of beneficial bacteria population through the process of fermentation. Brown seaweed polysaccharides (BSP) have been described as emerging prebiotics due to their potential to stimulate gut microbiota activities at in vitro and in vivo stages. This review therefore examines evidence of the relationship between the prebiotic capacity of BSP, their structure, extraction, and possible mechanisms of immunomodulation. Practical applications Bio‐functional ingredients have been widely explored for numerous health benefits. Of interest to this review are polysaccharides of brown seaweed which have great prebiotic prospects. Prebiotics are important bio‐functional ingredients having the potential to improve immune health. An understanding of the prebiotic and immunomodulatory potential of BSP provides the food industry a novel alternative source of prebiotics. Excerpts from this review will provide background knowledge and advance scientific research into prospects of BSP as prebiotics and a possible commercialization of BSP products.

Top‐down proteomics is emerging as a preferred approach to investigate biological systems, with objectives ranging from the detailed assessment of a single protein therapeutic, to the complete characterization of every possible protein including their modifications, which define the human proteoform. Given the controlling influence of protein modifications on their biological function, understanding how gene products manifest or respond to disease is most precisely achieved by characterization at the intact protein level. Top‐down mass spectrometry (MS) analysis of proteins entails unique challenges associated with processing whole proteins while maintaining their integrity throughout the processes of extraction, enrichment, purification, and fractionation. Recent advances in each of these critical front‐end preparation processes, including minimalistic workflows, have greatly expanded the capacity of MS for top‐down proteome analysis. Acknowledging the many contributions in MS technology and sample processing, the present review aims to highlight the diverse strategies that have forged a pathway for top‐down proteomics. We comprehensively discuss the evolution of front‐end workflows that today facilitate optimal characterization of proteoform‐driven biology, including a brief description of the clinical applications that have motivated these impactful contributions.

Food-derived bioactive proteins and peptides have gained acceptance among researchers, food manufacturers and consumers as health-enhancing functional food components that also serve as natural alternatives for disease prevention and/or management. Bioactivity in food proteins and peptides is determined by their conformations and binding characteristics, which in turn depend on their primary and secondary structures. To maintain their bioactivities, the molecular integrity of bioactive peptides must remain intact, and this warrants the study of peptide form and structure, ideally with robust, highly specific and sensitive techniques. Short single-stranded nucleic acids (i.e. aptamers) are known to have high affinity for cognate targets such as proteins and peptides. Aptamers can be produced cost-effectively and chemically derivatized to increase their stability and shelf life. Their improved binding characteristics and minimal modification of the target molecular signature suggests their suitability for real-time detection of conformational changes in both proteins and peptides. This review discusses the developmental progress of systematic evolution of ligands by exponential enrichment (SELEX), an iterative technology for generating cost-effective aptamers with low dissociation constants (K ) for monitoring the form and structure of bioactive proteins and peptides. The review also presents case studies of this technique in monitoring the structural stability of bioactive peptide formulations to encourage applications in functional foods. The challenges and potential of aptamers in this research field are also discussed. Graphical abstract Advancing bioactive proteins and peptide functionality via aptameric ligands.

Indigestible oligosaccharides (OSs) with specific properties are known to influence overall health status of individuals as well as that of the gastro‐intestinal tract via alteration of the gut microbial composition. These biomolecules selectively stimulate proliferation of desirable bacterial species while inhibiting harmful microbes. Gut microbiota release short chain fatty acids on fermenting these OSs that also promote a healthy gut. Prebiotic activity is resultant of a synergy between the chemical nature of the OSs and the metabolic machinery of beneficial microflora in the human gut. Prebiotic effectiveness of the OSs is also dependent on processing stability during extraction and incorporation into the edible food‐matrix. The present review provides a structural perspective on conventional and potential prebiotic OSs with regards to their effects on colonic microflora, stability and potential application in food systems. Practical applications Altering intestinal microbiota is being viewed as an active mechanism of developing immune resistance, infectious process control and overall health promotion in individuals. Food researchers and segments of the food industry are actively developing products with prebiotic properties looking to maintain health status of the populace and strengthening the competitive market. The insights from this review can drive towards developing food‐incorporated prebiotic formulations from a number of different sources.

The past decade has seen an increased interest in the conversion of food proteins into functional biomaterials, including their use for loading and delivery of physiologically active compounds such as nutraceuticals and pharmaceuticals. Proteins possess a competitive advantage over other platforms for the development of nanodelivery systems since they are biocompatible, amphipathic, and widely available. Proteins also have unique molecular structures and diverse functional groups that can be selectively modified to alter encapsulation and release properties. A number of physical and chemical methods have been used for preparing protein nanoformulations, each based on different underlying protein chemistry. This review focuses on the chemistry of the reorganization and/or modification of proteins into functional nanostructures for delivery, from the perspective of their preparation, functionality, stability and physiological behavior.