Flow‐through immobilized enzyme reactors based on monoliths: I. Preparation of heterogeneous biocatalysts

Влах, Е. Г.; Tennikova, Tatiana

doi:10.1002/jssc.201200594

Cited by 36 publications

(14 citation statements)

References 145 publications

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“…Also, immobilization enhances enzyme specificity and activity (Pollard et al, 2007;Woodley, 2008;Garcia-Galan et al, 2011), reduces the possibility of contamination by microbes (Singh, 2008), decreases the cost of continuous production, and improves purity of the final products (D'Souza, 1999). Indeed, studies of immobilized enzymes have advanced tremendously since Tosa et al (1967) first utilized immobilized aminoacylase to achieve continuous industrial production of L-amino acids in the 1960s (Tosa et al, 1967;Xie et al, 2009;Abdelmajeed et al, 2012;Vlakh et al, 2013;Contesini et al, 2013). In this study, we utilized DEAE-52 cellulose as the carrier to adsorb and immobilize puerarin glycosidase extracted from M. oxydans CGMCC 1788 to transform puerarin.…”

Section: Brazilian Journal Of Chemical Engineeringmentioning

confidence: 99%

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Liu

Sun

et al. 2014

Braz. J. Chem. Eng.

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-For immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 on DEAE-52 cellulose, the optimal amount of enzyme protein was 12 mg protein: 1 g DEAE-52 cellulose; the optimal pH was 6.5; and the optimal immobilization time was 6 hr. The specific activity of immobilized enzyme was 36.67 mU.g -1 carrier with an immobilization yield of 98.87% and an enzyme recovery yield of 92.43%. The molar transformation rates of puerarin by immobilized enzyme and by the relative bacterial cell amount equal to the same amount of enzyme were 53.3% and 2.2%, respectively, after 1 hr of transformation. The former molar transformation rate, which was similar to that for free enzyme, was more than 24-fold greater than the latter. The immobilized puerarin glycosidase showed improved enzymatic properties and stability. The immobilized puerarin glycosidase retained 88% of its initial activity after being reused 10 times.

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Section: Brazilian Journal Of Chemical Engineeringmentioning

confidence: 99%

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Liu

Sun

et al. 2014

Braz. J. Chem. Eng.

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“…Monoliths are particularly suitable for immobilization of enzymes (such as proteases) that act on molecules that have low diffusional constants. Different strategies for preparation of monolith IMERs have been described [117,127]. On-line sample trypsinization can be performed in seconds using an IMER microreactor [128][129][130].…”

Section: Imer In Bottom-up Htp Ms-based Proteomicsmentioning

confidence: 99%

Use of monolithic supports for high‐throughput protein and peptide separation in proteomics

2017

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The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.

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“…Owing to the mentioned advantages of monoliths, they have become popular not only for application in different kinds of chromatography [8][9][10] and solid-phase extraction [11,12], but also for the preparation of flow-through immobilized enzyme reactors (IMERs) suitable for proteomics [13][14][15][16][17], microfluidic analysis [18,19], pharmaceutics [20,21], biodiesel [22] and oligosaccharides [23,24] production, etc. In most cases, the covalent binding of enzyme to the surface of macroporous monoliths was applied [15,25,26].…”

Section: Introductionmentioning

confidence: 99%

Immobilized enzyme reactors based on monoliths: Effect of pore size and enzyme loading on biocatalytic process

et al. 2017

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Macroporous monolithic columns with different mean pore size (from 360 to 2020 nm) and appropriate flow-through properties were synthesized using free radical in situ copolymerization of glycidyl methacrylate, 2-hydroxyethyl methacrylate and ethylene dimethacrylate. In order to predict the composition of porogen mixture to generate the pores in the interested size interval, the Hildebrand theory was used. Ribonuclease A and its specific low- and macromolecular substrates cytidine-2',3'-cyclic monophosphate sodium salt and RNA were applied as model system. The effect of mean pore size of macroporous monoliths used for enzyme immobilization on molecular recognition and biocatalytic characteristics was examined. The monitoring of RNA degradation was performed using anion-exchange HPLC on monolithic CIM DEAE analytical column. The high efficiency of heterogeneous biocatalysts obtained comparatively to the catalytic reaction of RNA degradation in solution was demonstrated. Additionally, the series of six monolithic immobilized enzyme reactors with different amount of biocatalyst was prepared and studied regarding to the biocatalytic properties at recirculation mode at two experimental variants, e.g. (i) fixed range of concentrations of circulated substrate solutions, and (ii) fixed range of substrate/enzyme molar ratios.

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Flow‐through immobilized enzyme reactors based on monoliths: I. Preparation of heterogeneous biocatalysts

Cited by 36 publications

References 145 publications

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Use of monolithic supports for high‐throughput protein and peptide separation in proteomics

Immobilized enzyme reactors based on monoliths: Effect of pore size and enzyme loading on biocatalytic process

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