XRT for visualizing microstructure of extruded meat replacers.

X-Ray Tomography (XRT) was used to visualize the microstructure of extruded meat replacers. The high moisture extrudates contained lamella, that became visible upon pulling the extrudate apart. In frozen state, these lamella could be visualized with XRT. The freezing increased the density difference between the water-rich and protein-rich layers, thus increasing the contrast obtained in the XRT. Differences in the physical structure were reflected in the measured structure. In non-frozen samples, no lamella were visible, indicating insufficient contrast. Because of the contrast obtained in frozen samples, we conclude that the XRT technique is a valuable addition to investigate extrudate structure, that can be used to quantify differences in extrudates obtained by for example variation in composition. Here we showed a higher lamella thickness for soy protein isolate (SPI) compared to more fibre-rich soy protein samples.

Entomophagy: Nutritional, ecological, safety and legislation aspects.

Globally, there is a need to seek alternative sources of protein in addition to meat. This has led to considerable interest in edible insects. Such insects form part of cultures and diets in many Asian and African countries, and are an excellent source of essential nutrients, minerals, vitamins and proteins. Furthermore, they have been reported to be sustainable. The ecological importance of insects is related to their short life cycles when reared and farmed. This makes them ideal in mitigating greenhouse gas emissions, cutting land uses and polluted water, and reducing environmental contamination. However, the use of edible insects as food in Europe is minimal. To ensure safety of insects when eaten as food, considerations should be made on: microbiological contamination; toxicological hazards, e.g. chemical hazards and antinutrients; allergenicity issues that are related to different exposures, including injection, ingestion, inhalation and skin contact. In this review, we summarize the nutritional and sustainable values of edible insects, look at safety and legislative measures and we finally discuss future issues.

Traditional consumption of and rearing edible insects in Africa, Asia and Europe.

The traditional consumption of edible insects is common in one third of the world's population, mostly in Latin America, Africa and Asia. There are over one thousand identified species of insects eaten in some stage of their life cycle; and they play important roles in ensuring food security. The most common way to collect insects are from the wild, which is seasonal with limited availability and has an increasing demand resulting in a disruption to the ecosystem. There is a growing interest shown in rearing insects for commercial purposes, and an industrial scale production will be required to ensure steady supplies. Industrial production will need to take into account the living environment of insects, the nutritional composition of their feed and the overall efficiency of the production system. We provide a short overview on the consumption of and rearing insects in Africa, Asia and Europe. For Africa, a snapshot is given for Nigeria, Ghana, Central African Republic, Kenya and Uganda, while the following countries are reported for Asia: China, Japan, Lao People's Democratic Republic, Thailand and Vietnam. In addition, a list of insect species with the highest potential for food and feed in the European Union is provided with some reference to The Netherlands and Finland. The review concludes that there is need to better understand the rearing and farming procedures that will yield high quality edible insects in Africa, Asia and Europe.

The influence of amino acid sequence on structure and morphology of polydiacetylene containing peptide fibres.

A systematic study was performed on the influence of charge and steric hindrance on the assembly into fibres of a series of pentameric peptides based on the well-known ß-sheet forming sequence Gly-Ala-Gly-Ala-Gly, which were N-terminally acylated with pentacosadiynoic acid. To investigate the effect of steric hindrance and charge repulsion on the fibre structure, either the N-terminal or the C-terminal amino acid in the sequence was replaced by a glutamic acid or lysine residue. Furthermore, peptide amphiphiles (PAs) with an amide or a free acid group at the C-terminus were compared. Steric hindrance and charge repulsion were addressed individually by varying the pH during and after fibre preparation. The self-assembled structures were examined with circular dichroism (CD) spectroscopy and transmission electron microscopy (TEM). UV spectroscopy was used to probe the diacetylene packing in the hydrophobic tail, both by polymerisation behaviour and chromatic properties of the polymers. In brief, the assembly was hindered more if the modification was close to the alkyl tail, and glutamic acid brought about a larger effect than lysine. PAs with two charges yielded assemblies which after polymerisation were found to be the most susceptible towards changes in pH, behaving as a colour-based pH sensor. Typically, TEM and UV showed the same trends, indicating that a distorted morphology as observed with TEM is indicative of a poorer molecular packing of the peptide amphiphile fibres, probed via the changes in absorption of the polydiacetylene backbone.

Characterization of heat-set gels from RuBisCO in comparison to those from other proteins.

To anticipate a future shortage in functional proteins, it is important to study the functionality of new alternative protein sources. Native RuBisCO was extracted from spinach, and its gelation behavior was compared to other native proteins from animal and plant origins. Protein gels were analyzed for their mechanical gel properties during small and large deformation and for their microstructure. Heat-induced aggregation and network formation of RuBisCO resulted in gels with unique characteristics compared to, for example, whey protein and egg white protein. Having a very low critical gelling concentration and low denaturation temperature, RuBisCO readily forms a network with a very high gel strength (G', fracture stress), but upon deformation it has a brittle character (low critical strain, low fracture strain). This breakdown behavior can be explained by the dominant role of hydrophobic and hydrogen bonds between RuBisCO molecules during network formation and by the coarse microstructure. RuBisCO was shown to exhibit high potential as a functional ingredient giving opportunities for the design of new textures at low protein concentration.

Incorporation of mesoporous silica particles in gelatine gels: effect of particle type and surface modification on physical properties.

The aim of this work was to investigate the impact of mesoporous silica particles (MSPs) on the physicochemical properties of filled protein gels. We have studied the effect of the addition of different mesoporous silica particles, either bare or functionalized with amines or carboxylates, on the physical properties of gelatine gels (5% w/v). Textural properties of the filled gels were investigated by uniaxial compression, while optical properties were investigated by turbidity. The MSPs were characterized with the objective of correlating particle features with their impact on the corresponding filled-gel properties. The addition of MSPs (both with and without functionalization) increased the stiffness of the gelatine gels. Furthermore, functionalized MSPs showed a remarkable increase in the strength of the gels and a slight reduction in the brittleness of the gels, in contrast with nonfunctionalized MSPs which showed no effect on these two properties. The turbidity of the gels was also affected by the addition of all tested MSPs, showing that the particles that formed smaller aggregates resulted in a higher contribution to turbidity. MSPs are promising candidates for the development of functional food containing smart delivery systems, also being able to modulate the functionality of protein gels.