A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles†

Abstract

A review of the literature covering research on the immobilization of lipases on hydrophobic supports was performed using systematic mapping (SM) concepts. This approach consists of a rigorous review of the methodology used to catalog evidence, to identify gaps at the frontier of knowledge, to identify unknown trends, and to list research groups. Our results show a wide variety of available lipases, including commercial, wild-type and recombinant strains. However, the most commonly used lipases are lipases from Thermomyces lanuginosus (TLL), Candida rugosa (CRL) or Rhizomucor miehei (RML) and lipase B from Candida antarctica (CALB). A wide variety of supports with different degrees of hydrophobicity were identified and the supports activated with a layer of octyl or octadecyl groups were the most commonly used. The advantages of lipase immobilization on these supports are discussed. Among them, the immobilization, purification, stabilization and hyperactivation of lipases in a single step stand out. Moreover, problems related to lipase immobilization by interfacial activation are highlighted (mainly enzyme release). Strategies to overcome these problems include immobilization on heterofunctional supports or intermolecular crosslinking of enzymes immobilized by physical and/or chemical agents. The possibility of increasing the capacity of supports by lipase multilayer immobilization is also discussed. Finally, the structure, distribution of the network and the frequency of co-occurrence between lipases and supports are elucidated to determine the possible hotspots and hitherto unexplored advances in knowledge.