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Sol-gel Matrix (sol-gel + matrix)

Distribution by Scientific Domains
Chemistry100%

Selected Abstracts

KINETIC BEHAVIOR OF SOYBEAN LIPOXYGENASE: A COMPARATIVE STUDY OF THE FREE ENZYME AND THE ENZYME IMMOBILIZED IN AN ALGINATE SILICA SOL-GEL MATRIX,

JOURNAL OF FOOD BIOCHEMISTRY, Issue 1 2000
AN-FEI HSU
Lipoxygenase (LOX) is an enzyme that regioselectively introduces a hydroperoxide into polyunsaturated fatty acids (PUFA). We recently reported a procedure that immobilizes soybean LOX within an alginate sol-gel matrix. In this study, the kinetic profile of free LOX was compared with that of the sol-gel immobilized LOX. The temperature dependent activity profile of free LOX was optimal at 25C whereas immobilized LOX had optimal activity over the temperature range of 25,35C. Enzyme activity, measured in aqueous buffer, for both the free and immobilized LOX preparations had Km values of 2.5 and 1.40 mmoles/L, respectively, and Vmax values of 0.056 and 0.02 ,mol/min, respectively. The relative rates of oxidation of linoleic acid and acylgfycerols containing linoleoyl residues catalyzed by free and immobilized LOX also were determined The results showed that both free and immobilized LOX favor linoleic acid as a substrate. Relative substrate preference for free LOX was linoleic acid >1-monolinolein > 1,3-dilinolein >trilinolein, and for immobilized LOX was linoleic acid >l, 3-dilinolein >1-monolinolein >trilinolein. In general, LOX immobilized in alginate silica sol-gel matrix retained the physical and chemical characteristics of free LOX. [source]

Amperometric Nitrite Sensor Based on PVP-Os Entrapped in Titania Sol-Gel Matrix

ELECTROANALYSIS, Issue 19 2004
Yancai Li
Abstract A novel nitrite sensor was developed based on the immobilization of a partially quaternized poly(4-vinylpyridine) complexed with [Os(bpy)2Cl]+/2+ (PVP-Os) in a porous TiO2 sol-gel matrix by a vapor deposition method. The preparation process simplified the traditional sol-gel process and prevented the cracking of conventional sol-gel derived glasses. Electrochemical behavior of the sensor was characterized by cyclic voltammetry and shows excellent electrocatalytic response for the reduction of nitrite. Effect of operating potential on electrochemical responses of the sensor was explored for optimum analytical performance by using the amperometric method. The stability of the sensor was also evaluated. [source]

Sol-Gel Entrapped Pyridinium Hydrobromide Perbromide as a Recyclable Bromination Agent: Its Application to a One-Pot Bromination and Dehydrobromination Process

EUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 6 2006
Yevgenia Levin
Abstract Silica sol-gel encaged pyridinium hydrobromide perbromide can be used for clean, odorless bromination of a variety of substrates, including alkenes, ketones, and arenes. The used heterogenized bromination reagent can be recharged with bromine and recycled. In the presence of sol-gel entrapped 1,5,7-triazabicyclo[4.4.0]dec-5-ene, dibromides are dehydrobrominated to give vinyl monobromides and/or alkynes. Encapsulation of the pyridinium derivative and the guanidine base within separate sol-gel matrices enables the use of both opposing reagents in one-pot reactions without their mutual destroying each other. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006) [source]

Electrocatalytic Reduction of Nitrite Ion on a Toluidine Blue Sol-Gel Thin Film Electrode Derived from 3-Aminopropyl Trimethoxy Silane

ELECTROANALYSIS, Issue 22 2007
K. Thenmozhi
Abstract An organically modified sol-gel electrode using 3-aminopropyltrimethoxy silane for covalent immobilization of a redox mediator namely toluidine blue has been reported. Cyclic voltammetric characterization of the modified electrode in the potential range of 0.2,V to ,0.6,V exhibited stable voltammetric behavior in aqueous supporting electrolyte with a formal potential of ,0.265,V vs. SCE, corresponding to immobilized toluidine blue. The electrocatalytic activity of the modified electrode when tested towards nitrite ion exhibited a favorable response with the electrocatalytic reduction of nitrite occurring at a reduced potential of ,0.34,V. A good linear working range from 2.94×10,6,M to 2.11×10,3,M with a detection limit of 1.76×10,6,M and quantification limit of 5.87×10,6,M was obtained for nitrite determination. The stable and quick response (4,s) of the modified electrode towards nitrite under hydrodynamic conditions shows the feasibility of using the present sensor in flow systems. Significant improvements in the operational stability by overcoming the leachability problem and repeatability with a relative standard deviation of 1.8% of the TB thin film sensor have been obtained by the strategy of immobilization of the mediator in the sol-gel matrix. [source]

Amperometric Nitrite Sensor Based on PVP-Os Entrapped in Titania Sol-Gel Matrix

ELECTROANALYSIS, Issue 19 2004
Yancai Li
Abstract A novel nitrite sensor was developed based on the immobilization of a partially quaternized poly(4-vinylpyridine) complexed with [Os(bpy)2Cl]+/2+ (PVP-Os) in a porous TiO2 sol-gel matrix by a vapor deposition method. The preparation process simplified the traditional sol-gel process and prevented the cracking of conventional sol-gel derived glasses. Electrochemical behavior of the sensor was characterized by cyclic voltammetry and shows excellent electrocatalytic response for the reduction of nitrite. Effect of operating potential on electrochemical responses of the sensor was explored for optimum analytical performance by using the amperometric method. The stability of the sensor was also evaluated. [source]

KINETIC BEHAVIOR OF SOYBEAN LIPOXYGENASE: A COMPARATIVE STUDY OF THE FREE ENZYME AND THE ENZYME IMMOBILIZED IN AN ALGINATE SILICA SOL-GEL MATRIX,

JOURNAL OF FOOD BIOCHEMISTRY, Issue 1 2000
AN-FEI HSU
Lipoxygenase (LOX) is an enzyme that regioselectively introduces a hydroperoxide into polyunsaturated fatty acids (PUFA). We recently reported a procedure that immobilizes soybean LOX within an alginate sol-gel matrix. In this study, the kinetic profile of free LOX was compared with that of the sol-gel immobilized LOX. The temperature dependent activity profile of free LOX was optimal at 25C whereas immobilized LOX had optimal activity over the temperature range of 25,35C. Enzyme activity, measured in aqueous buffer, for both the free and immobilized LOX preparations had Km values of 2.5 and 1.40 mmoles/L, respectively, and Vmax values of 0.056 and 0.02 ,mol/min, respectively. The relative rates of oxidation of linoleic acid and acylgfycerols containing linoleoyl residues catalyzed by free and immobilized LOX also were determined The results showed that both free and immobilized LOX favor linoleic acid as a substrate. Relative substrate preference for free LOX was linoleic acid >1-monolinolein > 1,3-dilinolein >trilinolein, and for immobilized LOX was linoleic acid >l, 3-dilinolein >1-monolinolein >trilinolein. In general, LOX immobilized in alginate silica sol-gel matrix retained the physical and chemical characteristics of free LOX. [source]

Sol-gel-derived Poly(dimethylsiloxane) Enzymatic Reactor for Microfluidic Peptide Mapping

CHINESE JOURNAL OF CHEMISTRY, Issue 7 2006
Hui-Ling Wu
Abstract The silica-based poly(dimethylsiloxane) (PDMS) microfluidic enzymatic reactor was reported along with its analytical features in coupling with MALDI TOF and ESI MS. Microfluidic chip was fabricated using PDMS casting and O2 -plasma techniques, and used for the preparation of enzymatic reactor. Plasma oxidation for PDMS enabled the channel wall of microfluidics to present a layer of silanol (SiOH) groups. These SiOH groups as anchors onto the microchannel wall were linked covalently with the hydroxy groups of trypsin-encapsulated sol matrix. As a result, the leakage of sol-gel matrix from the microchannel was effectively prevented. On-line protein analysis was performed with the microfluidic enzymatic reactor by attachment of stainless steel tubing electrode and replaceable tip. The success of trypsin encapsulation was investigated by capillary electrophoresis (CE) detection, and MALDI TOF and ESI MS analysis. The lab-made device provided excellent extent of digestion even at the fast flow rate of 7.0 (L/min with very short residence time of ca. 2 s. In addition, the encapsulated trypsin exhibits increased stability even after continuous use. These features are the most requisite for high-throughput protein identification. [source]