The Rehydration Ability of Whey Ingredients

The purpose of this research was to studythe ability of whey protein concentrates (WPC) and whey permeate produced with ultrafiltration of cheese whey to rehydrate. The products studied were cheese whey concentrate witha PDM percentage of 80% (WPC-80), and cheese whey permeate, both produced under the conditions of the PJSC Dairy “Voronezhsky”.WPC-80 and the whey permeate dissolution processes were studied using microscopy. Water-impermeable hydrophobic layers were formed at the boundary, preventing water penetration into dry particles. The result was a higher dissolution timeforWPC-80 compared with whey permeate. When WPC-80 came into contact with water,it initially formed an obtuse wetting angle with a slow change over time. Whey permeate reached the equilibrium wetting angle more quickly. Quickreconditioning of WPC moisture content required avoiding capillary penetration of water, which created a turbulent liquid flow. The application of these ingredients in different food industry areas can reduce the costs for finished products, contribute to cost-effectiveness, increase the total production, and reduce environmental risks. Keywords: whey protein concentrate, whey permeate powder, water-wetting, dissolutio

Features and Possible Applications of Plant Lipid-Binding and Transfer Proteins

In plants, lipid trafficking within and inside the cell is carried out by lipid-binding and transfer proteins. Ligands for these proteins are building and signaling lipid molecules, secondary metabolites with different biological activities due to which they perform diverse functions in plants. Many different classes of such lipid-binding and transfer proteins have been found, but the most common and represented in plants are lipid transfer proteins (LTPs), pathogenesis-related class 10 (PR-10) proteins, acyl-CoA-binding proteins (ACBPs), and puroindolines (PINs). A low degree of amino acid sequence homology but similar spatial structures containing an internal hydrophobic cavity are common features of these classes of proteins. In this review, we summarize the latest known data on the features of these protein classes with particular focus on their ability to bind and transfer lipid ligands. We analyzed the structural features of these proteins, the diversity of their possible ligands, the key amino acids participating in ligand binding, the currently known mechanisms of ligand binding and transferring, as well as prospects for possible application

Do Lipids Influence Gastrointestinal Processing: A Case Study of Major Soybean Allergen Gly m 4

Previously, we have demonstrated that Gly m 4, one of the major soybean allergens, could pass through the Caco-2 epithelial barrier and have proposed a mechanism of sensitization. However, it is not known yet whether Gly m 4 can reach the intestine in its intact form after digestion in stomach. In the present work, we studied an influence of various factors including lipids (fatty acids and lysolipids) on digestibility of Gly m 4. Using fluorescent and CD spectroscopies, we showed that Gly m 4 interacted with oleic acid and LPPG (lyso-palmitoyl phosphatidylglycerol), but its binding affinity greatly decreased under acidic conditions, probably due to the protein denaturation. The mimicking of gastric digestion revealed that Gly m 4 digestibility could be significantly reduced with the change of pH value and pepsin-to-allergen ratio, as well as by the presence of LPPG. We suggested that the protective effect of LPPG was unlikely associated with the allergen binding, but rather connected to the pepsin inhibition due to the lipid interaction with its catalytic site. As a result, we assumed that, under certain conditions, the intact Gly m 4 might be able to reach the human intestine and thereby could be responsible for allergic sensitization

The Rehydration Ability of Whey Ingredients

The purpose of this research was to studythe ability of whey protein concentrates (WPC) and whey permeate produced with ultrafiltration of cheese whey to rehydrate. The products studied were cheese whey concentrate witha PDM percentage of 80% (WPC-80), and cheese whey permeate, both produced under the conditions of the PJSC Dairy “Voronezhsky”.WPC-80 and the whey permeate dissolution processes were studied using microscopy. Water-impermeable hydrophobic layers were formed at the boundary, preventing water penetration into dry particles. The result was a higher dissolution timeforWPC-80 compared with whey permeate. When WPC-80 came into contact with water,it initially formed an obtuse wetting angle with a slow change over time. Whey permeate reached the equilibrium wetting angle more quickly. Quickreconditioning of WPC moisture content required avoiding capillary penetration of water, which created a turbulent liquid flow. The application of these ingredients in different food industry areas can reduce the costs for finished products, contribute to cost-effectiveness, increase the total production, and reduce environmental risks. Keywords: whey protein concentrate, whey permeate powder, water-wetting, dissolutio

How Do Pollen Allergens Sensitize?

Plant pollen is one of the main sources of allergens causing allergic diseases such as allergic rhinitis and asthma. Several allergens in plant pollen are panallergens which are also present in other allergen sources. As a result, sensitized individuals may also experience food allergies. The mechanism of sensitization and development of allergic inflammation is a consequence of the interaction of allergens with a large number of molecular factors that often are acting in a complex with other compounds, for example low-molecular-mass ligands, which contribute to the induction a type 2-driven response of immune system. In this review, special attention is paid not only to properties of allergens but also to an important role of their interaction with lipids and other hydrophobic molecules in pollen sensitization. The reactions of epithelial cells lining the nasal and bronchial mucosa and of other immunocompetent cells will also be considered, in particular the mechanisms of the activation of B and T lymphocytes and the formation of allergen-specific antibody responses

Structural and Immunologic Properties of the Major Soybean Allergen Gly m 4 Causing Anaphylaxis

Gly m 4 is the major soybean allergen, causing birch pollen cross allergic reactions. In some cases, Gly m 4-mediated anaphylaxis takes place, but the causative factors are still unknown. Here, we studied the structural and immunologic properties of Gly m 4 to shed light on this phenomenon. We showed that Gly m 4 retained its structure and IgE-binding capacity after heating. Gly m 4 was cleaved slowly under nonoptimal gastric conditions mimicking duodenal digestion, and IgE from the sera of allergic patients interacted with the intact allergen rather than with its proteolytic fragments. Similar peptide clusters of Bet v 1 and Gly m 4 were formed during allergen endolysosomal degradation in vitro, but their sequence identity was insignificant. Animal polyclonal anti-Gly m 4 and anti-Bet v 1 IgG weakly cross-reacted with Bet v 1 and Gly m 4, respectively. Thus, we supposed that not only conserved epitopes elicited cross-reactivity with Bet v 1, but also variable epitopes were present in the Gly m 4 structure. Our data suggests that consumption of moderately processed soybean-based drinks may lead to the neutralizing of gastric pH as a result of which intact Gly m 4 can reach the human intestine and cause IgE-mediated system allergic reactions

Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3

Plant lipid transfer proteins (LTPs) are known to be clinically significant allergens capable of binding various lipid ligands. Recent data showed that lipid ligands affected the allergenic properties of plant LTPs. In this work, we checked the assumption that specific amino acid residues in the Len c 3 structure can play a key role both in the interaction with lipid ligands and IgE-binding capacity of the allergen. The recombinant analogues of Len c 3 with the single or double substitutions of Thr41, Arg45 and/or Tyr80 were obtained by site-directed mutagenesis. All these amino acid residues are located near the “bottom” entrance to the hydrophobic cavity of Len c 3 and are likely included in the IgE-binding epitope of the allergen. Using a bioinformatic approach, circular dichroism and fluorescence spectroscopies, ELISA, and experiments mimicking the allergen Len c 3 gastroduodenal digestion we showed that the substitution of all the three amino acid residues significantly affected structural organization of this region and led both to a change of the ligand-binding capacity and the allergenic potential of Len c 3