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Forty each of aspergilli and penicillia were screened for extracellular lipase production on agar plates and in liquid medium containing olive oil as substrate. Twenty-nine aspergilli and twenty-six penicillia produced lipase. Out of these, 19 aspergilli and 22 penicillia showed activity both on Nile blue sulfate and glycerol tributyrate agar plates while only 10 aspergilli and 4 penicillia showed a positive response to glycerol tributyrate agar alone. The screening revealed 11 Aspergillus spp. and 15 Penicillium spp. as new lipase producers. Pig fat as an economic substrate for lipase production was also investigated.

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The potential of ornamental plant Syngonium podophyllum leaf extract has been explored for the synthesis of silver nanoparticles, which was confirmed by appearance of absorption peak at 420 nm in ultraviolet-visible (UV-Vis) spectrum. Silver nanoparticles were predominantly spherical in shape and size observed under scanning electron microscopy (SEM) was in the range of 11 to 26 nm. A sharp signal recorded at 3 keV under energy-dispersive X-ray (EDX) spectrum indicated the presence of elemental silver nanoparticles. Zeta potential was measured as-26.77 mV, which indicated the presence of moderately stable silver nanoparticles in the solution. Under Fourier transform infrared (FTIR), two prominent bands were assigned, i.e., 3,454.89 cm −1 represents the O-H stretching vibration and 1,637.46 cm −1 represents the-NH stretching vibration of the amide group. It indicates that protein might be responsible for the synthesis.

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A study of the pancreatic lipase inhibitory activity of a protein from the seed of Litchi chinensis was carried out. Protein was isolated by 70 % ammonium sulphate precipitation followed by dialysis. Lipase inhibitory activity of the protein was evaluated using both synthetic (p-nitrophenyl palmitate) and natural (olive oil) substrates. Protein at the final concentration of 100 µg/mL was able to inhibit 68.2 % pancreatic lipase on synthetic substrate and 60.0 % on natural substrate. Proteinaceous nature of the inhibitor was determined using trypsinization assay. Pancreatic lipase inhibitory protein was sensitive to 0.05 % trypsin treatment with the loss of 61.9 % activity. IC50 of this proteinaceous pancreatic lipase inhibitor was 73.1 µg/mL using synthetic substrate. This inhibitory protein was sensitive to pH, with the highest inhibitory activity at pH=8.0 and the lowest at pH=3.0. Protein was further analyzed using 10 % non-reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and, interestingly, it showed the presence of a single band of (61±2) kDa when stained with Coomassie brilliant blue. The isolated protein was finally crystallized to see its homogeneity by batch crystallization method. Crystals were well formed with distinct edges. The isolated protein showed good pancreatic lipase inhibitory activity.