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Background New developments in next-generation sequencing technologies and massive data received from this approach open wide prospects for personalised medicine and nutrition studies. Metagenomic analysis of the gut microbiota is paramount for the characterization of human health and wellbeing. Despite the intensive research, there is a huge gap and inconsistency between different studies due to the non-standardised and biased pipeline. Methodical and systemic understanding of every stage in the process is necessary to overcome all bottlenecks and grey zones of gut microbiota studies, where all details and interactions between processes are important. Results Here we show that an inexpensive, but reliable iSeq 100 platform is an excellent tool to perform the analysis of the human gut microbiota by amplicon sequencing of the 16 S rRNA gene. Two commercial DNA extraction kits and different starting materials performed similarly regarding the taxonomic distribution of identified bacteria. DNA/RNA Shield reagent proved to be a reliable solution for stool samples collection, preservation, and storage, as the storage of faecal material in DNA/RNA Shield for three weeks at different temperatures and thawing cycles had a low impact on the bacterial distribution. Conclusions Altogether, a thoroughly elaborated pipeline with close attention to details ensures high reproducibility with significant biological but not technical variations.

This study investigated meat analogs produced using low-moisture extrusion from oat and pea protein blends at ratios 20:80, 30:70, 50:50, and 70:30. Response surface methodology was used to assess the effect of blend composition, screw speed (200–1200 rpm), barrel temperature (135–160 °C), and moisture content (25–35%) on the properties of extruded meat analogs. Blend composition had a relatively stronger effect on water holding capacity, water solubility index, bitterness, cohesiveness, and springiness, while extrusion conditions had more influence on hardness, fibrousness, and moistness. As the oat content increased from 20% to 70% the maximum sensory fibrousness increased from 7.2 to 8.6 on a scale of 0–9. Although the mean water holding capacity decreased from 2.1 to 1.4 g g−1, the mean sensory moistness remained around 4.1. Cereal taste dominated over legumes with the mean intensities 3.9 and 2.0, however, the differences between oat-pea blends were small. In general, the extruded meat analogs had a mild flavor and high fibrousness, and the developed response surface models can be used to tune the properties further. This confirms that oat protein in combination with pea is a practical alternative to soy and gluten proteins for the production of meat analogs.

It is evident that the interest in plant-based milk alternative products is increasing, although there are still difficulties with undesired sensorial properties. This study seeks to contribute to sustainable food development through a better understanding of the market situation. The objective of this study was to get a comprehensive overview of 90 plant-based beverages currently available on the Estonian market. Main focus of this research was to map the plant-based beverage market sensorially. To evaluate such a large set of samples, RATA (Rate-All-That-Apply) was explored as a method for market mapping. A wide range of products made from different raw materials was characterized. Sensory analysis was able to make some conclusions based on specific raw materials, as there was a lot of variety among different sample groups. Combining the data collected from sensory and aroma analysis (GC/MS/O) helped to further examine the effect of volatile compounds on sensory properties of various product types. Some key compounds were found in different products, including compounds that may be causing off-flavors.

The kombucha market is a fast-growing segment in the functional beverage category. The selection of kombuchas on the market varies between the traditional and flavoured kombuchas. Our research aimed to characterise the chemical, microbial, and sensory profiles of the commercial kombuchas. We analysed 16 kombuchas from 6 producers. The dominant metabolites were acetate, lactate, and ethanol, the last of which might put some kombuchas into the alcoholic beverage section in some countries. The metagenomic analyses demonstrated that LAB dominates in green tea, and AAB in black tea kombuchas. The main bacterial species were Komagataeibacter rhaeticus and Lactobacillus ssp, and yeast species Dekkera anomala and Dekkera bruxellensis. The sweet and sour balance correlated with acid concentrations. The free sorting task showed that commercial kombuchas clustered into three main categories "fruity and artificial flavour", herbal and tea notes", and "classical notes". Our research results showed the necessity of the definition of kombucha.

Pea protein dry-fractionated (PDF), pea protein isolated (PIs), soy protein isolated (SIs) and oat protein (OP) were combined in four mixes (PDF_OP, PIs_OP, PDF_PIs_OP, SIs_OP) and extruded to produce meat analogues. The ingredients strongly influenced the process conditions and the use of PDF required higher specific mechanical energy and screw speed to create fibrous texture compared to PIs and SIs. PDF can be conveniently used to produce meat analogues with a protein content of 55 g 100 g&minus, 1, which is exploitable in meat-alternatives formulation. PDF-based meat analogues showed lower hardness (13.55&ndash, 18.33 N) than those produced from PIs and SIs (nearly 27 N), probably due to a more porous structure given by the natural presence of carbohydrates in the dry-fractionated ingredient. PDF_OP and PIs_PDF_OP showed a significantly lower water absorption capacity than PIs OP and SIs_OP, whereas pea-based extrudates showed high oil absorption capacity, which could be convenient to facilitate the inclusion of oil and fat in the final formulation. The sensory evaluation highlighted an intense odor and taste profile of PDF_OP, whereas the extrudates produced by protein isolates had more neutral sensory characteristics. Overall, the use of dry-fractionated protein supports the strategies to efficiently produce clean-labeled and sustainable plant-based meat analogues.

Plant materials that are used for the production of extruded meat analogs are often nutritionally incomplete and also contain antinutrients, thus there is a need to explore alternative plant proteins and pre-treatments. This study demonstrates application of phytase and fermentation to a pea-oat protein blend with a good essential amino acid profile and subsequent texturization using extrusion cooking. Enzymatic treatment reduced the content of antinutrient phytic acid by 32%. Extrusion also degraded phytic acid by up to 18%, but the effect depended on the material. Differences in physicochemical, sensorial, and textural properties between untreated and phytase-treated extruded meat analogs were small. In contrast, fermented material was more difficult to texturize due to degradation of macromolecules, physicochemical and textural properties of extrudates were markedly different, sensory analysis showed enhancement of flavor, but also detected an increase in some unwanted taste attributes (bitterness, cereal and off-taste). Phytic acid was not degraded by fermentation. Analysis of volatile compounds showed extrusion eliminated volatiles from the raw material but introduced Maillard reaction products. Overall, phytase treatment and fermentation demonstrated the potential for application in extruded meat analogs but also highlighted the necessity of optimization of process conditions.

Isothermal microcalorimetry was used to study the exothermic heat flow caused by the absorption of water into carrageenans and a furcellaran, leading to their thermodynamic instability under moderate storage conditions (35 °C, τ = 12 h), where τ is the reaction time (h). The net heats evolved by furcellaran, ι-carrageenan, κ-carrageenan, and a mixture of κ/λ-carrageenan were 43.5 J/g, 45.9 J/g, 31.6 J/g, and 28.1 J/g, respectively. The pronounced exothermic behavior of furcellaran was attributed to the enthalpic association of water molecules with the thermally degraded carbohydrate matrix. The responses of a heat treatment of carrageenans at 55 °C, 85 °C, and 105 °C for 15 min on exothermic heat Q (J/g) at different water activities (aw = 0.26, 0.51, 0.76, and 1.0) were measured. The dependence of the net recorded heat Q on water activity can be satisfactorily approximated by the equation Q = a[1 − (1 − aw)b], where a and b are the coefficients found by the nonlinear least-squares method. It was concluded that carrageenans affected by excessive heat treatment should be preferably stored with limited water access.

Ice-binding proteins (IBPs) bind to ice crystals and control their growth, enabling host organisms to adapt to subzero temperatures. By binding to ice, IBPs can affect the shape and recrystallization of ice crystals. The shapes of ice crystals produced by IBPs vary and are partially due to which ice planes the IBPs are bound to. Previously, we have described a bacterial IBP found in the metagenome of the symbionts of Euplotes focardii ( EfcIBP). EfcIBP shows remarkable ice recrystallization inhibition activity. As recrystallization inhibition of IBPs and other materials are important to the cryopreservation of cells and tissues, we speculate that the EfcIBP can play a future role as an ice recrystallization inhibitor in cryopreservation applications. Here we show that EfcIBP results in a Saturn-shaped ice burst pattern, which may be due to the unique ice-plane affinity of the protein that we elucidated using the fluorescent-based ice-plane affinity analysis. EfcIBP binds to ice at a speed similar to that of other moderate IBPs (5 ± 2 mM-1 s-1); however, it is unique in that it binds to the basal and previously unobserved pyramidal near-basal planes, while other moderate IBPs typically bind to the prism and pyramidal planes and not basal or near-basal planes. These insights into EfcIBP allow a better understanding of the recrystallization inhibition for this unique protein

Ice-binding proteins (IBPs), also known as antifreeze proteins, were added to ice cream to investigate their effect on structure and texture. Ice recrystallization inhibition was assessed in the ice cream mixes using a novel accelerated microscope assay and the ice cream microstructure was studied using an ice crystal dispersion method. It was found that adding recombinantly produced fish type III IBPs at a concentration 3 mg·L−1 made ice cream hard and crystalline with improved shape preservation during melting. Ice creams made with IBPs (both from winter rye, and type III IBP) had aggregates of ice crystals that entrapped pockets of the ice cream mixture in a rigid network. Larger individual ice crystals and no entrapment in control ice creams was observed. Based on these results a model of ice crystals aggregates formation in the presence of IBPs was proposed.

In the production of biopolymers, the processing operations (e.g. extraction and drying) involve some degradation of the polysaccharide-causing structural and functional changes in final products. In this study, short-term heat treatment (75–115 °C, 15 min) influence on commercial carrageenans' — furcellaran, κ-carrageenan, ι-carrageenan and a κ/λ-carrageenan — structure, molecular weight and gel rheology was studied. Compared with other carrageenans, commercial furcellaran that had undergone multiple heatings at high temperatures during production was found to be susceptible to polymer degradation. Heat caused the desulphation and degradation of furcellaran galactans and the molecular weight was significantly decreased, causing a drop in viscosity and gel hardness. The loss of the network cross-linking of furcellaran gels was confirmed by scanning electron microscopy. Carrageenan gel storage modulus values decreased with the increase in the temperature of the treatment. The greatest decrease in storage modulus values occurred with κ/λ-carrageenan gels, followed by ι-carrageenan > furcellaran > κ-carrageenan., Carrageenan; NMR; Molecular weight; Rheology

Ice-binding proteins (IBPs) contribute to the survival of many living beings at subzero temperature by controlling the formation and growth of ice crystals. This work investigates the structural basis of the ice-binding properties of EfcIBP, obtained from Antarctic bacteria. EfcIBP is endowed with a unique combination of thermal hysteresis and ice recrystallization inhibition activity. The three-dimensional structure, solved at 0.84 A resolution, shows that EfcIBP belongs to the IBP-1 fold family, and is organized in a right-handed β-solenoid with a triangular cross-section that forms three protein surfaces, named A, B, and C faces. However, EfcIBP diverges from other IBP-1 fold proteins in relevant structural features including the lack of a 'capping' region on top of the β-solenoid, and in the sequence and organization of the regions exposed to ice that, in EfcIBP, reveal the presence of threonine-rich ice-binding motifs. Docking experiments and site-directed mutagenesis pinpoint that EfcIBP binds ice crystals not only via its B face, as common to other IBPs, but also via ice-binding sites on the C face. Database Coordinates and structure factors have been deposited in the Protein Data Bank under accession number 6EIO.

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