Immobilization of <i>Candida lipolytica</i> lipase on macroporous beaded terpolymers with epoxy groups

Li, Wentao; Duan, Haiyan; Meng, Xiangjian; Qin, Dawei; Wang, Xingjian; Zhang, Juan

doi:10.1002/app.38023

Cited by 5 publications

(3 citation statements)

References 25 publications

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“…[5,8,9] Fluorine-based monomers, such as pentafluorostyrene (PFS), have also been used on the manufacture of functionalized polymer materials. [20][21][22][23][24] However, most studies perform the polymer synthesis and functionalization in solution, which is not ideal regarding the production of nanoparticles and enzyme supports.…”

Section: Introductionmentioning

confidence: 99%

Production of New Functionalized Polymer Nanoparticles and Use for Manufacture of Novel Nanobiocatalysts

Pinto

Cipolatti

Manoel

et al. 2020

Macro Materials & Eng

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New nanoparticles are synthesized through emulsion polymerization, using distinct comonomers (styrene, divinylbenzene, glycidyl methacrylate and pentafluorostyrene). Then, for the first time, two strategies are adopted to functionalize such nanoparticles using benzylamine and thiophenol: (i) after the manufacture of the nanoparticles; and (ii) in situ during the polymerization reaction. Afterwards, the functionalized nanoparticles are used as nanosupports for immobilization of lipase B from Candida antarctica and the performance of the novel nanobiocatalysts are evaluated. It is shown that the nanoparticles exhibit different properties (specific areas ranging from 34 m2 g−1 to 324 m2 g−1; and contact angles ranging from 29° to 126°), indicating that both procedures can be used to adjust the properties of the polymer supports. Moreover, the nanobiocatalysts are applied successfully in hydrolysis and esterification reactions, exhibiting higher activities than the non‐functionalized biocatalysts. It is also observed that more hydrophilic supports result in more active biocatalysts in hydrolysis (27 ± 1 U g−1) and intermediate hydrophobic matrices conduct to more active biocatalysts in esterification reactions (1564 ± 50 U g−1). It is shown that highly hydrophobic surfaces may cause a significant decrease in the activity of such biocatalysts, probably due to distortions on the enzyme active center and to more intense chemical partitioning effects.

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Section: Introductionmentioning

confidence: 99%

Production of New Functionalized Polymer Nanoparticles and Use for Manufacture of Novel Nanobiocatalysts

Pinto

Cipolatti

Manoel

et al. 2020

Macro Materials & Eng

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“…Meanwhile, their high cost and difficulty of recycle are also concerned for their industrial applications. An effective method to solve the above problems was the immobilization of cellulases , including adsorption, crosslinked enzyme aggregates, embedding, and covalent binding . Some researchers immobilized cellulase on different carriers, and the obtained immobilized cellulase exhibited excellent residual activities .…”

Section: Introductionmentioning

confidence: 99%

“…A good choice to overcome these questions is using porous terpolymers as the supports instead of inorganic and organic materials. Duan and coworkers chose glycidyl methacrylate (GMA) as the functional monomer of porous terpolymer to immobilize Candida lipolytica lipase, and the results showed that the pore structure of terpolymers was beneficial for immobilization of enzyme. Cao et al immobilized cellulase on a pH‐sensitive polyacrylate terpolymer (P MDB ) and they found that the terpolymer had better immobilization efficiency.…”

Section: Introductionmentioning

confidence: 99%

Preparation of magnetic porous terpolymer and its application in cellulase immobilization

Duan

Wang

et al. 2014

Polymer Engineering & Sci

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In this work, a series of porous terpolymers with degrees of crosslinking at 30–65% were synthesized by suspension polymerization. Fe3O4 nanoparticles were used to modify the porous terpolymer with degree of crosslinking at 30%. The resulting terpolymers with mean pore size of 10–30 nm were used as supports for immobilization of cellulases through covalent bondings. The Fourier transform infrared spectroscopy and thermal gravity analysis measurements demonstrated that cellulases were immobilized onto the porous terpolymers. The effects of pH and temperature on enzyme activity were investigated in acetate buffer medium by hydrolysis of sodium carboxymethyl celluloses. The reusability of immobilized cellulases was also investigated. The result showed that immobilized cellulases exhibited higher residual activities and enzyme activities than free cellulases in wide ranges of pH and temperature. We also found that the reusability of cellulases immobilized on terpolymers with magnetism was better than that of cellulases immobilized on terpolymers without magnetism. POLYM. ENG. SCI., 55:1039–1045, 2015. © 2014 Society of Plastics Engineers

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The optimization of glycidyl methacrylate based terpolymer monolith synthesis: an effective Candida rugosa lipase immobilization support

et al. 2020

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Immobilization of Candida lipolytica lipase on macroporous beaded terpolymers with epoxy groups

Cited by 5 publications

References 25 publications

Production of New Functionalized Polymer Nanoparticles and Use for Manufacture of Novel Nanobiocatalysts

Production of New Functionalized Polymer Nanoparticles and Use for Manufacture of Novel Nanobiocatalysts

Preparation of magnetic porous terpolymer and its application in cellulase immobilization

The optimization of glycidyl methacrylate based terpolymer monolith synthesis: an effective Candida rugosa lipase immobilization support

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