Lipases form a group of versatile enzymes, which could be used in various biotechnological applications. In order to establish an economic process, immobilization of the enzyme could be a useful tool. The aim of the work was to develop different immobilization strategies, which could be used for site-directed and stable coupling of the enzyme without affecting the enzymatic activity. Lipase LipT1 from Geobacillus sp. T1 was applied as model enzyme in the study. In separate approaches, several variants of the lipase were designed containing either amino acid substitutions on the protein surface or fusions with peptide tags. Coupling to solid supports was carried out either chemically using side chains of lysine, cysteine or histidine residues or enzymatically via glutamine residues by applying microbial transglutaminase. Besides investigations on the immobilization behavior of the variants, the stability and reusability of the immobilized enzyme in a hydrolysis reaction was tested.