Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Abstract

For over a century, enzyme immobilisation has been proven to be a superior strategy to improve catalytic activity and reusability and ensure easy separation, easy operation, and reduced cost. Enzyme immobilisation allows for an easier separation of the enzyme from the reaction mixture, thus simplifying downstream processing. This technology protects the enzyme from degradation or inactivation by harsh reaction conditions, making it more robust and suitable to be used in various applications. Recent strategies of immobilisation methods, such as adsorption, cross-linking, entrapment or encapsulation, and covalent bonding, were critically reviewed. These strategies have shown promising results in improving enzyme stability, activity, and reusability in various applications. A recent development in enzyme immobilisation in nanomaterials and agrowaste renewable carriers is underlined in the current review. Furthermore, the use of nanomaterials and agrowaste carriers in enzyme immobilisation has gained significant attention due to their unique properties, such as high surface area, high mass transfer, biocompatibility, and sustainability. These materials offer promising outcomes for developing more efficient and sustainable immobilised enzymes. This state-of-the-art strategy allows for better control over enzyme reactions and enhances their reusability, leading to more cost-effective and environmentally friendly processes. The use of renewable materials also helps to reduce waste generation and promote the utilisation of renewable resources, further contributing to the development of a circular economy.

The function of microbial enzymes in breaking down soil contaminated with pesticides: a review

“… No Hexachlorocyclohexane (HCH) [ 1 , 26 ] Esd (serine hydrolase) Myobacterium sp. Flavin and NADH Endosulfan [ 1 , 12 , 43 ] Ese (monooxygenase) Arthrobacter sp. Flavin (FMN) Endosulfan; Endosulfan sulphate [ 1 , 12 , 43 ] CotA (laccase) Bacillus subtilis No Endosulfan [ 43 ] Organophosphate (OP) pesticides OpdA (organophosphate hydrolase) Agrobacterium radiobacter; Pseudomonas diminuta; Flavobacterium Fe 2+ and Zn 2+ Phosphotriester insecticides [ 1 ] PTE (phosphotriesterase) Pseudomonas diminuta ; Sulfolobus solfataricus; Deinococcus radiodurans Zn 2+ Paraoxon [ 15 , 17 ] SsoPox (phosphotriesterase-like lactonases) Sulfolobus solfataricus Zn 2+ Paraoxon [ 15 ] OPAA (prolidases) Alteromonas sp.…”

“…The degradation process via Lin pathway was extensively studied [ 10 , 42 , 43 ]. Figure 8 demonstrates the degradation pathway.…”

“…In the case of lindane, the degradation initiated by two LinA from UT26 that catalyzed dehydrochlorinations, producing 1,4-TCDN (1,3,4,6-tetrachloro-1,4-cyclohexadiene) via gamma-PCCH (pentachlorocyclohexene) which is the metabolic intermediates. Then, two LinB catalyzed hydrolytic dechlorination, producing 2,5-DDOL (2,5-dichloro-2,5-cyclohexadiene-1,4-diol) via 2,4,5-DNOL (2,4,5-trichloro2,5-cyclohexadiene-1-ol) [ 10 , 42 , 43 ].

Fig.

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“…For delta-HCH, two types of dichlorination mechanisms observed. One is the dehydrochlorination of delta-HCH to delta-PCCH by LinA from UT26, while another one is the hydrolytic dichlorination of delta-HCH to tetrachlorocyclohexanediol via PCHL by LinB from B90A [ 10 , 42 , 43 ].…”

“…The biodegradability of endosulfan and its metabolites by enzymes from the family of two-component flavin diffusible monooxygenase (TC-FDM) has been studied in the literature [ 43 , 46 , 48 ]. Ese and Esd are the two members of the TC-FDM family which derived from endosulfan-exposed soil bacteria, capable of degrading the endosulfan and endosulfan sulfate [ 46 ].…”