The larvae of black soldier fly (BSFL) are rich in lipids, and in the current study, BSFL was used to produce biodiesel by enzymatic transesterification with methanol. Biodiesel obtained by free lipase-catalyzed transesterification is always with side-reactions. To address the limitation of free lipase, for the first time, Lipase SMG1 and Lipase Eversa Transform 2.0 were combined to use as catalysts at the same time. The effects of different reaction conditions on the yield of biodiesel were investigated, including the type of enzyme, reaction temperature, and molar ratio of BSFL to methanol. The molar ratio of BSFL to methanol 1:3, one-step addition of methanol at 25 °C were selected as optimal conditions. The fatty acid methyl ester content achieved to 98.45% after 8h reaction under the optimal conditions. Moreover, the main properties of the final biodiesel indicators met the EN14214 biodiesel standard.

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In this paper the ability of immobilized lipase MAS1-H108A to prepare α-linolenic acid-rich partial glycerides was studied. The effects of different reaction conditions on the yield of Diacylglycerol (DAG) and Monoglyceride (MAG) were investigated, including substrate molar ratio, substrate concentration, temperature and lipase dosage. The highest yield (63.92% of MAG and 30.61% of DAG) was obtained when silkworm pupa oil/glycerol ratio of 1:3, lipase dosage was 50 U/g, substrate concentration was 40% (w/v), at 40 °C. Under the optimal conditions, the scale-up (50 times) and single-stage molecular distillation were carried out to separate DAG and MAG, the yield of MAG in the light phase was 99.18%, and the concentration of DAG in the heavy phase was 89.47%, α-linolenic acid in MAG and DAG accounted for 28.96% and 28.23%, respectively. The results can be shown that the immobilized lipase MAS1-H108A has excellent potential for enzymatic glycerolysis to prepare functional partial glycerides.

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