Enzymes are the biocatalysts which accelerate the biochemical reactions by lowering their activation energy and have exceptional specificity and efficiency, which makes them desirable for a wide array of industrial processes. However, challenges such as enzyme instability, limited reusability, and recovery inefficiencies have emphasized on the use of enzyme immobilization technologies. Immobilization involves restricting enzymes to inert, solid support materials, which enhances their stability, reusability, and tolerance to fluctuations in environmental conditions. This technique significantly reduces production costs and facilitates continuous processing. A variety of organic, inorganic, and nanomaterial carriers including alginate, chitosan, silica, and hybrid nanomaterials have been used to optimize enzyme performance. In pharmaceutical industries, enzyme immobilization plays a crucial role in the efficient synthesis of active pharmaceutical ingredients, therapeutic proteins, and optically pure compounds. Immobilized enzymes support high specificity and operational stability in key pharmaceutical reactions, including esterification, deracemization, and biotransformation. Techniques such as adsorption, covalent binding, cross-linking, and entrapment extend enzyme activity and process efficiency. Additionally, immobilized enzymes have therapeutic applications in treating metabolic, genetic, and infectious diseases. Commercial examples, such as Novozym 435, accentuate the industrial relevance of immobilized biocatalysts. This book chapter highlights on different methods of enzyme immobilization and the role of enzyme immobilization in progressing pharmaceutical biotechnology towards cost-effective, scalable, and environmentally sustainable biomedicine development.