Simultaneous immobilization of glucose oxidase and peroxidase to urea derivative of regenerated acetylcellulose granules

Yotova, Lyubov; Ivanov, Ivan P.

doi:10.1007/bf02787801

Cited by 6 publications

(6 citation statements)

References 17 publications

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“…The early interest toward immobilized multienzyme catalysts is increasing. [1][2][3][4][5] One of the most widely used systems is glucose oxidase and catalase (GODϩCAT), [6][7][8][9] because of their application in food processing, fermentation areas, production of gluconic acid, desugaring of eggs in egg solids production, deoxygenating of liquid foodstuffs, chemical processing, analytical practice, and medicine. GOD catalyzes the conversion of glucose and oxygen to gluconic acid and hydrogen peroxide.…”

Section: Introductionmentioning

confidence: 99%

“…Versatile methods for immobilization of the dual enzyme GODϩCAT on various carriers have been developed. 10 -14 The use of matrix-bound enzymes has the two following serious problems: (1) The effectivity of the enzyme catalysts is limited by substrate masstransfer; (2) Catalase coimmobilized to decompose H 2 O 2 resulting from the first enzyme reaction is also inactivated by hydrogen peroxide. The use of porous polymer membranes as carriers for immobilization of enzymes makes the solving of these problems easier.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Simultaneous covalent immobilization of glucose oxidase and catalase onto chemically modified acrylonitrile copolymer membranes

Godjevargova¹,

Dayal²,

Marinov³

2004

J of Applied Polymer Sci

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Ultrafiltration membranes from acrylonitrile copolymer were chemically modified with different concentrations of hydrogen peroxide (from 5 to 30% H 2 O 2 ). The amount of the amide groups in the modified membranes was determined. The water flow and permeability coefficients of the initial and modified membranes were also researched. The modified membranes were used as carriers for covalent immobilization of the dual enzyme system of glucose oxidase and catalase (GODϩCAT). It was found that the best matrices for immobilization of the dual system were membranes modified with 20% H 2 O 2 and the optimal activity ratio was GOD : CAT ϭ 1 : 5. The glucose conversion efficiency with the dual enzyme system was twice as high as that of bound GOD alone. Some of the basic characteristics (optimum pH, optimum temperature, pH, temperature stability, and storage stability) of the dual enzyme system were determined and compared with characteristics of free and bound enzymes. The catalytic parameters of the enzyme reaction (K m and V max ) were determined with GOD immobilized alone and with the dual system GODϩCAT. The higher rate observed with the dual enzyme system clearly showed the advantage and the efficiency of the immobilized system. Glucose oxidase without catalase was deactivated by H 2 O 2 more rapidly than the immobilized dual GODϩCAT system. These experimental evidences can be explained by the protecting effect of catalase on glucose oxidase from inhibition by H 2 O 2 .

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Simultaneous covalent immobilization of glucose oxidase and catalase onto chemically modified acrylonitrile copolymer membranes

Godjevargova¹,

Dayal²,

Marinov³

2004

J of Applied Polymer Sci

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“…this method was applied in previous research as well. the advantage of the method is that immobilization does not change the conformation of the enzyme molecule and binding always takes place outside the active centres (27). the catalytic properties of hRP and tyrosinase on the different membranes are presented in Table 1 and Table 2.…”

Section: Resultsmentioning

confidence: 99%

Co-Immobilization of Peroxidase and Tyrosinase onto Hybrid Membranes Obtained by the Sol-Gel Method for the Construction of an Optical Biosensor

Yotova

Yaneva

Marinkova

et al. 2013

Biotechnology & Biotechnological Equipment

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“…7,8 Nevertheless, the introduction of reactive groups into cellulose that may allow a covalent, nonreversible attachment of biomolecules leads to more stable systems. [9][10][11][12] Quite recently, polyamidoamine (PAMAM) dendrimer-modified cellulose film surfaces were prepared either as a composite material or by covalent binding using 1,3-phenylene diisocyanate as a linker. The ability for enzyme immobilization using laccase as a model enzyme was demonstrated.…”

Section: Introductionmentioning

confidence: 99%

“…Due to the excellent biocompatibility, hydrophilicity, and the nontoxicity, cellulose is also a useful support for the immobilization of enzymes . Different types of unmodified cellulose shapes (e.g., fibers and membranes) and various cellulose derivatives were used as support to immobilize enzymes or cells, attached by physical adsorption or ionic interactions. − In this regard, polyelectrolyte complex (symplex) capsules formed from oppositely charged polyelectrolytes, for example, cellulose sulfate and poly(dimethyldiallylammonium) chloride were successfully used to entrap sensitive biological materials including enzymes. , Nevertheless, the introduction of reactive groups into cellulose that may allow a covalent, nonreversible attachment of biomolecules leads to more stable systems. − …”

Section: Introductionmentioning

confidence: 99%

Biofunctional Surfaces Based on Dendronized Cellulose

et al. 2009

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Biofunctionalized surfaces based on dendronized cellulose were prepared either by embedding 6-deoxy-6-(1,2,3-triazolo)-4-polyamidoamine (PAMAM) cellulose (degree of substitution, DS 0.25), obtained by homogeneous conversion of 6-deoxy-6-azido cellulose with propargyl-PAMAM dendron via the copper-catalyzed Huisgen reaction, in a cellulose acetate (DS 2.50) matrix or by the heterogeneous functionalization of deoxy-azido cellulose film with the dendron. The amount of amino groups provided by the solid supports was determined and the covalent attachment of enzyme was proven with glucose oxidase as model enzyme after activation with glutardialdehyde. The quality of glucose oxidase immobilization was defined by determining of the specific enzyme activity, coupling efficiency, storage stability, and reproducibility. Although the heterogeneous functionalization of the deoxy-azido film yields a product that binds more enzyme compared to the blend of dendronized cellulose derivative with cellulose acetate, the coupling efficiency is comparatively small. Nevertheless, the different approaches for the preparation of biofunctionalized surfaces based on dendronized cellulose provide an excellent reproducibility and good storage stability.

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Simultaneous immobilization of glucose oxidase and peroxidase to urea derivative of regenerated acetylcellulose granules

Cited by 6 publications

References 17 publications

Simultaneous covalent immobilization of glucose oxidase and catalase onto chemically modified acrylonitrile copolymer membranes

Simultaneous covalent immobilization of glucose oxidase and catalase onto chemically modified acrylonitrile copolymer membranes

Co-Immobilization of Peroxidase and Tyrosinase onto Hybrid Membranes Obtained by the Sol-Gel Method for the Construction of an Optical Biosensor

Biofunctional Surfaces Based on Dendronized Cellulose

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