Modifying bio-catalytic properties of enzymes for efficient biocatalysis: a review from immobilization strategies viewpoint

Bilal, Muhammad; Zhao, Yuping; Noreen, Sadia; Shah, Syed Zakir Hussain; Bharagava, Ram Naresh; Iqbal, Hafiz M.N.

doi:10.1080/10242422.2018.1564744

Cited by 134 publications

(69 citation statements)

References 164 publications

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“…However, soon, the technique showed a great potential to improve many enzyme properties, such as stability, selectivity, specificity, purity, etc. [2][3][4][5][6][7][8][9][10][11]. The selection of the support is in many instances decisive for the final implementation of the biocatalysts [12].…”

Section: Introductionmentioning

confidence: 99%

Increasing the Enzyme Loading Capacity of Porous Supports by a Layer-by-Layer Immobilization Strategy Using PEI as Glue

et al. 2019

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A new strategy to increase the enzyme-loading capacity of porous supports was investigated. Lipase from Pseudomonas fluorescens (PFL) was immobilized on octyl-agarose (OA) beads and treated with polyethyleneimine (PEI). Then, PFL was immobilized on the previous PFL layer. Next, the biocatalyst was coated with PEI and a third layer of PFL was added. Sodium dodecyl sulfate polyacrylamide electrophoresis showed that the amount of PFL proportionally increased with each enzyme layer; however, the effects on biocatalyst activity were not as clear. Hydrolyzing 50 mM of triacetin at 25 °C, the activity of the three-layer biocatalyst was even lower than that of the bi-layer one; on the contrary its activity was higher when the activity was measured at 4 °C in the presence of 30% acetonitrile (that reduced the activity and thus the relevance of the substrate diffusion limitations). That is, the advantage of the multilayer formation depends on the specific activity of the enzyme and on the diffusion limitations of the substrate. When octyl agarose (OA)-PFL-PEI-PFL preparation was treated with glutaraldehyde, the activity was reduced, although the enzyme stability increased and the immobilization of the last PFL layer offered results similar to the one obtained using the three-layer preparation without glutaraldehyde modification (90%).

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Section: Introductionmentioning

confidence: 99%

Increasing the Enzyme Loading Capacity of Porous Supports by a Layer-by-Layer Immobilization Strategy Using PEI as Glue

et al. 2019

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“…After modification with 2-Melm, 2-Melm@PLA 1 /MSNC had the two above-mentioned benefits: interfacial catalysis and facilitated acyl group migration. Microenvironmental modification aimed at enhancing the catalytic reaction of enzymes in specific reaction media is an important method to improve the activity of immobilized enzymes [30][31][32][33]. The modification of 2-Melm maintained the alkaline microenvironment of 2-Melm@PLA 1 /MSNC in the nanostructure, which was more suitable for the catalytic conditions of PLA 1 .…”

Section: Characterization Of 2-melm@pla1/msncmentioning

confidence: 99%

“…The microenvironment in nanostructures plays an important role in enzymatic activity [27][28][29]. The microenvironmental modification of nanocarriers can enhance the enzymatic catalytic activity and catalytic performance characteristics, which has received more and more attention [30][31][32][33]. ε-Poly-L-lysine (EPL)-modified mesoporous titanium dioxide (M-TiO 2 ) with negative charges for immobilized enzymes displayed strong storage stability, thermal stability, and good reusability [28].…”

Section: Introductionmentioning

confidence: 99%

Alkaline Modification of a Metal–Enzyme–Surfactant Nanocomposite to Enhance the Production of L-α-glycerylphosphorylcholine

Cao

et al. 2019

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Microenvironment modification within nanoconfinement can maximize the catalytic activity of enzymes. Phospholipase A1 (PLA1) has been used as the biocatalyst to produce high value L-α-glycerylphosphorylcholine (L-α-GPC) through hydrolysis of phosphatidylcholine (PC). We successfully developed a simple co-precipitation method to encapsulate PLA1 in a metal–surfactant nanocomposite (MSNC), then modified it using alkalescent 2-Methylimidazole (2-Melm) to promote catalytic efficiency in biphasic systems. The generated 2-Melm@PLA1/MSNC showed higher catalytic activity than PLA1/MSNC and free PLA1. Scanning electron microscopy and transmission electron microscopy showed a typical spherical structure of 2-Melm@PLA1/MSNC at about 50 nm, which was smaller than that of 2-Melm@MSNC. Energy disperse spectroscopy, N2 adsorption isotherms, Fourier transform infrared spectrum, and high-resolution X-ray photoelectron spectroscopy proved that 2-Melm successfully modified PLA1/MSNC. The generated 2-Melm@PLA1/MSNC showed a high catalytic rate per unit enzyme mass of 1.58 μmol mg-1 min-1 for the formation of L-α-GPC. The 2-Melm@PLA1/MSNC also showed high thermal stability, pH stability, and reusability in a water–hexane biphasic system. The integration of alkaline and amphiphilic properties of a nanocomposite encapsulating PLA1 resulted in highly efficient sequenced reactions of acyl migration and enzymatic hydrolysis at the interface of a biphasic system, which cannot be achieved by free enzyme.

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“…Immobilization of enzymes on different supports is a useful tool to increase their stability, activity, and selectivity under operational conditions [42][43][44]. Due to a simpler separation of the biocatalyst from the reaction environment, such preparations may be reused in many catalytic cycles without losing their catalytic properties, which increases the economic efficiency of the industrial process [45].…”

Section: Introductionmentioning

confidence: 99%

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters

et al. 2020

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The influence of buffer type, co-solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4-arylbut-3-en-2-yl esters using Lecitase™ Ultra (LU). Immobilized preparations of the Lecitase™ Ultra enzyme had significantly higher activity and enantioselectivity than the free enzyme, particularly for 4-phenylbut-3-en-2-yl butyrate as the substrate. Moreover, the kinetic resolution with the immobilized enzyme was achieved in a much shorter time (24–48 h). Lecitase™ Ultra, immobilized on cyanogen bromide-activated agarose, was particularly effective, producing, after 24 h of reaction time in phosphate buffer (pH 7.2) with acetone as co-solvent, both (R)-alcohols and unreacted (S)-esters with good to excellent enantiomeric excesses (ee 90–99%). These conditions and enzyme were also suitable for the kinetic separation of racemic (E)-4-phenylbut-3-en-2-yl butyrate analogs containing methyl substituents on the benzene ring (4b,4c), but they did not show any enantioselectivity toward (E)-4-(4’-methoxyphenyl)but-3-en-2-yl butyrate (4d).

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Modifying bio-catalytic properties of enzymes for efficient biocatalysis: a review from immobilization strategies viewpoint

Cited by 134 publications

References 164 publications

Increasing the Enzyme Loading Capacity of Porous Supports by a Layer-by-Layer Immobilization Strategy Using PEI as Glue

Increasing the Enzyme Loading Capacity of Porous Supports by a Layer-by-Layer Immobilization Strategy Using PEI as Glue

Alkaline Modification of a Metal–Enzyme–Surfactant Nanocomposite to Enhance the Production of L-α-glycerylphosphorylcholine

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters

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