Design of a Functional Pea Protein Matrix for Fermented Plant-Based Cheese

The production of a fermented plant-based cheese requires understanding the behavior of the selected raw material prior to fermentation. Raw material processing affects physicochemical properties of plant protein ingredients, and it determines their ability to form fermentation-induced protein gels. Moreover, the addition of oil also influences structure formation and therefore affects gel firmness. This study focuses on identifying and characterizing an optimal pea protein matrix suitable for fermentation-induced plant-based cheese. Stability and gel formation were investigated in pea protein matrices. Pea protein isolate (PPI) emulsions with 10% protein and 0, 5, 10, 15, and 20% olive oil levels were produced and further fermented with a starter culture suitable for plant matrices. Emulsion stability was evaluated through particle size, ζ-potential, and back-scattered light changes over 7 h. Gel hardness and oscillation measurements of the fermented gels were taken after 1 and 7 days of storage under refrigeration. The water-holding capacity of the gels was measured after 7 days of storage and their microstructure was visualized with confocal microscopy. Results indicate that all PPI emulsions were physically stable after 7 h. Indeed, ζ-potential did not change significantly over time in PPI emulsions, a bimodal particle size distribution was observed in all samples, and no significant variation was observed after 7 h in any of the samples. Fermentation time oscillated between 5.5 and 7 h in all samples. Higher oil content led to weaker gels and lower elastic modulus and no significant changes in gel hardness were observed over 7 days of storage under refrigeration in closed containers. Water-holding capacity increased in samples with higher olive oil content. Based on our results, an optimal pea protein matrix for fermentation-induced pea protein gels can be produced with 10% protein content and 10% olive oil levels without compromising gel hardness.

Results of the complex evaluation of bryndza cheese and the byproduct milk whey with the use of enzyme MTG and its activity degree during storage

The paper examines the question of using the enzyme microbial transglutaminase (mTG) for bryndza cheese production. Microbial transglutaminase belongs to the enzyme family that catalyzes formation of bonds between amino groups. One of the problems in production of high-protein products, in particular, cheeses from goat milk is flabbiness of the clot. The use of mTG in the technological process would allow strengthening the product protein matrix, thereby improving its commercial characteristics. When performing the histological investigation of cheeses with this enzyme type to characterize the state of the protein matrix, the authors established that the product protein structure was more condensed compared to the control samples (without mTG), which affected cheese consistency. Consistency became more rubbery negatively influencing the product sensory properties, which are important traits for a consumer when buying a product. Using a Brookfield texture analyzer, it was shown that structural-mechanical characteristics were improved by 1.5 times for cheese samples produced from cow milk and by 2 times for goat cheese when mTG was used. Analysis of the enzyme catalytic activity showed that this enzyme retained its activity throughout the whole storage period, which is a potential hazard for human health. After shelf-life expiration, a change in the mTG activity was not more than 5% relative to the initial levels. The enzyme activity retained not only in cheese but also in the by-product — cheese whey, which made its processing more difficult.

Encapsulation of Cinnamic Acid on Plant-Based Proteins: Evaluation by HPLC, DSC and FTIR-ATR

Plant-based protein matrices can be used for the formulation of delivery systems of cinnamic acid. Pumpkin, pea and almond protein matrices were used for the formulation of dried complexes. The matrices were used in varying amounts (1%, 2%, 5% and 10%) whilst the amount of cinnamic acid was maintained constant. The obtained complexes were analyzed by HPLC, DSC and FTIR-ATR. The highest amounts of cinnamic acid were determined on complexes prepared by the lowest amounts of protein matrices, regardless of their type. The highest affinity for cinnamic acid adsorption was determined for the pumpkin protein matrix. DSC analysis revealed that adsorption of cinnamic acid caused an increase in the thermal stability of the almond protein matrix, while the other two matrices had the opposite behavior. The complexation of protein matrices and cinnamic acid was proven by recording the IR spectra. The obtained complexes could have potential applications in food products to achieve enrichment with cinnamic acid as well as proteins.

Physicochemical, Functional, Fatty Acids Profile, Health Lipid Indices, Microstructure and Sensory Characteristics of Walnut-Processed Cheeses

In the present study, processed cheeses fortified with walnut paste (a high source of omega-3 fatty acids) were developed and characterized. In order to identify the best cheese formulation, the effects of different proportions of walnut paste (0, 5, 10, and 15%) on cheese physicochemical, functional, fatty acids profile, health lipid indices (atherogenic and thrombogenic), microstructure, and sensorial characteristics were studied. Results showed that walnut-added samples had significantly (p ≤ 0.05) higher levels of acidity, protein, fat, and ash contents with lower meltability and oil separation index compared to the control. Processed cheeses with walnuts contained significantly (p ≤ 0.05) higher percentages of MUFAs, and ω-3 PUFAs (mainly α-linolenic acid) and significantly (p ≤ 0.05) lower amounts of SFAs (mainly myristic, palmitic and stearic acids) and ω6/ω3 ratio. Scanning Electron Micrograph of processed cheese containing walnut paste showed uniform distribution of walnut in the protein matrix. Processed cheeses made with 5 or 10% walnut paste presented the most acceptable sensory properties. These results indicated that walnut paste supplementation can be used as a nutritional strategy to increase concentrations of human health-promoting fatty acids in processed cheeses while maintaining good sensory and technological properties.

Proton Stimulation Targeting Plaque Magnetite Reduces Amyloid-β Plaque and Iron Redox Toxicity and Improves Memory in an Alzheimer’s Disease Mouse Model

Background: The coexistence of magnetite within protein aggregates in the brain is a typical pathologic feature of Alzheimer’s disease (AD), and the formation of amyloid-β (Aβ) plaques induces critical impairment of cognitive function. Objective: This study aimed to investigate the therapeutic effect of proton stimulation (PS) targeting plaque magnetite in the transgenic AD mouse brain. Methods: A proton transmission beam was applied to the whole mouse brain at a single entrance dose of 2 or 4 Gy to test the effect of disruption of magnetite-containing Aβ plaques by electron emission from magnetite. The reduction in Aβ plaque burden and the cognitive function of the PS-treated mouse group were assayed by histochemical analysis and memory tests, respectively. Aβ-magnetite and Aβ fibrils were treated with PS to investigate the breakdown of the amyloid protein matrix. Results: Single PS induced a 48–87%reduction in both the amyloid plaque burden and ferrous-containing magnetite level in the early-onset AD mouse brain while saving normal tissue. The overall Aβ plaque burden (68–82%) and (94–97%) hippocampal magnetite levels were reduced in late onset AD mice that showed improvements in cognitive function after PS compared with untreated AD mice (p < 0.001). Analysis of amyloid fibrils after exposure to a single 2 or 4 Gy proton transmission beam demonstrated that the protein matrix was broken down only in magnetite-associated Aβ fibrils. Conclusion: Single PS targeting plaque magnetite effectively decreases the amyloid plaque burden and the ferrous-containing magnetite level, and this effect is useful for memory recovery.

Neuroglobin Provides a Convenient Scaffold to Investigate the Triplet-State Properties of Porphyrins by Time-Resolved EPR Spectroscopy and Magnetophotoselection

The photo-excited triplet state of Zn-protoporphyrin IX located in the heme pocket of human neuroglobin has been investigated by time-resolved EPR coupled to magnetophotoselection. The triplet state in the protein matrix has been compared with the model complex in organic glass, considering both non-coordinating and coordinating solvent mixtures. The protein matrix plays an important role in stabilizing the coordination of the embedded chromophore, resulting in a more homogeneous environment relative to that of the chromophore in a glassy solvent, even in the presence of an axial nitrogenous ligand like pyridine. The EPR spectral parameters point out a slow Jahn–Teller interconversion between slightly different triplet states, both in organic solvent and in the protein matrix. The EPR-magnetophotoselection allows us to propose a reinterpretation of the assignment of the Q bands in the electronic absorption spectrum.