Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The main parameters of growth and glucose oxidase production by the mutant Penicillium funiculosum strains BIM F-15.3, NMM95.132, and 46.1 were studied. The synthesis of extracellular glucose oxidase by these strains was constitutive and occurred following the phase of exponential growth. The mutant strains also synthesized extracellular invertase and cell-associated catalase and glucose oxidase. The syntheses of invertase, the cell-associated enzymes, and extracellular glucose oxidase were found to be maximum between 14 and 18 h, between 48 and 52 h, and by the 96th h of cultivation, respectively. Among the mutants studied, P. funiculosum 46.1 showed the maximal rates of growth and glucose oxidase synthesis.
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PMID:[Growth characteristics and glucose oxidase production by mutant Penicillium funiculosum strains]. 1531 27

Fructo-oligosaccharides (FOS) represent the most abundantly supplied and utilized group of nondigestible oligosaccharides as food ingredients. These prebiotics can be produced from sucrose using the transglycosylating activity of beta-fructofuranosidases (EC 3.2.1.26) at high concentrations of the starting material. The main problem during FOS synthesis is that the activity of the enzyme is inhibited by the glucose generated during the reaction, and therefore the maximum FOS content in commercial products reaches up to 60% on a dry substance basis. The glucose oxidase (gox) gene from Aspergillus niger BT18 was cloned and integrated, as part of an expression cassette, into the ribosomal DNA of a Saccharomyces cerevisiae host strain. One of the recombinant strains with a high copy number of the gox gene and showing a high GOX specific activity was used to produce the enzyme. Addition of the extracellular glucose oxidase to the FOS synthesis reaction helped to remove the glucose generated, avoiding the inhibition of the fungal beta-fructofuranosidase. As a result, a final syrup containing up to 90% of FOS was obtained.
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PMID:Expression of an Aspergillus niger glucose oxidase in saccharomyces cerevisiae and its use to optimize fructo-oligosaccharides synthesis. 1688 85

A new colorimetric method for determining the isomerization activity of sucrose isomerase was developed. This colorimetric method is based on the enzymatic reactions of invertase and glucose oxidase-peroxidase (GOD-POD). The main scheme for assaying sucrose isomerase activity is to degrade sucrose in the reaction mixture to glucose and fructose by invertase and to detect the concentration of glucose generated using GOD-POD. The concentrations of trehalulose and isomaltulose, reaction products of sucrose isomerase, are calculated from the concentration of glucose. This method allows rapid and accurate determination of the isomerization activity of sucrose isomerase without inhibition by hydrolysis activity.
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PMID:A new colorimetric method for determining the isomerization activity of sucrose isomerase. 1728 28

In present studies, the new optical sensing platform based on optical planar waveguide (OPWG) for sucrose estimation was reported. An evanescent-wave biosensor was designed by using novel agarose-guar gum (AG) biopolymer composite sol-gel with entrapped enzymes (acid invertase (INV) and glucose oxidase (GOD)). Partially purified watermelon invertase isolated from Citrullus vulgaris fruit (specific activity 832 units mg(-1)) in combination with GOD was physically entrapped in AG sol-gel and cladded on the surface of optical planar waveguide. Na(+)-K(+) ion-exchanged glass optical waveguides were prepared and employed for the fabrication of sucrose biosensor. By addressing the enzyme modified waveguide structure with, the optogeometric properties of adsorbed enzyme layer (12 microm) at the sensor solid-liquid interface were studied. The OPWG sensor with short response time (110 s) was characterized using the 0.2M acetate buffer, pH 5.5. The fabricated sucrose sensor showed concentration dependent linear response in the range 1 x 10(-10) to 1 x 10(-6)M of sucrose. Lower limit of detection of this novel AG-INV-GOD cladded OPWG sensor was found to be 2.5 x 10(-11)M sucrose, which indicates that the developed biosensor has higher sensitivity towards sucrose as compared to earlier reported sensors using various transducer systems. Biochips when stored at room temperature, showed high stability for 81 days with 80% retention of original sensitivity. These sucrose sensing biochips showed good operational efficiency for 10 cycles. The proper confinement of acid invertase and glucose oxidase in hydrogel composite was confirmed by scanning electron microscopy (SEM) images. The constructed OPWG sensor is versatile, easy to fabricate and can be used for sucrose measurements with very high sensitivity.
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PMID:Fabrication of sucrose biosensor based on single mode planar optical waveguide using co-immobilized plant invertase and GOD. 1731 40

Sensors for the simultaneous determinations of sucrose and glucose, lactose and glucose, and starch and glucose were prepared by a combination of the enzyme system shown below and an oxygen electrode: The mechanism for separating the substrates with the proposed sensors is based on the time lag arising from reaction and diffusion. Invertase, beta-galactosidase, amyloglucosidase, mutarotase, and glucose oxidase were covalently immobilized on triacetyl cellulose membranes containing 1,8-diamino-4-aminomethyloctane. A glucose oxidase membrane, mutarotase membrane, three sheets of triacetyl cellulose membranes, and invertase, or beta-galactosidase or amyloglucosidase membrane were placed in that order on the tip of the oxygen electrode. Calibration curves for sucrose, lactose, and starch were linear up to 40 mM, 60-180 mM, and 10%, respectively. The simultaneous determination of sucrose and glucose, lactose and glucose, and starch and glucose was possible when the amount of glucose coexised was in the range of 2-16% sucrose, 2.8-8.3% lactose, or 0.1-1% starch. The relative errors were +/-4% for sucrose and +/-3% for lactose in 100 assays. The starch sensor was reused only five times. Each enzyme membrane was fairly stable for more than 10 days.
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PMID:Development of biosensors for the simultaneous determination of sucrose and glucose, lactose and glucose, and starch and glucose. 1860 Jul 3

We are reporting fabrication and characterization of electrochemical sucrose biosensor using ultra-microelectrode (UME) for the detection of heavy metal ions (Hg(II), Ag(I), Pb(II) and Cd(II)). The working UME, with 25 microm diameter, was modified with invertase (INV, EC: 3.2.1.26) and glucose oxidase (GOD, EC: 1.1.3.4) entrapped in agarose-guar gum. The hydrophilic character of the agarose-guar gum composite matrix was checked by water contact angle measurement. The atomic force microscopy (AFM) images of the membranes showed proper confinement of both the enzymes during co-immobilization. The dynamic range for sucrose biosensor was achieved in the range of 1 x 10(-10) to 1 x 10(-7)M with lower detection limit 1 x 10(-10)M at pH 5.5 with 9 cycles of reuse. The spectrophotometric and electrochemical studies showed linear relationship between concentration of heavy metal ions and degree of inhibition of invertase. The toxicity sequence for invertase using both methods was observed as Hg(2+)>Pb(2+)>Ag(+)>Cd(2+). The dynamic linear range for mercury using electrochemical biosensor was observed in the range of 5 x 10(-10) to 12.5 x 10(-10)M for sucrose. The lower detection limit for the fabricated biosensor was found to be 5 x 10(-10)M. The reliability of the electrochemical biosensor was conformed by testing the spike samples and the results were comparable with the conventional photometric DNSA method.
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PMID:Invertase inhibition based electrochemical sensor for the detection of heavy metal ions in aqueous system: Application of ultra-microelectrode to enhance sucrose biosensor's sensitivity. 1866 98

Stabilisation of electrochemically deposited Prussian blue (PB) films on glassy carbon (GC) electrodes has been investigated and an enhancement in the stability of the PB films is reported if the electrodes are treated with tetrabutylammonium toluene-4-sulfonate (TTS) in the electrochemical activation step following the electrodeposition. A multi-enzyme PB based biosensor for sucrose detection was made in order to demonstrate that PB films can be coupled with an oxidase system. A tri-enzyme system, comprising glucose oxidase, mutarotase and invertase, was crosslinked with glutaraldehyde and bovine albumin serum on the PB modified glassy carbon electrode. The deposited PB operated as an electrocatalyst for electrochemical reduction of hydrogen peroxide, the final product of the enzyme reaction sequence. The electrochemical response was studied using flow injection analysis for the determination of sucrose, glucose and H(2)O(2). The optimal concentrations of the immobilisation mixture was standardised as 8U of glucose oxidase, 8U of mutarotase, 16U of invertase, 0.5% glutaraldehyde (0.025mul) and 0.5% BSA (0.025mg) in a final volume of 5mul applied at the electrode surface (0.066cm(2)). The biosensor exhibited a linear response for sucrose (4-800muM), glucose (2-800muM) and H(2)O(2) (1-800muM) and the detection limit was 4.5, 1.5 and 0.5muM for sucrose, glucose and H(2)O(2), respectively. The sample throughput was ca. 60 samples h(-1). An increase in the operational and storage stability of the sucrose biosensor was also noted when the PB modified electrodes were conditioned in phosphate buffer containing 0.05M TTS during the preparation of the PB films.
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PMID:Prussian blue modified glassy carbon electrodes-study on operational stability and its application as a sucrose biosensor. 1896 61

A spectrophotometric method for determining sucrose is proposed. Sucrose is hydrolyzed by invertase into glucose and fructose. Then, glucose is oxidized in presence of glucose oxidase and the produced hydrogen peroxide reacts with phenol-4-sulfonic acid sodium salt and 4-aminoantipyrine in presence of peroxidase, yielding a pink dye with an absorption maximum at 505 nm. This method was validated following the EURACHEM and VAM project guidelines for method validation. Trueness, precision, robustness, sensitivity and linearity were considered. The method was applied to the determination of sucrose in green and roasted coffee beans. A comparison with the HPLC method with pulsed amperometric detection was carried out.
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PMID:Enzymatic-spectrophotometric determination of sucrose in coffee beans. 1897 Feb 37

A nanostructured system composed of enzyme-functionalized silica microparticles, ca. 74 microm, and gold-coated magnetic nanoparticles, 18 +/- 3 nm, modified with pH-sensitive organic shells was used to process biochemical signals and transduce the output signal into the changes of the optoelectronic properties of the assembly. The enzymes (glucose oxidase, invertase, esterase) covalently bound to the silica microparticles performed Boolean logic operations AND/OR processing biochemical information received in the form of chemical input signals resulting in changes of the solution pH value. Dissociation state of the organic shells on the gold-coated magnetic nanoparticles was controlled by pH changes generated in situ by the enzyme logic systems. The charge variation on the organic shells upon the reversible protonation/dissociation process resulted in the changes of the gold layer localized surface plasmon resonance energy (LSPR), thus producing optical changes in the system. The proton transfer process allowed the functional coupling of the information processing enzyme systems with the signal transducing gold-coated magnetic nanoparticles providing their cooperative performance. Magnetic properties of the gold-coated magnetic nanoparticles allowed separation of the signal-transducing nanoparticles from the enzyme-modified signal processing silica microparticles. The reversible system operation was achieved by the Reset function, returning the pH value and optical properties of the system to the initial state. This process was biocatalyzed by another immobilized enzyme (urease) activated with a biochemical signal. The studied approach opens the way to novel optical biosensors logically processing multiple biochemical signals and "smart" multisignal responsive materials with logically switchable optical properties.
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PMID:Optoelectronic properties of nanostructured ensembles controlled by biomolecular logic systems. 1920 63

Application of Boolean logic operations performed by enzymes to control electrochemical systems is presented. Indium-tin oxide (ITO) electrodes with the surface modified with poly-4-vinyl pyridine (P4VP) brush were synthesized and used as switchable electrochemical systems. The switch ON and OFF of the electrode activity were achieved by pH changes generated in situ by biocatalytic reactions in the presence of enzymes used as input signals. Two logic gates operating as AND/OR Boolean functions were designed using invertase and glucose oxidase or esterase and glucose oxidase as input signals, respectively. The electrode surface coated with a shrunk P4VP polymer at neutral pH values was not electrochemically active because of the blocking effect of the polymer film. The positive outputs of the logic operations yielded a pH drop to acidic conditions, resulting in the protonation and swelling of the P4VP polymer allowing penetration of a soluble redox probe to the conducting support, thus switching the electrode activity ON. The electrode interface was reset to the initial OFF state, with the inhibited electrochemical reaction, upon in situ pH increase generated by another enzymatic reaction in the presence of urease. Logically processed biochemical inputs of various enzymes allowed reversible activation-inactivation of the electrochemical reaction.
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PMID:Switchable electrode controlled by Boolean logic gates using enzymes as input signals. 1962 18


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