No abstract

There is a pressing need to extend the knowledge on the properties of insect protein fractions to boost their use in the food industry. In this study several techno-functional properties of a black soldier fly (Hermetia illucens) protein concentrate (BSFPC) obtained by solubilization and precipitation at pH 4.0–4.3 were investigated and compared with whey protein isolate (WPI), a conventional dairy protein used to stabilize food emulsions. The extraction method applied resulted in a BSFPC with a protein content of 62.44% (Kp factor 5.36) that exhibited comparable or higher values of emulsifying activity and foamability than WPI for the same concentrations, hence, showing the potential for emulsion and foam stabilization. As for the emulsifying properties, the BSFPC (1% and 2%) showed the capacity to stabilize sunflower and lemon oil-in-water emulsions (20%, 30%, and 40% oil fraction) produced by dynamic membranes of tunable pore size (DMTS). It was proved that BSFPC stabilizes sunflower oil-in-water emulsions similarly to WPI, but with a slightly wider droplet size distribution. As for time stability of the sunflower oil emulsions at 25 °C, it was seen that droplet size distribution was maintained for 1% WPI and 2% BSFPC, while for 1% BSFPC there was a slight increase. For lemon oil emulsions, BSFPC showed better emulsifying performance than WPI, which required to be prepared with a pH 7 buffer for lemon oil fractions of 40%, to balance the decrease in the pH caused by the lemon oil water soluble components. The stability of the emulsions was improved when maintained under refrigeration (4 °C) for both BSFPC and WPI. The results of this work point out the feasibility of using BSFPC to stabilize O/W emulsions using a low energy system.

In a preliminary study, commercial insect powders were successfully identified using infrared spectroscopy combined with multivariate analysis. Nonetheless, it is necessary to check if this technology is capable of discriminating, predicting, and quantifying insect species once they are used as an ingredient in food products. The objective of this research was to study the potential of using attenuated total reflection Fourier transform mid-infrared spectroscopy (ATR-FTMIR) combined with multivariate analysis to discriminate doughs and 3D-printed baked snacks, enriched with Alphitobius diaperinus and Locusta migratoria powders. Several doughs were made with a variable amount of insect powder (0–13.9%) replacing the same amount of chickpea flour (46–32%). The spectral data were analyzed using soft independent modeling of class analogy (SIMCA) and partial least squares regression (PLSR) algorithms. SIMCA models successfully discriminated the insect species used to prepare the doughs and snacks. Discrimination was mainly associated with lipids, proteins, and chitin. PLSR models predicted the percentage of insect powder added to the dough and the snacks, with determination coefficients of 0.972, 0.979, and 0.994 and a standard error of prediction of 1.24, 1.08, and 1.90%, respectively. ATR-FTMIR combined with multivariate analysis has a high potential as a new tool in insect product authentication.

Water-in-oil-in-water (W1/O/W2) emulsions are complex delivery systems for polyphenols amongst other bio-actives. To stabilize the oil–water interphase, dairy proteins are commonly employed, which are ideally replaced by other, more sustainable sources, such as insect proteins. In this study, lesser mealworm (Alphitobius diaperinus) protein concentrate (LMPC) is assessed and compared to whey protein (WPI) and pea protein (PPI), to stabilize W1/O/W2 emulsions and encapsulate a commercial polyphenol. The results show that LMPC is able to stabilize W1/O/W2 emulsions comparably to whey protein and pea protein when using a low-energy membrane emulsification system. The final droplet size (d4,3) is 7.4 μm and encapsulation efficiency is between 72 and 74%, regardless of the protein used. Under acidic conditions, the LMPC shows a similar performance to whey protein and outperforms pea protein. Under alkaline conditions, the three proteins perform similarly, while the LMPC-stabilized emulsions are less able to withstand osmotic pressure differences. The LMPC stabilized emulsions are also more prone to droplet coalescence after a freeze–thaw cycle than the WPI-stabilized ones, but they are the most stable when exposed to the highest temperatures tested (90 °C). The results show LMPC’s ability to stabilize multiple emulsions and encapsulate a polyphenol, which opens the door for application in foods.