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Polypropylene as a selective support for the immobilization of lipolytic enzymes: hyper‐activation, purification and biotechnological applications

2021; Wiley; Volume: 97; Issue: 2 Linguagem: Inglês

10.1002/jctb.6876

1097-4660

María Guadalupe Sánchez-Otero, Rodolfo Quintana‐Castro, Adela‐Sofía Rojas‐Vázquez, Giselle‐Lilian Badillo‐Zeferino, Karina Mondragón‐Vázquez, Graciela Espinosa‐Luna, Ashok Kumar, Rosa María Oliart‐Ros,

biodegradable polymer synthesis and properties

Abstract Lipases are the versatile biological catalysts used in a wide range of commercial synthetic applications. Microbial lipases have been widely used in the pharmaceutical, food, textile, oleochemical, paper, and bioenergy industries, in the composition of detergents, and in the production of polymers and enantiomerically pure chemical intermediates. Lipases have a unique lid opening mechanism that makes them interesting biocatalysts to catalyze reactions in hydrophobic environments. Water insoluble substrates have also been efficiently transformed by lipases in organic solvents. The use of lipases in industrial processes could be limited by the cost of their production, the difficulties in their recovery and disposal, or by the harsh conditions of some processes that could inactivate or denature the protein. The immobilization of enzymes helps overcome these physical and economical drawbacks, making the catalyst more active, stable, and reusable, resulting in the reduction of costs and of contaminating and harmful byproducts. Polypropylene has unique properties that aid in the activation of the lid opening mechanism and improve the catalytic efficiency of immobilized lipases. The aim of this review is to present an overview of the uses of polypropylene as a support for immobilization of lipolytic enzymes, the study of the immobilization procedure conditions, the characteristics of the immobilized enzymes, and the perspectives of their use in the future as a powerful tool in sustainable industry. © 2021 Society of Chemical Industry (SCI).