This review discusses the sources, immobilization techniques on nanomaterials, and applications of lipases. Lipases are important biocatalysts used in various industries, including food, pharmaceuticals, and biofuels. However, their aqueous solubility and instability limit their application. Immobilization techniques are used to enhance lipase activity and stability, and nanomaterials have shown great potential in this regard. The review examines recent advancements in lipase immobilization on nanomaterials and discusses methods for determining lipase activity. It also highlights the potential for multiple applications of immobilized lipases. Lipases are enzymes that catalyze the hydrolysis of triacylglycerol ester linkages, converting them into free fatty acids and glycerol. They are important in biotechnology and have diverse applications in commercial sectors such as biopolymer and biodiesel manufacturing, medicines, agrochemicals, cosmetics, and flavors. Fungal lipases are particularly interesting due to their stability, selectivity, and wide substrate specificity. However, lipases have limitations, including low stability, susceptibility to deactivation, and challenges in isolation for reuse. Therefore, optimizing immobilization techniques is essential to maximize lipase activity and operational stability. The stability of lipases is influenced by factors such as temperature, reaction media, water concentration, and synthesis technique. The folded structure of lipases is stabilized by various bonds, including disulfide bonds, salt bridges, and hydrogen bonds. The review also discusses the sources of lipases, including plant and animal sources. Plant lipases are found in various plant parts, with significant quantities in food storage tissues of developing seedlings. Animal-derived lipases are digestive enzymes secreted by exocrine cells in the digestive system. Lipases can be extracted and purified using various methods, such as aqueous two-phase systems, chromatography, and ultrafiltration. Plant lipases are stable in interesterification reactions, inexpensive to produce, and provide an excellent alternative for the utilization of agricultural waste products.This review discusses the sources, immobilization techniques on nanomaterials, and applications of lipases. Lipases are important biocatalysts used in various industries, including food, pharmaceuticals, and biofuels. However, their aqueous solubility and instability limit their application. Immobilization techniques are used to enhance lipase activity and stability, and nanomaterials have shown great potential in this regard. The review examines recent advancements in lipase immobilization on nanomaterials and discusses methods for determining lipase activity. It also highlights the potential for multiple applications of immobilized lipases. Lipases are enzymes that catalyze the hydrolysis of triacylglycerol ester linkages, converting them into free fatty acids and glycerol. They are important in biotechnology and have diverse applications in commercial sectors such as biopolymer and biodiesel manufacturing, medicines, agrochemicals, cosmetics, and flavors. Fungal lipases are particularly interesting due to their stability, selectivity, and wide substrate specificity. However, lipases have limitations, including low stability, susceptibility to deactivation, and challenges in isolation for reuse. Therefore, optimizing immobilization techniques is essential to maximize lipase activity and operational stability. The stability of lipases is influenced by factors such as temperature, reaction media, water concentration, and synthesis technique. The folded structure of lipases is stabilized by various bonds, including disulfide bonds, salt bridges, and hydrogen bonds. The review also discusses the sources of lipases, including plant and animal sources. Plant lipases are found in various plant parts, with significant quantities in food storage tissues of developing seedlings. Animal-derived lipases are digestive enzymes secreted by exocrine cells in the digestive system. Lipases can be extracted and purified using various methods, such as aqueous two-phase systems, chromatography, and ultrafiltration. Plant lipases are stable in interesterification reactions, inexpensive to produce, and provide an excellent alternative for the utilization of agricultural waste products.