Biocatalysts are preferred by industries over chemical catalysts. In the lipid modification business, lipases (triacylglycerol acylhydrolase) are considered the best biocatalysts. Animals, plants, and microbes all have large amounts of lipases. Bacterial lipases account for 45% of the total, followed by fungus (21%), animal (18%), plant (11%), and algae (3%). Because they are readily available and can catalyze processes such as hydrolysis, esterification, and alcoholysis, microbial lipases are the preferred option among them. Microbial lipases are now more effective when immobilized, making them useful for a variety of reactions and reducing the need to add fragrance to the immobilization procedures. Additionally, particular attention has been paid to elements like modeling, design, and process optimization that are essential for future industrial implementation and scale-up. Enzymologists have always been captivated by the distinct interfacial activation of lipases, and in the past few years, biophysicists and crystallographers have made strides toward grasping the structure–function links of these enzymes. Because of their accessibility, ability to work in a range of media, stability in organic solvents, ability to catalyze at the lipid–water interface and even in non-aqueous conditions, and ability to function in a variety of media, they are a versatile option for the food, flavor, detergent, pharmaceutical, leather, textile, cosmetic, and paper industries.