The aim of this study was to spur the lipid accumulation by larvae of Hermetia illucens or black soldier fly (BSFL) via feeding with yeast fermented medium. The Saccharomyces cerevisiae, a single cell yeast, was introduced at different concentrations (0.02, 0.1, 0.5, 1.0, 2.5 wt %) to execute an in-situ fermentation on coconut endosperm waste. The rearing of BSFL was started simultaneously and the rearing was stopped once the BSFL reached the fifth instar. With the increasing of yeast concentration, the rearing duration of BSFL was shortened from 15.5 to 13.5 days. Moreover, it was found that at 0.5 to 1.0 wt % yeast concentration, the lipid yield and lipid productivity of BSFL were statistically enhanced to their highest peaks, namely, at 49.4% and 0.53 g/day, respectively. With regard to biodiesel composition, BSFL-derived biodiesel contained mainly C12:0, C14:0, C16:0 and Sustainability 2020, 12, 1558 2 of 10 C18:1. The higher amount of saturated fatty acids could strengthen the oxidative stability biodiesel produced as compared with non-edible oils or microalgal lipid. At last, the addition of yeast was also found to improve the waste reduction index of coconut endosperm waste (CEW) from 0.31 to 0.40 g/day, heralding the capability of BSFL to valorize organic waste via bioconversion into its biomass to serve as a feedstock for biodiesel production.

There is considerable interest in the exploring of an alternative protein source due to ever-growing population in the world. Black soldier fly (BSF), Hermetia illucens, can be a promising alternative protein-rich food due to its high protein content as compared to livestock. This study investigated the effect of different feeding strategies on the crude protein of BSF prepupae (BSFP) to further enhance the protein contents. The feeding strategy was done at BSFP stage using two different diets which were a mixture of food waste as a control, and bacterial dried cells. Protein and fatty acid content analyses were done on the freeze-dried BSFP samples harvested on day 4 after feeding in order to determine the crude protein and fatty acid. BSFP fed with lyophilized cells showed enhancement in the nutritional contents, compared to the conventional feeding strategy using food waste, with increased crude protein content by 17%. This study demonstrated that the bacterial dried cells can be utilized as a single cell protein to further increase the protein content in the BSFP body which can be applied for the animal feed and potential human consumption.

Background Proteomic analyses have broadened the horizons of vector control measures by identifying proteins associated with different biological and physiological processes and give further insight into the mosquitoes’ biology, mechanism of insecticide resistance and pathogens-mosquitoes interaction. Female Ae. aegypti ingests human blood to acquire the requisite nutrients to make eggs. During blood ingestion, female mosquitoes transmit different pathogens. Therefore, this study aimed to determine the best protein extraction method for mass spectrometry analysis which will allow a better proteome profiling for female mosquitoes. Methods In this present study, two protein extractions methods were performed to analyze female Ae. aegyti proteome, via TCA acetone precipitation extraction method and a commercial protein extraction reagent CytoBusterTM. Then, protein identification was performed by LC-ESI-MS/MS and followed by functional protein annotation analysis. Results The CytoBusterTM reagent gave the highest protein yield with a mean of 475.90 µg compared to TCA acetone precipitation extraction showed 283.15 µg mean of protein. LC-ESI-MS/MS identified 1,290 and 890 proteins from the CytoBusterTM reagent and TCA acetone precipitation, respectively. When comparing the protein class categories in both methods, there were three additional categories for proteins identified using CytoBusterTM reagent. The proteins were related to scaffold/adaptor protein (PC00226), protein binding activity modulator (PC00095) and intercellular signal molecule (PC00207). In conclusion, the CytoBusterTM protein extraction reagent showed a better performance for the extraction of proteins in term of the protein yield, proteome coverage and extraction speed.

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