Green synthesis and effective utilization of biogenic Al 2 O 3 -nanocoupled fungal lipase in the resolution of active homochiral 2-octanol and its immobilization via aluminium oxide nanoparticles

The present study highlights the true potential of Rhizopus oligosporus IIB-08 to produce lipase enzyme under solid-state fermentation and focuses on improving the properties of lipase by immobilizing it on biogenic aluminium oxide nanoparticles (Al-NPs) for better resolution of active homochiral 2-octanol. For this purpose, almond meal substrate showed 10.44 ± 0.36 U·g −1 lipase activity. The immobilization of lipase on biogenic Al-NPs prepared using Mentha spicata leaf extract led towards improved stability and catalytic efficiency, resulting in a 9.3% increase in activity compared to free enzyme. This study also examined the potential of the immobilized lipase in the effective resolution of 2-octanol. Gas chromatography-mass spectrometry confirmed the presence of lipase-catalysed fatty acids, such as linolenic acid (C18:3), linoleic acid (C18:2), palmitic acid, and oleic acid (C18:1), with palmitic acid exhibiting the highest concentration (142 μg·ml −1 ) at a retention time of 23.2 min. This study concludes that R. oligosporus IIB-08 is a promising source for lipase production and demonstrates the significant potential of nanoparticle-immobilized lipase in resolving pharmaceutically important organic chemicals, thereby making it a promising approach for different industrial applications. However, further scaling up is needed for better implementation in the industry.