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.

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.

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An isolation procedure for proteins from duckweed was optimized based on a previously developed method for protein isolation from sugar beet leaves. Optimization included the protocol for disrupting cells and protein recovery. With the optimized protocol, protein was isolated (protein yield 14.2%, RuBisCO yield 27%). The concentrate was off-white and contained 67.2% protein. The isolation procedure resulted in a large enrichment in RuBisCO (from 48% to 92%). Denaturation of duckweed protein concentrate was observed at 62 °C at pH 7, while heating at pH 4 did not show denaturation peaks. Solubility was good far from the iso-electric point and showed a minimum around pH 5. Gelling was better at pH 7 than at pH 4. At pH 7, duckweed gels were much stronger than soy and only slightly weaker compared to egg white protein, while at pH 4 duckweed gel strength was similar to soy and lower than egg white.

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