Obtaining a biodegradable biocatalyst – study on lipase immobilization on spent coffee grounds as potential carriers.

Coffee waste can be reused as matrices for enzyme immobilization, as it contains various organic compounds able to adsorb catalytic proteins. In this study, spent coffee grounds were used as a support in the immobilization process in their native form and after being pretreated with hexane, ethanol, and sulphuric acid solution, respectively. Microbial lipases from Aspergillus oryzae , Thermomyces lanuginosus , and Rhizomucor miehei were adsorbed on the carrier, and as a reference, the abovementioned lipases were also immobilized on a synthetic matrix - Lewatit VP OC 1600. The research investigated the impact of the purification step on the immobilization process and the full characteristics of the obtained biocatalysts. The hydrolytic and synthetic activities of the immobilized enzyme preparations were tested, as well as substrate specificity, recovery, and temperature and pH activity profiles. SEM and FTIR analyses were also performed. The results showed that the chemical composition of coffee waste influenced the activity of the obtained biocatalysts, and the lack of hemicellulose caused a reduction in lipolytic activity. The study reveals that spent coffee grounds can be a potential support for enzyme immobilization, and lipases adsorbed on them have improved properties such as hydrolytic or synthetic activity, and stability in pH. • Spent coffee grounds can be a potential support for lipase immobilization. • The presence of hemicellulose in SCG is crucial for enzyme adsorption onto a carrier. • Immobilization of fungal lipases on SCG resulted in higher catalytic efficiency. [ABSTRACT FROM AUTHOR]