Functionalized bicomponent polymer membranes as supports for covalent immobilization of enzymes

Sandu, Teodor; Sârbu, Andrei; Damian, Celina Maria; Pătroi, Delia; Iordache, Tanta‐Verona; Budinova, T.; Tsyntsarski, Boyko; Yardim, M. Ferhat; Sirkecioğlu, Ahmet

doi:10.1016/j.reactfunctpolym.2015.09.001

Cited by 15 publications

(4 citation statements)

References 32 publications

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“…2D) showed an increase in the peak intensity of ~70 °C, probably caused by enzyme denaturation added to the water removal energy. Another endothermic peak verified at ~200 °C was likely due to residual glycerol of commercial enzyme (Sandu et al, 2015). Immobead-Ac-KL-Gal kept the exothermic peak at 210 °C and showed other variation peaks at higher temperatures.…”

Section: Thermal and Physico-chemical Study Of Treated Immobead Supports And Their Derivativesmentioning

confidence: 91%

STABILIZATION STUDY OF TETRAMERIC Kluyveromyces lactis β-GALACTOSIDASE BY IMMOBILIZATION ON IMMOBEAD: THERMAL, PHYSICO-CHEMICAL, TEXTURAL AND CATALYTIC PROPERTIES

Gennari

Mobayed

Rafael

et al. 2019

Braz. J. Chem. Eng.

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Section: Thermal and Physico-chemical Study Of Treated Immobead Supports And Their Derivativesmentioning

confidence: 91%

STABILIZATION STUDY OF TETRAMERIC Kluyveromyces lactis β-GALACTOSIDASE BY IMMOBILIZATION ON IMMOBEAD: THERMAL, PHYSICO-CHEMICAL, TEXTURAL AND CATALYTIC PROPERTIES

Gennari

Mobayed

Rafael

et al. 2019

Braz. J. Chem. Eng.

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“…To characterize the occurred changes, various techniques are employed. The characterization techniques like scanning electron microscopy/field emission scanning electron microscopy (SEM/FESEM), transmission electron microscopy (TEM), atomic force microscopy (AFM), Fourier transform infrared spectroscopy (FTIR), attenuated total reflectance‐Fourier transform infrared spectroscopy (ATR‐FTIR), thermal gravimetry analysis (TGA), X‐ray photoelectron spectroscopy (XPS), Raman spectroscopy, confocal laser scanning microscopy (CLSM), and inverted fluorescence microscopy (IFM) have been applied to characterize the enzyme immobilized membrane (Sandu et al., 2015; Taheran et al., 2017; Veismoradi et al., 2019; Wen‐qiong & Xiao‐feng, 2018; Xu et al., 2017). These techniques provide a comprehensive understanding of the enzyme confinement on a membrane and the possible effect on the performance of heterogeneous biocatalyst.…”

Section: Immobilization Of Enzymes On Membranementioning

confidence: 99%

“…Whereas, FTIR, ATR‐FTIR, Raman spectroscopy, and XPS analysis assessed the enzyme immobilization as well determined surface chemical composition. Investigation of thermal behavior of enzyme carrying membrane sample was carried out by TGA analysis (Sandu et al., 2015). Whereas, protein distribution on membrane support is examined by IFM and CLSM.…”

Section: Immobilization Of Enzymes On Membranementioning

confidence: 99%

A review on pectinase properties, application in juice clarification, and membranes as immobilization support

Patel

Chatterjee

Dhoble

2022

Journal of Food Science

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Pectic substances cause haziness and high viscosity of fruit juices. Pectinase enzymes are biological compounds that degrade pectic compounds. Nontoxicity and ecofriendly nature make pectinases excellent biocatalysts for juice clarification. However, the poor stability and nonreusability of pectinases trim down the effectiveness of the operation. The immobilization techniques have gained the attention of researchers as it augments the properties of the enzymes. Literature has reported the stability improvement of enzymes like lipase, laccase, hydrogen peroxidase, and cellulase upon immobilization on the membrane. However, only a few research articles divulge pectinase immobilization using a membrane. The catalysis‐separation synergy of membrane‐reactor has put indelible imprints in industrial applications. Immobilization of pectinase on the membrane can enhance its performance in juice processing. This review delineates the importance of physicochemical and kinematic properties of pectinases relating to the juice processing parameters. It also includes the influence of metal‐ion cofactors on enzymes’ activity. Considering the support and catalytic‐separation facets of the membrane, the prediction of the membrane as support for pectinase immobilization has also been carried out.

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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%

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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Functionalized bicomponent polymer membranes as supports for covalent immobilization of enzymes

Cited by 15 publications

References 32 publications

STABILIZATION STUDY OF TETRAMERIC Kluyveromyces lactis β-GALACTOSIDASE BY IMMOBILIZATION ON IMMOBEAD: THERMAL, PHYSICO-CHEMICAL, TEXTURAL AND CATALYTIC PROPERTIES

STABILIZATION STUDY OF TETRAMERIC Kluyveromyces lactis β-GALACTOSIDASE BY IMMOBILIZATION ON IMMOBEAD: THERMAL, PHYSICO-CHEMICAL, TEXTURAL AND CATALYTIC PROPERTIES

A review on pectinase properties, application in juice clarification, and membranes as immobilization support

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

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