Adsorption and Activity of Lipase on Polyphosphazene-Modified Polypropylene Membrane Surface

Chen, Pengcheng; Qian, Yue-Cheng; Fang, Fei; Zhu, Xueyan; Huang, Xiaojun

doi:10.3390/catal6110174

Cited by 6 publications

(6 citation statements)

References 34 publications

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“…The optimal pH value for free lipase was found to be 7.5, whereas that for immobilized lipase shifted to 8.0. The shift of the optimal pH could be attributed to the changes in the microenvironment of the immobilized enzyme due to the loss of −NH 2 groups on the enzyme surface after coupling to the carriers, leading to increased exposure of the active site to the solvent (Chen, Qian, Fang, Zhu, & Huang, ; Li, Ding, & Zhou, ). The immobilized lipase was also found to possess a wider pH tolerance range than that of the free enzyme.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of lipase onto N -succinyl-chitosan beads and its application in the enrichment of polyunsaturated fatty acids in fish oil

et al. 2017

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Bovine pancreatic lipase was immobilized onto N‐succinyl‐chitosan beads by using N‐(3‐dimethylaminopropyl)‐N′‐ethylcarbodiimide (EDC)/N‐hydroxysuccinimide (NHS) as the activating agent. The immobilized lipase was characterized by Fourier transform infrared spectra and scanning electron microscopy. The activity of the immobilized lipase obtained under the optimized immobilization conditions was found to reach 1,480 U/g, with enzyme activity recovery of 74.5%. Compared to the free lipase, thermal stability of the immobilized lipase was greatly improved. The reusability study indicated that the immobilized lipase retained 76.6% of its initial activity after being recycled five times. A preliminary study indicated that the prepared immobilized lipase can effectively enrich the polyunsaturated fatty acid in fish oil (increasing from 45.1 to 67.7%), of which the combined docosahexaenoic acid and eicosapentaenoic acid contents increased from 16.3 to 27.1%. Practical applications To overcome the drawbacks of using free lipase, an effective method was developed by immobilization of lipase onto N‐succinyl‐chitosan beads using EDC/NHS as the activating agent. The immobilized lipase prepared by this method may find application in the enrichment of polyunsaturated fatty acids of fish oil.

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Section: Resultsmentioning

confidence: 99%

Immobilization of lipase onto N -succinyl-chitosan beads and its application in the enrichment of polyunsaturated fatty acids in fish oil

et al. 2017

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“…Enzymatic membrane bioreactors (EMBRs), combined with enzyme immobilization and membrane technology, exhibit synergistic catalysis and separation by integrating the high catalytic efficiency of enzymes with the high selectivity of membrane separation; this technique has shown great potential in many fields, such as the food industry, chemical manufacturing, and environmental purposes [ 1 , 2 , 3 , 4 , 5 , 6 ]. Nevertheless, there are still some concerns and urgent problems to be solved in the future research and application of EMBRs, one of the most crucial of which is the enhancement of the catalytic properties [ 7 , 8 , 9 ]. The performance of EMBRs is mainly dependent on the enzyme loading and activity, which are intricately connected with the microstructure and microenvironment of the supporting membrane, respectively [ 10 , 11 , 12 ].…”

Section: Introductionmentioning

confidence: 99%

“…The performance of EMBRs is mainly dependent on the enzyme loading and activity, which are intricately connected with the microstructure and microenvironment of the supporting membrane, respectively [ 10 , 11 , 12 ]. It is well known that high enzyme loading can greatly promote the catalytic efficiency of EMBRs and thus, many relevant methods have been developed in the past decades [ 9 , 13 ]. Some researchers focused on the immobilization behavior of the enzyme, including chemical bonding, physical adsorption, and entrapment [ 13 , 14 , 15 ].…”

Section: Introductionmentioning

confidence: 99%

“…Some researchers focused on the immobilization behavior of the enzyme, including chemical bonding, physical adsorption, and entrapment [ 13 , 14 , 15 ]. Others studied ways to immobilize as many enzyme molecules as possible through surface modification of the membrane [ 9 , 16 ]. However, the decrease in enzyme activity induced by aggregation of the enzyme molecules is often ignored [ 12 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Enzymes on a Phospholipid Bionically Modified Polysulfone Gradient-Pore Membrane for the Enhanced Performance of Enzymatic Membrane Bioreactors

et al. 2018

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Enzymatic membrane bioreactors (EMBRs), with synergistic catalysis-separation performance, have increasingly been used for practical applications. Generally, the membrane properties, particularly the pore structures and interface interactions, have a significant impact on the catalytic efficiency of the EMBR. Therefore, a biomimetic interface based on a phospholipid assembled onto a polysulfone hollow-fiber membrane with perfect radial gradient pores (RGM-PSF) has been prepared in this work to construct a highly efficient and stable EMBR. On account of the special pore structure of the RGM-PSF with the apertures decreasing gradually from the inner side to the outer side, the enzyme molecules could be evenly distributed on the three-dimensional skeleton of the membrane. In addition, the supported phospholipid layer in the membrane, prepared by physical adsorption, was used for the immobilization of the enzymes, which provides sufficient linkage to prevent the enzymes from leaching but also accommodates as many enzyme molecules as possible to retain high bioactivity. The properties of the EMBR were studied by using lipase from Candida rugosa for the hydrolysis of glycerol triacetate as a model. Energy-dispersive X-ray and circular dichroism spectroscopy were employed to observe the effect of lecithin on the membrane and structure changes in the enzyme, respectively. The operational conditions were investigated to optimize the performance of the EMBR by testing substrate concentrations from 0.05 to 0.25 M, membrane fluxes from 25.5 to 350.0 L·m−2·h−1, and temperatures from 15 to 55 °C. As a result, the obtained EMBR showed a desirable performance with 42% improved enzymatic activity and 78% improved catalytic efficiency relative to the unmodified membrane.

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“…Enzyme immobilization can overcome these limitations [12][13][14][15]. Besides increasing the enzyme reusability and stability, enzyme immobilization can also greatly improve the enzyme activity [16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Using Laccases in the Nanoflower to Synthesize Viniferin

Zhu

et al. 2017

Catalysts

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Abstract:The laccase-incorporated nanoflower was fabricated and characterized by scanning electron microscope (SEM) and Fourier transform infrared spectroscopy (FTIR). SEM images indicate that the laccase-incorporated nanoflower has a high surface area, which may facilitate the mass transfer of the substrate and the product. FTIR spectrums identify the existence of laccase in the nanoflowers. The novel immobilized laccase was used for the synthesis of viniferin. The reaction conditions had been optimized and the laccase-incorporated nanoflower can show its maximum specific activity (16.3 µmol/g/h) under the optimal reaction conditions. The specific activity of the laccase in the nanoflowers is enhanced about 2.2-fold compared with free laccase in solution without copper (II) ions. Furthermore, the laccase in the nanoflowers shows an increase in specific activity of~180% compared with free laccase in a solution containing high concentrations (similar to the concentration in the flower) of copper (II) ions. The results also indicate that the laccase in the nanoflowers retain 93.2% of its initial specific activity even after ten continuous batches.

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Adsorption and Activity of Lipase on Polyphosphazene-Modified Polypropylene Membrane Surface

Cited by 6 publications

References 34 publications

Immobilization of lipase onto N -succinyl-chitosan beads and its application in the enrichment of polyunsaturated fatty acids in fish oil

Immobilization of lipase onto N -succinyl-chitosan beads and its application in the enrichment of polyunsaturated fatty acids in fish oil

Immobilization of Enzymes on a Phospholipid Bionically Modified Polysulfone Gradient-Pore Membrane for the Enhanced Performance of Enzymatic Membrane Bioreactors

Using Laccases in the Nanoflower to Synthesize Viniferin

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