A review on the important aspects of lipase immobilization on nanomaterials

Abstract

Lipase is one of the most widely used enzymes and plays an important role in biotechnological and industrial processes including food, paper, and oleochemical industries, as well as in pharmaceutical applications. However, its aqueous solubility and instability make its application relatively difficult and expensive. The immobilization technique is often used to improve lipase performance, and the strategy has turned out to be a promising method. Immobilized lipase on nanomaterials (NMs) has shown superiority to the free lipase, such as improved thermal and pH stability, longer stable time, and the capacity of being reused. However, immobilization of lipase on NMs also sometimes causes activity loss and protein loading is relatively lowered under some conditions. The overall performance of immobilized lipase on NMs is influenced by mechanisms of immobilization, type of NMs being used, and physicochemical features of the used NMs (such as particle size, aggregation behavior, NM dimension, and type of coupling/modifying agents being used). Based on the specific features of lipase and NMs, this review discusses the recent developments, some mechanisms, and influence of NMs on lipase immobilization and their activity. Multiple application potential of the immobilized lipases has also been considered.

Synthesis, physicochemical properties, and health aspects of structured lipids: A review

“…Compared to free lipases, their immobilized counterparts can be obtained through physical adsorption, physical entrapment, covalent bonding, and chemical crosslinking, with improved stability against heat and pH, easy recovery and reusability, and suitability for continuous processes (Facin, Melchiors, ValéRio, Oliveira, & Oliveira, 2019;Mateo, Palomo, Fernandez-Lorente, Guisan, & Fernandez-Lafuente, 2007). For physical immobilization, lipases can be immobilized onto the supports through weak interactions including van der Waals forces, hydrogen bonds, and hydrophobic interactions, or can be confined inside the support matrix, whereas chemical immobilization generally involves the formation of covalent bonds between the amino groups of lipases and the functional groups of the carriers (Facin et al, 2019;Shuai, Das, Naghdi, Brar, & Verma, 2017).…”

Design of an Immobilized Biohybrid Catalyst by Adsorption Interactions onto Magnetic Srebrodolskite Nanoparticles

“…In the last years, magnetic metal oxide nanoparticles have had considerable progress as inorganic carriers for enzyme immobilization since a selective magnetic separation from the reaction mixture makes them useful for a smart immobilization . In this line, nanoparticles of metal ferrite have been continually evaluated in recent years for its use in biocatalysis …”

Preparation and anti‐tumor efficiency evaluation of bacterial magnetosome–anti‐4‐1BB antibody complex: Bacterial magnetosome as antibody carriers isolated from Magnetospirillum gryphiswaldense

“…The bilayer membrane component of BMs contains many amino groups, which can be combined with biological molecules that include enzymes, antibodies, and antitumor medicines . Many in vitro results have demonstrated that BMs have many advantages over artificial iron oxide nanoparticles, particularly when the nanoparticles are used for biological applications .…”