Naringinase, an enzyme complex, is commercially attractive due to its potential usefulness in pharmaceutical and food industries. It is of particular interest in the biotransformation of steroids, antibiotics, and mainly of glycosides hydrolysis. Moreover, it can be used in citrus juices debittering and wine industries. Naringinase expresses activity on alpha-l-rhamnosidase and beta-d-glucosidase. Many natural glycosides, including naringin, rutin, quercitrin, hesperidin, diosgene, and ter-phenyl glycosides, containing terminal alpha-rhamnose and beta-glucose can act as substrates of naringinase. The sources, production, activity, biochemical properties, and substrate specificity of naringinase are reviewed, along with a description of the enzymatic deglycosylation systems and applications, concluding with the identification of areas which need further extensive studies.