Physical effects upon whey protein aggregation for nano-coating production

Production of edible nanostructures constitutes a major challenge in food nanotechnology, and has attracted a great deal of interest from several research fields — including (but not limited to) food packaging. Furthermore, whey proteins are increasingly used as nutritional and functional ingredients owing to their important biological, physical and chemical functionalities. Besides their technological and functional characteristics, whey proteins are generally recognized as safe (GRAS). Denaturation and aggregation kinetics behavior of such proteins are of particular relevance toward manufacture of novel nanostructures possessing a number of potential uses. When these processes are properly engineered and controlled, whey proteins may form nanostructures useful as carriers of bioactive compounds (e.g. antimicrobials, antioxidants and nutraceuticals). This review discusses the latest advances in nano-scale phenomena involved in protein thermal aggregation aiming at formation of bio-based nano-coating networks. The extent of aggregation is dependent upon a balance between molecular interactions and environmental factors; therefore, the impact of these conditions is addressed in a critical manner. A particular emphasis is given to the effect of temperature as long as being one of the most critical variables. The application of moderate electric fields (MEF), an emergent approach, as such or combined with conventional heating is considered as it may inhibit/prevent excessive denaturation and aggregation of whey proteins — thus opening new perspectives for development of innovative protein nanostructures (i.e. nano-coatings). A better understanding of the mechanism(s) involved in whey protein denaturation and aggregation is crucial as it conveys information relevant to select methods for manipulating interactions between molecules, and thus control their functional properties in tailor-made applications in the food industry.     

Antimicrobial peptides generated from milk proteins: a survey and prospects for application in the food industry. A review

Milk proteins constitute a natural reservoir of bioactive peptides with physiological and/or antimicrobial properties, the release of which requires hydrolysis of the precursor molecules by digestive proteases or by fermentation with proteolytic micro‐organisms. Depending on the digestive or microbial proteases used, an array of bioactive peptides would be released either from caseins or whey proteins, but only a small part of these peptides has so far been identified and characterised with respect to their antimicrobial activity. The antimicrobial peptides known thus far have proven to be potent inhibitors to the growth of a wide range of undesirable micro‐organisms of health or spoilage significance. Nevertheless, previous research work has largely been oriented towards their possible application in medicine, which has hindered their high potential as food‐grade biopreservatives and/or as supplements in functional foods. This review attempts to study the literature pertaining to antimicrobial peptides derived from major milk proteins (caseins, α‐lactalbumin and β‐lactoglobulin) upon hydrolysis either by digestive proteases or by fermentation with proteolytic lactic acid bacteria. Their possible application in the food industry and their mechanism of action will also be discussed. Reference antimicrobial peptides produced by living micro‐organisms as innate immune defence components against microbial infections will occasionally be invoked for comparison purposes.     

Functional Biopolymer Particles: Design,Fabrication, and Applications

Abstract: Biopolymer nano‐ and micro‐particles, fabricated from either proteins and/or polysaccharides, can be utilized as delivery systems or to modulate the physicochemical and sensory characteristics of food products. This article reviews the principles underlying the design, fabrication, and application of biopolymer particles fabricated from globular proteins, used either alone or in combination with polysaccharides, within the food industry. The properties of biopolymer particles and their impact on the physicochemical and functional properties of foods are described. The molecular characteristics and interactions of the building blocks (proteins and polysaccharides) used to assemble these particles are briefly reviewed. The major structural design principles that can be used to fabricate biopolymer particles from food‐grade proteins and polysaccharides are outlined. Finally, some of the potential applications of functional biopolymer particles within foods are highlighted.     

Hierarchical mesoporous silica materials for separation of functional food ingredients — A review

Recently developed mesoporous silica materials are proposed as adsorbents for the separation of food bioactive molecules, due to their narrow pore size distributions and high surface area. These materials can be synthesised with a variety of porous architectures with uniform pore sizes in the mesoporous range, making them attractive candidates for adsorption of biomacromolecules. Research on these materials to date has largely focused on their synthesis, characterisation and applications in catalysis. However, recent developments in the bioadsorption ability and capacity as well as the aqueous stability of mesoporous materials demonstrate their potential as adsorbents for separations in the food industry. This paper reviews the research in this area and identifies the challenges remaining for the application of these materials in food based separations.Industrial relevanceThe increasing demand for health-promoting foods is a key driver for the development of highly selective, cost-effective separation technologies for food bioactive molecules. Separation and purification stages in industrial biotechnology processes can account for up to 70% of the capital and operating costs. A significant portion of the functional food market is devoted to dairy functional foods and ingredients, as milk and whey provide rich sources of bioactive proteins and peptides with a variety of biological and nutritional properties. Hence this paper focuses upon the potential for use of hierarchical mesoporous silica materials for separation of functional food ingredients, taking dairy streams as a representative example.     

Whey protein concentrates and isolates: Processing and functional properties

Substantial progress has been made in understanding the basic chemical and structural properties of the principal whey proteins, that is, β‐lactoglobulin β‐Lg), α‐lactalbumin (α‐La), bovine serum albumin (BSA), and immunoglobulin (Ig). This knowledge has been acquired in terms of: (1) procedures for isolation, purification, and characterization of the individual whey proteins in buffer solutions; and (2) whey fractionation technologies for manufacturing whey protein concentrates (WPC) with improved chemical and functional properties in food systems. This article is a critical review of selected publications related to (1) whey fractionation technology for manufacturing WPC and WPI; (2) fundamental properties of whey proteins; and (3) factors that affect protein functionality, that is, composition, protein structure, and processing.     

Whey as a source of peptides with remarkable biological activities

The dairy industry generates increased amounts of whey from both cheese and casein production facilities. Whey presents an elevated content of lactose and proteins, which are associated with its high biological oxygen demand and decomposing potential. Despite its potential as pollutant, whey has been considered as a dairy by-product due to its nutritional, functional and bioactive properties. The use of enzyme technology may be an interesting strategy to convert whey into added-value products. The hydrolysis of whey proteins can generate bioactive peptides, which are described to perform physiological effects in vivo, such as antioxidant, antimicrobial, antihypertensive and antidiabetic activities. Bioactive peptides derived from whey proteins have been also associated with immunomodulatory, anticancer, opioid and hypocholesterolemic activities. This review presents a discussion on the main biological activities of peptides derived from whey proteins.     

Food‐Grade Covalent Complexes and Their Application as Nutraceutical Delivery Systems: A Review

Food proteins, polysaccharides, and polyphenols are 3 major food constituents with distinctly different functional attributes. Many proteins and polysaccharides are capable of stabilizing emulsions and foams, thickening solutions, and forming gels, although they differ considerably in their abilities to provide these functional attributes. Many plant polyphenols exhibit beneficial physiological functions, such as antitumor, antioxidant, antibacterial, and antiviral properties. Proteins, polysaccharides, and polyphenols can form complexes with each other, which leads to changes in the functional and nutritional properties of the combined systems. Recently, there has been considerable interest in understanding and utilizing covalent interactions between polyphenols and biopolymers (proteins and polysaccharides). The binary or tertiary conjugates formed may be designed to have physicochemical properties and functional attributes that cannot be achieved using the individual components. This article provides a review of the formation, characterization, and utilization of conjugates prepared using proteins, polysaccharides, and polyphenols. It also discusses the relationship between the structural properties and functionality of the conjugates, and it highlights the bioavailability of bioactive compounds loaded in conjugate‐based delivery systems. In addition, it highlights the main challenges to be considered when preparing and analyzing conjugates. This article provides an improved understanding of the chemical reactions that occur between major food ingredients and how they can be utilized to develop biopolymer‐based delivery systems with enhanced functional attributes.     

Functional and Biological Properties of Peptides Obtained by Enzymatic Hydrolysis of Whey Proteins

The study of peptides released by enzymatic hydrolysis of whey proteins has been initially focusing on improving their functional properties in food model systems. Our first study showed that peptides 41 to 60 and 21 to 40 from β-lactoglobulin (β-LG) were responsible for improved emulsifying properties of a tryptic hydrolysate of whey protein concentrate (WPC). Further work showed that adding negatively charged peptides from tryptic hydrolysates of WPC could prevent phase separation of dairy-based concentrated liquid infant formula, as a replacement for carrageenan. Hydrolysis of whey proteins using a bacterial enzyme was also successful in improving heat stability of whey proteins in an acidic beverage. Some tryptic peptides demonstrated improvement in the heat stability and in modifying thermal aggregation of whey proteins. Recent research has shown that whey peptides could trigger some physiological functions. Within the scope of this research our work has led to the development of a whey protein enzymatic hydrolysate that has demonstrated antihypertensive properties when orally administered to spontaneously hypertensive rats and human subjects. Our work then focused on the fractionation of hydrolysates by nanofiltration to prepare specific peptidic fractions; however, peptide/peptide and peptide/protein interactions impaired membrane selectivity. The study of those interactions has lead to the demonstration of the occurrence of interactions between β-LG and its hydrophobic fragment 102–105 (opioid peptide), which probably binds in the central cavity of the protein. This latest result suggests that β-LG could be used as a carrier for the protection of bioactive peptides from gastric digestion. Our work therefore has shown that the enzymatic hydrolysis of whey proteins is not only improving their functional properties, but it is also providing powerful technology in the exploitation of their biological properties for functional foods and nutraceutical applications.     

Design of Nano-Laminated Coatings to Control Bioavailability of Lipophilic Food Components

ABSTRACT:  There is currently a lack of effective delivery systems to encapsulate, protect, and release bioactive lipophilic components, such as ω-3 fatty acids, conjugated linoleic acid, tributyrin, vitamins, antioxidants, carotenoids, and phytosterols, which is holding back the development of functional foods designed to combat diseases such as coronary heart disease, diabetes, hypertension, and cancer. Delivery systems consisting of lipid droplets encapsulated by nano-laminated biopolymer coatings have great potential for use in the food industry for the encapsulation, protection, and release of bioactive lipids.
This article reviews the potential impact of the physicochemical characteristics of nano-laminated biopolymer coatings on the bioavailability of encapsulated lipids. The effects of layer thickness, composition, electrical charge, permeability, and environmental responsiveness on digestion, release, and absorption of lipophilic components are highlighted. The possibility of designing nano-laminated biopolymer coatings to increase, decrease, or control the bioavailability of encapsulated lipids is shown. Data generated from  in vitro  digestion models and animal feeding studies are presented. This knowledge could be used by the food industry to produce functional foods designed to improve human health and wellness.     

Predictive Response Surface Model for Heat‐Induced Rheological Changes and Aggregation of Whey Protein Concentrate

Whey proteins are now far more than a by‐product of cheese processing. In the last 2 decades, food manufacturers have developed them as ingredients, with the dairy industry remaining as a major user. For many applications, whey proteins are modified (denatured) to alter their structure and functional properties. The objective of this research was to study the influence of 85 to 100 °C, with protein concentration of 8% to 12%, and treatment times of 5 to 30 min, while measuring rheological properties (storage modulus, loss modulus, and complex viscosity) and aggregation (intermolecular beta‐sheet formation) in dispersions of whey protein concentrate (WPC). A Box–Behnken Response Surface Methodology modeled the heat denaturation of liquid sweet WPC at 3 variables and 3 levels. The model revealed a very significant fit for viscoelastic properties, and a lesser fit for protein aggregation, at temperatures not previously studied. An exponential increase of rheological parameters was governed by protein concentration and temperature, while a modest linear relationship of aggregation was governed by temperature. Models such as these can serve as valuable guides to the ingredient and dairy industries to develop target products, as whey is a major ingredient in many functional foods.     

κ-Casein Macropeptides from Cheese Whey: Physicochemical, Biological, Nutritional, and Technological Features for Possible Uses

κ-Casein macropeptide (CMP), one of the components of whey, is produced during cheese making. Whey production has grown enormously in the last three decades and will continue to grow, along with cheese production. There is an increased interest in research for new applications of food industry by-products in order to avoid their extensive elimination and negative environmental implications. In this respect, CMP has been the focus of extensive scientific research that has proven its value as a functional and bioactive peptide, as well as a source of biologically active peptides. This article evaluates the possibilities and future perspectives of the use of CMP and related peptides obtained from cheese whey from different ruminant species. Physicochemical, technological, biological, and nutritional aspects are considered, and processes for analysis, fractionation, and separation are reviewed. The objective is to help to promote further exploitation of cheese industry coproducts for the preparation of high added-value ingredients to be included in the composition of nutraceuticals or functional food products.     

κ-Casein Macropeptides from Cheese Whey: Physicochemical,Biological, Nutritional,and Technological Features for Possible Uses

Abstract

κ-Casein macropeptide (CMP), one of the components of whey, is produced during cheese making. Whey production has grown enormously in the last three decades and will continue to grow, along with cheese production. There is an increased interest in research for new applications of food industry by-products in order to avoid their extensive elimination and negative environmental implications. In this respect, CMP has been the focus of extensive scientific research that has proven its value as a functional and bioactive peptide, as well as a source of biologically active peptides. This article evaluates the possibilities and future perspectives of the use of CMP and related peptides obtained from cheese whey from different ruminant species. Physicochemical, technological, biological, and nutritional aspects are considered, and processes for analysis, fractionation, and separation are reviewed. The objective is to help to promote further exploitation of cheese industry coproducts for the preparation of high added-value ingredients to be included in the composition of nutraceuticals or functional food products.     

Starch–lipid and starch–lipid–protein complexes: A comprehensive review

Physical interactions often occur between major food components during food processing. These interactions may involve starch, lipids, and proteins forming V‐type starch–lipid complexes or ternary starch–lipid–protein complexes of larger molecular size and greater structural order. Complexes between starch and lipids have been the subject of intensive research for over half a century, whereas the study of starch–lipid–protein complexes is a relatively new field with only a limited amount of knowledge being gained so far. The formation of these complexes can significantly affect the functional and nutritional properties of finished food products in terms of flavor, texture, shelf life, and digestibility. This article provides a comprehensive review of starch–lipid and starch–lipid–protein complexes, including their classification, factors affecting their formation and structure, and preparative and analytical methods. The review also considers how complexes affect the physicochemical and functional properties of starch, including digestibility, and potential applications in the food industry.     

Protein deamidation to produce processable ingredients and engineered colloids for emerging food applications

With the ever-increasing demands for functional and sustainable foods from the general public, there is currently a paradigm shift in the food industry toward the production of novel protein-based diet. Food scientists are therefore motivated to search for natural protein sources and innovative technologies to modify their chemical structure for desirable functionality and thus utilization. Deamidation is a viable, efficient, and attractive approach for modifying proteins owing to its ease of operating, specificity, and cost-effective processes. Over the past three decades, the knowledge of protein deamidation for food applications has evolved drastically, including the development of novel approaches for deamidation, such as protein-glutaminase and ion exchange resin, and their practices in new protein substrate. Thanks to deamidation, enhanced functionalities of food proteins from cereals, legumes, milk, oil seeds and others, and thereby their processabilities as food ingredients have been achieved. Moreover, deamidated proteins have been used to fabricate engineered food colloids, including self-assembled protein particles, protein–metallic complexes, and protein–carbohydrate complexes, which have demonstrated tailored physicochemical properties to modulate oral perception, improve gastrointestinal digestion and bioavailability, and protect and/or deliver bioactive nutrients. Novel bioactivity, altered digestibility, and varied allergenicity of deamidated proteins are increasingly recognized. Therefore, deamidated proteins with novel techno-functional and biological properties hold both promise and challenges for future food applications, and a comprehensive review on this area is critically needed to update our knowledge and provide a better understanding on the protein deamidation and its emerging applications.     

Characterisation of hydrogels and aerogels as carriers for sea buckthorn pomace extract

In this study, aerogels were prepared from kognac glucomannan (KG) or whey proteins loaded with bioactive sea buckthorn pomace extract. KG was diacetylated with Na₂CO₃ (0.1; 0.2; 0.3; 0.4 m ) resulting hydrogel formation that were further freeze-dried to obtain an aerogel structure. Whey protein aerogels were prepared by removing pore fluid from alcogels using supercritical CO₂ drying. Produced aerogels evaluated for microstructure, porosity, specific surface area, absorption capacity, encapsulation efficiency and antioxidant capacity of the extract. It was found that higher concentration of alkali induced higher hardness, resilience and elastic modulus values. It was also obtained that pores in the konjac glucomannan aerogels were irregular in shape and a decrease in total pore volume (0.026 to 0.019 cc/g) and surface area (12.39 to 11.40 m²/g) after increasing the carbonate concentration was observed. These aerogels were found to have better encapsulation efficiency properties for sea buckthorn pomace extract (17 to 20%) in comparison to whey protein aerogels (0.05 to 0.36%). Overall, the KG aerogels show potential for applications in the food industry as a carrier of bioactive sea buckthorn pomace extract, while whey proteins must be used in combination with other biopolymers to enhance their bioactive compound loading capacity.     

Complexation between milk proteins and polysaccharides via electrostatic interaction: principles and applications – a review

This article details recent research conducted on the complexation between milk proteins and polysaccharides and the properties of the complexes, and the application of such relationships to the food industry. Complexation between proteins and polysaccharides through electrostatic interactions gives either soluble complexes in a stable solution or insoluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio of protein to polysaccharide, charge density of protein and polysaccharide as well as processing conditions (temperature, shearing and time). The functional properties of milk proteins, such as solubility, surface activity, conformational stability, gel‐forming ability, emulsifying properties and foaming properties, are improved through the formation of complexes with polysaccharides. These changes in the functional properties provide opportunities to create new ingredients for the food industry.     

Role of whey proteins in combating geriatric disorders

Ageing in humans is usually accompanied by deterioration in physical fitness and increased susceptibility to disease, adding to the economic burden of the person concerned. Inadequate food intake, reduced desire to eat, decline in food digestion or absorption, compromise in nutritional metabolic pathways, poor dental hygiene or preponderance of chronic diseases, which are commonly found in the elderly, can lead to an increased risk of under‐nutrition. Adequate dietary nutrition has an undisputed role in healthy ageing. Among the various nutrients, proteins play an important role in geriatric health. This review emphasizes the nutritional aspects of milk‐based whey proteins and their role in tackling health problems in the geriatric population. Nutritionally rich whey protein constituents such as β‐lactoglobulin, α‐lactalbumin, bovine serum albumin, lactoferrin and proteose peptone have all been reported to have a plethora of functional roles in various biological processes and organ systems in geriatrics and thus help in the management of geriatric health problems through proper nutrition. © 2013 Society of Chemical Industry     

Functional improvement of milk whey proteins induced by high hydrostatic pressure

High pressure is emerging as a new processing technology that produces particular changes in the molecular structure of proteins and thus gives rise to new properties inaccessible via conventional methods of protein modification. This review deals with the main effects of high hydrostatic pressure on the physicochemical characteristics of milk whey proteins and how modifications in their structural properties contribute to functionality. In this paper the mechanism underlying pressure-induced changes in ss-lactoglobulin, a-lactabumin, and bovine serum albumin is explained, and related to functional properties such as gel-forming ability, emulsifying activity, or foaming capacity. The possibility of using high pressures to favor chemical reactions of proteins with other food components, such as carbohydrates, to produce novel molecules with new food uses is also considered.     

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Both intrinsic and extrinsic factors impact amyloid formation of food proteins. We here review the impact of various conditions and food constituents on amyloid fibrillation of milk and legume proteins. Much less is known about casein and legume protein amyloid‐like fibril formation than about that of whey proteins such as β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. Proteins of both sources are often studied after heating under strong acidic (pH < 3) conditions. The latter induces changes in protein conformation and often peptide hydrolysis. At higher pH values, alcohols, chaotropic and/or reducing agents induce the conformational changes required to enhance fibrillation. Different types of food proteins can impact each other's fibrillation. Also, the presence of other food constituents can enhance or reduce it. No general conclusions on the mechanisms or impact of different food constituents on food proteins can be made. Optimal conditions for AF formation, that is, heating for several days at low pH, are rare in food processing. However, this does not exclude the possibility of AF formation in food products. For example, slow cooking of hydrolyzed proteins may enhance it. Future research should focus on the prevalence of AFs in complex food systems or model systems relevant for food processing.     

Electrodialytic phenomena and their applications in the dairy industry: a review

Electrodialysis (ED) is an electrochemical separation process by which electrically-charged species are transportedfrom one solution to another ED is a combined method of dialysis and electrolysis and can be performed with two main cell types: multi-membrane cells for dilution-concentration and water dissociation applications (membrane phenomena), and electrolysis cells for redox reactions (electrode phenomena). The dilution-concentration principle applications in the dairy industry consist mainly of the demineralization of milk or milk by-products. The use of ED with monopolar membrane for protein separation and acid caseinate production, and in bioreactors for organic acid production, is also studied in the dairy industry. The interest of ED as a membrane process has been triggered recently by the development of a new membrane type, bipolar membrane. This membrane carries out the dissociation of water molecules. ED with bipolar membranes was applied very recently to the production of lactic acid from whey product fermentation, production of caseinates, and fractionation of whey proteins. Two principle applications of electrode reactions were published: electrochemical coagulation (EC) to precipitate milk proteins, and electroreduction for the reduction of disulfide bonds in the proteins. It appears in this article that processes using membrane phenomena are more numerous and developed than electrolytic applications. This is the composition of milk and the lack of knowledge of redox reactions of the different food compounds that limit the applications and the development of electrolytic phenomena. Electrodialytic phenomena present a great potential for application in the dairy industry, and more generally, in the food industry; many of these applications have to be discovered.