ABSTRACT
One of the major challenges in sustainable waste management in the agri-food industry following the "zero waste" model is the application of the circular economy strategy, including the development of innovative waste utilization techniques. The conversion of agri-food waste into carriers for the immobilization of enzymes is one such technique. Replacing chemical catalysts with immobilized enzymes (i.e., immobilized/heterogeneous biocatalysts) could help reduce the energy efficiency and environmental sustainability problems of existing chemically catalysed processes. On the other hand, the economics of the process strongly depend on the price of the immobilized enzyme. The conversion of agricultural and food wastes into low-cost enzyme carriers could lead to the development of immobilized enzymes with desirable operating characteristics and subsequently lower the price of immobilized enzymes for use in biocatalytic production. In this context, this review provides insight into the possibilities of reusing food industry wastes, namely, eggshells, coffee grounds, and brown onion skins, as carriers for lipase immobilization.
ABSTRACT
Despite the already established route of chemically catalyzed transesterification reaction in biodiesel production, due to some of its shortcomings, biocatalysts such as lipases present a vital alternative. Namely, it was noticed that one of the key shortcomings for the optimization of the enzyme catalyzed biodiesel synthesis process is the information on the lipase activity in the reaction mixture. In addition to making optimization difficult, it also makes it impossible to compare the results of the independent research. This article shows how lipase intended for use in biodiesel synthesis can be easily and accurately characterized and what is the enzyme concentration that enables achievement of the desired level of fatty acid methyl esters (FAME) in the final product mixture. Therefore, this study investigated the effect of two different activity loads of Burkholderia cepacia lipase on the biodiesel synthesis varying the pH and temperature optimal for lipase activity. The optimal lipase pH and temperature were determined by two different enzyme assays: spectrophotometric and titrimetric. The B. cepacia lipase pH optimum differentiated between assays, while the lipase optimally hydrolyzed substrates at 50°C. The analysis of FAME during 24 hr of biodiesel synthesis, at two different enzyme concentrations, pH 7, 8, and 10, and using two different buffers, revealed that the transesterification reaction at optimal pH, 1 hr reaction time and lipase activity load of 250 U per gram of reaction mixture was sufficient to produce more than 99% FAME.
