This review intends to present some of the latest studies on the lipase A from Candida antarctica (CALA). This lipase is among the most stable ones and has some capability to attack the sn-2 position of triglycerides. This makes it a very interesting lipase, especially considering that it is commercially available. The cloning and production of the enzyme together with some structural facts and applications will be discussed in this review. Special focus will be put on the immobilization of the enzyme. The use of the commercially available crosslinked enzyme aggregates of this enzyme will be explained, together with the use of the enzyme in some new trends in enzyme immobilization, such as bio-imprinting of the open form of CALA by detergents and the fixation of the open structure, the design of heterofunctional supports able to take full advantage of the immobilization via interfacial activation but preventing enzyme release, or the design of strategies for the preparation of multiple layers of lipase enzymes (using just CALA or combining CALA with other lipases).