Efficient immobilization of phospholipase D on novel polymer supports with hierarchical pore structures

Li, Yan; Wu, Jiaqin; Long, Nengbing; Zhang, Ruifeng

doi:10.1016/j.ijbiomac.2019.08.192

Cited by 16 publications

(10 citation statements)

References 48 publications

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“…The presence of pores increases surface areas for enzyme adsorption [36][37][38][39]. Studies showed that the presence of micropores of silica aerogels protects lipase against alterations of the microenvironment and increases surface areas [40,41].…”

Section: Pore and Particle Sizesmentioning

confidence: 99%

“…Studies showed that the presence of micropores of silica aerogels protects lipase against alterations of the microenvironment and increases surface areas [40,41]. Porous carriers can be divided into three main categories, known as microporous, mesoporous, and macroporous materials [36,37]. Each type of support has different capabilities and disabilities [36].…”

Section: Pore and Particle Sizesmentioning

confidence: 99%

“…Each type of support has different capabilities and disabilities [36]. The pore diameters on microporous supports are too small for enzyme diffusion, even though the supports have strong adsorption and large surface areas [37][38][39]. Mesoporous supports are commonly used to immobilize lipases and peroxidase [42,43].…”

Section: Pore and Particle Sizesmentioning

confidence: 99%

“…The enzymes can be quickly immobilized on macroporous materials but also leach out quickly, mainly when the pH values of the media vary [48]. Macroporous supports only possess a small surface area and yield a low loading amount of enzymes, which is one of the significant problems in industrial applications [37,49].…”

Section: Pore and Particle Sizesmentioning

confidence: 99%

“…The physicochemical properties of macroporous resin NKA matrix supports are crucial for Burkholderia cepacia lipase immobilization, which influences enzyme loading as well as catalytic behavior [69]. A study showed that macroporous supports (5-50 µm) provide channels for mass transfer of Phospholipase D and substrates while mesoporous supports (10-50 nm) have high surface areas for enzyme adsorption [37]. Besides, polystyrenic macroporous resin (Purolite ® A109), which has better internal diffusional properties, excellent mechanical stability, high particle diameters (400 µm), and robustness, enables the efficient application of immobilized Candida sp.…”

Section: Criteriamentioning

confidence: 99%

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The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

et al. 2020

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Four major enzymes commonly used in the market are lipases, proteases, amylases, and cellulases. For instance, in both academic and industrial levels, microbial lipases have been well studied for industrial and biotechnological applications compared to others. Immobilization is done to minimize the cost. The improvement of enzyme properties enables the reusability of enzymes and facilitates enzymes used in a continuous process. Immobilized enzymes are enzymes physically confined in a particularly defined region with retention to their catalytic activities. Immobilized enzymes can be used repeatedly compared to free enzymes, which are unable to catalyze reactions continuously in the system. Immobilization also provides a higher pH value and thermal stability for enzymes toward synthesis. The main parameter influencing the immobilization is the support used to immobilize the enzyme. The support should have a large surface area, high rigidity, suitable shape and particle size, reusability, and resistance to microbial attachment, which will enhance the stability of the enzyme. The diffusion of the substrate in the carrier is more favorable on hydrophobic supports instead of hydrophilic supports. The methods used for enzyme immobilization also play a crucial role in immobilization performance. The combination of immobilization methods will increase the binding force between enzymes and the support, thus reducing the leakage of the enzymes from the support. The adsorption of lipase on a hydrophobic support causes the interfacial activation of lipase during immobilization. The adsorption method also causes less or no change in enzyme conformation, especially on the active site of the enzyme. Thus, this method is the most used in the immobilization process for industrial applications.

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Section: Pore and Particle Sizesmentioning

confidence: 99%

Section: Pore and Particle Sizesmentioning

confidence: 99%

Section: Pore and Particle Sizesmentioning

confidence: 99%

Section: Pore and Particle Sizesmentioning

confidence: 99%

Section: Criteriamentioning

confidence: 99%

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The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

et al. 2020

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Phospholipase D Immobilization on Lignin Nanoparticles for Enzymatic Transformation of Phospholipids

Rossato,

Morsali,

Ruffini

et al. 2023

ChemSusChem

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Lignin nanoparticles (LNPs) are promising components for various materials, given their controllable particle size and spherical shape. However, their origin from supramolecular aggregation has limited the applicability of LNPs as recoverable templates for immobilization of enzymes. In this study, we show that stabilized LNPs are highly promising for the immobilization of phospholipase D (PLD), the enzyme involved in the biocatalytic production of high‐value polar head modified phospholipids of commercial interest, phosphatidylglycerol, phosphatidylserine and phosphatidyl‐ethanolamine. Starting from hydroxymethylated lignin, LNPs were prepared and successively hydrothermally treated to obtain c‐HLNPs with high resistance to organic solvents and a wide range of pH values, covering the conditions for enzymatic reactions and enzyme recovery. The immobilization of PLD on c‐HLNPs (PLD‐c‐HLNPs) was achieved through direct adsorption. We then successfully exploited this new enzymatic preparation in the preparation of pure polar head modified phospholipids with high yields (60‐90%). Furthermore, the high PLD‐c‐HLNPs stability allows its recycling for a number of reactions with appreciable maintenance of its catalytic activity. Thus, PLD‐c‐HLNPs can be regarded as a new, chemically stable, recyclable and user‐friendly biocatalyst, based on a biobased inexpensive scaffold, to be employed in sustainable chemical processes for synthesis of value‐added phospholipids.

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Preparation and characterization of a novel 3D polymer support for the immobilization of cyclodextrin glucanotransferase and efficient biocatalytic synthesis of α-arbutin

Zhao

Zhou²,

Long³

et al. 2022

Biochemical Engineering Journal

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Efficient immobilization of phospholipase D on novel polymer supports with hierarchical pore structures

Cited by 16 publications

References 48 publications

The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

Phospholipase D Immobilization on Lignin Nanoparticles for Enzymatic Transformation of Phospholipids

Preparation and characterization of a novel 3D polymer support for the immobilization of cyclodextrin glucanotransferase and efficient biocatalytic synthesis of α-arbutin

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