Immobilized enzyme reactors in HPLC and its application in inhibitor screening: A review

Fang, Si-Meng; Haina, Wang; Zhao, Zhongxi; Wang, Weihong

doi:10.1016/j.jpha.2011.12.002

Cited by 38 publications

(12 citation statements)

References 31 publications

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“…These reactors may strongly differ in dimensions and structure depending on the experiment and product needed. However, major features that need to be considered for deriving a mathematical model for their quantitative description include their mode of operation, maintenance of reaction conditions (temperature, pH and humidity), and the quality of substrate mixing (Fang et al, 2012). Keeping in view the industrial application of the immobilized enzyme preparations developed in this study, batch reactor experiments were performed at 50 o C, indicating their efficacy for hydrolyzing lactose hydrolysis industrially.…”

Section: Batch Reactorsmentioning

confidence: 99%

Biotechnological Application of Surface Modified Cerium Oxide Nanoparticles

Ansari

Al-Shaeri

2019

Braz. J. Chem. Eng.

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Re-engineering of chemical materials at the nanoscale level that employ modification and improvement in their physical and chemical properties has been constantly pursued for application in biomedical and biotechnology industries. Moreover, immobilization of catalysts on these bio/chemically modified nanomaterials improved the performance of enzymes in a plethora of industrial uses. Hence, in this study, cerium oxide nanoparticles (CNPs) were synthesized and their morphology was investigated by TEM and UV-spectra. They were modified by carboxylation and glutaraldehyde to achieve highly efficient surface functionalized nanomatrices for immobilizing Aspergillus oryzae β-galactosidase for producing lactose-free products in dairy industries. Enzyme activity for soluble and immobilized enzyme was observed in different pH and temperature ranges, and on galactose mediated competitive inhibition offered by the substrate. It was observed that all the enzyme preparations exhibited temperature-optima at 50 °C and pH-optima at pH 4.5, respectively. Michaelis-Menten K m (mmole/L) values were 2.40, 5.88, 6.02 and 6.11 for soluble β-galactosidase, and enzyme immobilized on CNPs, carboxylated CNPs and glutaraldehyde modified CNPs, respectively. However, V max (mmole/L/min) was found to be 518, 507, 495 and 480 for these enzyme preparations under identical conditions. Immobilized enzyme demonstrated excellent reusability even after seven repeat uses. The bioconversion rates of lactose from solution in continuous batch reactors revealed the remarkable catalytic efficiency of β-galactosidase immobilized on glutaraldehyde modified CNPs in comparison to other enzyme preparations.

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Section: Batch Reactorsmentioning

confidence: 99%

Biotechnological Application of Surface Modified Cerium Oxide Nanoparticles

Ansari

Al-Shaeri

2019

Braz. J. Chem. Eng.

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“…The immobilized enzyme with good performance can be used as the screening of TuBb inhibitors [6][7][8] . There are many enzyme immobilization methods and immobilization methods can be roughly summarized as follows: vector adsorption method, including physical adsorption method, covalent binding method and ionic binding method; crosslinking; embedding method, including microcapsules type and grid type [9][10] .…”

Section: Introductionmentioning

confidence: 99%

Preparation of Immobilized Recombinant Tubulin Beta(TuBb) on Chitosan Nanoparticles by Covalent Binding Method

2016

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Abstract.Objective In order to screen TuBb inhibitors, this paper describes the preparation of immobilized TuBb on chitosan nanoparticles. Methods TuBb was immobilized onto chitosan nanoparticles by covalent binding method. Results The results of the univariate test indicated that the highest immobilized yield can be obtained when the optimal immobilization condition was 1 mg of TuBb, 0.5 mol/L of buffer solution with pH 6.5, immobilization 30 min and immobilization at 0-4 . Conclusions The authors conclude that the immobilized TuBb maintain the catalysis properties and can be used as the screening of TuBb inhibitors.

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“…Macroporous polymer monoliths satisfy all the requirements for solid phases intended for preparation of flow‐through biocatalytic systems: low mass transfer resistance, high porosity and appropriate pore size, presence of the native functional groups for protein covalent attachment, chemical and mechanical stability [20]. At present, monolithic immobilized enzyme reactors are used widely in proteomics [21, 22], drug discovery [23], biosensing [24], and biodiesel production [25]. Here we present the development and optimization of enzymatic monolithic reactors using Grindamyl β ‐xylanase and the recombinant β ‐xylosidase for the efficient degradation of xylan into xylooligosaccharides and xylose.…”

Section: Introductionmentioning

confidence: 99%

Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β‐xylosidase from Aspergillus awamori X‐100 and Grindamyl H121 β‐xylanase

Volokitina

Bobrov

Piens

et al. 2014

Biotechnology Journal

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Synergistic action of exo- and endohydrolazes is preferred for effective destruction of biopolymers. The main purpose of the present work was to develop an efficient tool for degradation of xylan. Macroporous lab-made monolithic columns and commercial CIM-Epoxy disk were used to immobilize the recombinant β-xylosidase from Aspergillus awamori and Grindamyl β-xylanase. The efficiency of xylan degradation using the low-loaded β-xylosidase column appeared to be four times higher than for the in-solution process and about six times higher than for the high-loaded bioreactor. Disk bioreactor with the Grindamil β-xylanase operated in a recirculation mode has shown noticeable advantages over the column design. Additionally, a system comprised of two immobilized enzyme reactors (IMERs) was tested to accelerate the biopolymer hydrolysis, yielding total xylan conversion into xylose within 20 min. Fast online monitoring HPLC procedure was developed where an analytical DEAE CIM disk was added to the two-enzyme system in a conjoint mode. A loss of activity of immobilized enzymes did not exceed 7% after 5 months of the bioreactor usage. We can therefore conclude that the bioreactors developed exhibit high efficiency and remarkable long-term stability.

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Immobilized enzyme reactors in HPLC and its application in inhibitor screening: A review

Cited by 38 publications

References 31 publications

Biotechnological Application of Surface Modified Cerium Oxide Nanoparticles

Biotechnological Application of Surface Modified Cerium Oxide Nanoparticles

Preparation of Immobilized Recombinant Tubulin Beta(TuBb) on Chitosan Nanoparticles by Covalent Binding Method

Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β‐xylosidase from Aspergillus awamori X‐100 and Grindamyl H121 β‐xylanase

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