Engineering Lipase Enzyme Nano-powder Using Nano Spray Dryer BÜCHI B-90: Experimental and Factorial Design Approach for a Stable Biocatalyst Production

Abstract

The industrial applications of lipases are hampered by their sensitive nature to processing and storage conditions. In this context, this study presents a simple statistical modeling approach using Nano Spray Dryer BUCHI B-90 as an ideal technique for the production of stable lipase nano-powder (LNP). In this study, factorial design is employed to optimize the spray drying process for Mucor racemosus lipase enzyme. Different variables were investigated such as adjuvant type (dextrin, mannitol, and lactose), concentration (2%, 4%, 8%), nozzle diameter, and inlet temperature (80 °C, 100 °C, 120 °C). Additionally, the physicochemical properties of LNP including particle size, residual enzyme activity, powder yield, morphology, and moisture content are investigated. Results indicate a significant effect of additive type on product yield value and particle size. LNP exhibited a broad range of physical characteristics (enzyme residual activity 80.5–100%, particle size 210–1313 nm, and yield value 24–99%) and 98.4% residual activity after storage for 2 months at 5 °C. Scanning electron microscopy (SEM) images have shown a variation in the morphology of LNP with a remarkable flower-like structure in presence of lactose. The measured pronounced lipase stability is accredited to high local lipase concentration, adjuvant stabilizing effect, and favorable lipase conformation at the nano-scale-solid state. Based on the results presented, a robust approach for the production of a maximally viable spray-dried LNP in solid form can be employed for extended biotherapeutic and biotechnological applications of lipase.