Ionic liquids (ILs) have now been acknowledged as reaction media for biotransformations. The first three examples were reported in this field in 2000, and since then, numerous applications have been reported for biocatalytic reactions using ILs. Two topics using ILs for enzymatic reactions have been reviewed from the standpoint of biocatalyst mediating organic synthesis; the first is “Biocatalysis in Ionic Liquids” which includes various types of biocatalytic reactions in ILs (section 2): (1) recent examples of lipase-mediated reactions using ILs as reaction media for biodiesel oil production and for sugar ester production, (2) oxidase-catalyzed reactions in ILs, (3) laccase-catalyzed reactions, (4) peroxidase-catalyzed reactions, (4) cytochrome-mediated reactions, (5) microbe-mediated hydrations, (6) protease-catalyzed reactions, (8) whole cell mediated asymmetric reduction of ketones, (10) acylase-catalyzed reactions, (11) glycosylation or cellulase-mediated hydrolysis of polysaccharides, (12) hydroxyni...

Ionic Liquids as Tool to Improve Enzymatic Organic Synthesis.

Compared with free enzymes, immobilized enzymes are more robust and resistant to environmental changes. In addition, with enhanced stability, immobilized enzymes can be separated from the reaction mixture and used for repeated cycles. These advantages prompt their applications in various fields. This review outlines the existing methods and easy separated support materials for enzymes immobilization. After a brief introduction on the immobilized enzyme, the immobilization methods of adsorption, entrapment, covalent attachment and cross-linking are discussed. The emphasis is given on the easy separated support materials of magnetic nanoparticles (MNPs), membranes and capillary columns. An outlook on the immobilized enzyme is given at last.

Advances on methods and easy separated support materials for enzymes immobilization

Recent progress in multienzymes co-immobilization and multienzyme system applications

Production and use of immobilized lipases in/on nanomaterials: A review from the waste to biodiesel production

Recent advances in hybrid organic-inorganic materials with spatial architecture for state-of-the-art applications

Increasing numbers of materials have been extensively used as platforms for enzyme immobilization to improve catalytic performance. However, activity of the most of the enzymes was declined after immobilization. Here, we develop a surfactant-activated lipase-inorganic flowerlike hybrid nanomaterials with rational design based on interfacial activation and self-assembly. The resulting surfactant-activated lipase-inorganic hybird nanoflower (activated hNF-lipase) exhibited 460% and 200% higher activity than native lipase and conventional lipase-inorganic hybird nanoflower (hNF-lipase). Furthermore, the activated hNF-lipase displayed good reusability due to its monodispersity and mechanical properties, and had excellent long-time stability. The superior catalytic performances were attributed to both the conformational modulation of surfactants and hierarchical structure of nanoflowers, which not only anchored lipases in an active form, but also decreased the enzyme-support negative interaction and mass-transfer limitations. This new biocatalytic system is promising to find widespread use in applications related to biomedicine, biosensor, and biodiesel.

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Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance.

BACKGROUND

Encapsulation of enzymes in biomimetic silica seems to be a promising immobilization method due to mild processing conditions and short preparation time. However, biomimetic silica particles may be considered too small for industrial applications because they result in difficult recovery. Furthermore, the use of R5 peptide or polymers as catalyst usually causes protein denaturation. To overcome these drawbacks, a new stable and recyclable biocatalyst based on co-encapsulation of magnetic nanoparticles and phenylalanine ammonia lyase (PAL) in biomimetic silica has been prepared using enzyme-assisted direct condensation reactions of silicon oxide with tetramethoxysilane (TMOS).



RESULTS

Under optimal conditions (10 mg mL−1 nanoparticles, 4.5 U mL−1 PAL, 0.8 mol L−1 TMOS), the highest activity recovery (52%) of encapsulated PAL was obtained. Compared with conventional PAL encapsulated in biomimetic silica (28%), the activity recovery was increased 1.86-fold. TEM, CLSM, magnetisation measurements, and FTIR confirmed that the magnetic nanopaticles and PAL had been co-encapsulated into the biomimetic silica. The resulting immobilized PAL exhibited higher activity and stability than native PAL, and the immobilized PAL can be easily separated by applying a magnetic field.



CONCLUSIONS

This work provides a convenient strategy to prepare stable and easy recycled biocatalyst with excellent catalytic performance. © 2015 Society of Chemical Industry

Ronglin Liu

Papers

Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance.

Magnetic mesoporous enzyme–silica composites with high activity and enhanced stability