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Updated: Jan 21, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Lipases: sources, immobilization methods, and industrial applications
Danielle Gonçalves Filho1, Amanda Gonçalves Silva1, Carla Zanella Guidini2
1Campus de Patos de Minas, Faculdade de Engenharia Química, Universidade Federal de Uberlândia, Av. Getúlio Vargas, 230, Centro, Patos de Minas, MG, 38700-126, Brazil.
Abstract:
Enzymes are natural catalysts highly specific to the substrate type and operate under mild conditions of temperature, pressure, and pH with high conversion rates, which makes them more efficient than conventional chemical catalysts. The enzymes can be obtained from various sources, animal, vegetable, and microbiological. Lipases are very versatile enzymes, and this has aroused the interest of the industries. However, the great problem of the use of soluble lipases is the high cost of acquisition, low operational stability, and difficulties of recovery, and reuse. Enzymatic immobilization has been suggested as an alternative to reduce the limitations of soluble enzymes, increasing their stability and facilitating recovery, and reuse, significantly reducing the cost of processes involving the use of enzymes. This review presents a discussion on the different immobilization methods for lipase, as well as the challenges of use lipases immobilized on the industrial scale.
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