Specific Strategies for One-Step and Simultaneous Immobilization-Purification of Lipases

Abstract

Lipases are the biocatalysts with outstanding prospects in industry and medicine. They have proven to be useful in various hydrolytic and synthetic reactions. However, there are some limitations for impure lipases that may restrict their widely uses in industrial applications. Purification is sometimes vital for the characterization of the function, structure, and interactions of lipases. The lipase immobilization is also an efficient strategy for increasing the enzyme activity and stability, and getting a simpler recovery. Lipases are naturally produced together with many other proteins that they may occupy some surface of immobilization solid support and decrease the final activity. The coupling of immobilization and purification of lipase will overcome the mentioned problems and obtain the maximum purification yields. The present mini-review will discuss the use of the techniques that permit to join immobilization and purification of lipases in a single step, including control of the immobilization conditions by interfacial activation on hydrophobic supports, the development of specific supports with affinity for lipases, and the use of bio-affinity supports including immuno- and lectin affinity HIGHLIGHTS •Lipases are the biocatalysts with outstanding prospects in industry and medicine. •Simultaneous immobilization-purification may enhance lipase activity and stability. •Lipases have a mechanism of interfacial activation in the presence of hydrophobic interfaces. •The lipase immobilization on hydrophobic supports is a much-utilized strategy. •Bio-affinity is a promising approach to increase lipase final yield and activity.