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)

In dormant conidia of Aspergillus oryzae, alpha-amylase, invertase, and glucose dehydrogenase were induced by their respective inducers. Neither germination nor swelling occurred during this period.
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PMID:Induction of enzymes in dormant spores of Aspergillus oryzae. 543 36

Based on a glucose oxidase sensor for determination of glucose several glucoseoxidase bioenzyme electrodes have been developed. Enzymes producing glucose by hydrolysis of saccharides (glucamylase, invertase, cellulase) as well as glucose consuming systems (hexo-kinase, glucose dehydrogenase) have been coupled to glucose oxidase. The function of the bienzyme systems was demonstrated by concentration measurements (blood glucose, maltose, ATP, NAD+, starch) and enzyme activity measurements (alpha-amylase, ATPase, lactate dehydrogenase).
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PMID:Glucose oxidase bienzyme electrodes for ATP, NAD+, starch and disaccharides. 677 73

A continuous optical method for the assay of glucose-releasing hydrolases is reported. Particular emphasis is given to the assay of purified sucrase from rabbit small intestine. The procedure requires glucose dehydrogenase and mutarotase. In the presence of the latter enzyme, the initial lag is substantially shortened when glucose is released as alpha-anomer. Under the test conditions used, the method shows a good proportionality up to an activity of 0.2 units/3 ml and may also be applied for measuring the activity in crude homogenates.
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PMID:Continuous optical assay of sucrase and other glucosidases. 741 35

A reliable method for the measurement of various disaccharidase activities such as maltase, isomaltase and sucrase is introduced. It is based on the continuous measurement of liberated glucose by a commercially available glucose dehydrogenase reagent. The procedures were first optimized for enzymes from rat intestinal mucosa. The pH optima were similar (6.3-6.7) for the three enzymes tested, and the apparent Kms were estimated to be 18, 12 and 19 mmol/l for maltase, isomaltase and sucrase, respectively. The procedures were adapted on a Cobas Mira automated analyzer. The assays correlated strongly with the conventional method of Dahlqvist. They were reliable, rapid, easy to perform and validate because the progress curve of each reaction rate can be continuously monitored. The method described has also been applied to human intestinal mucosa (Caco-2 cells).
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PMID:A continuous automated method for the determination of intestinal disaccharidase activities. 981 97

The enzymatic conversion of sugars to hydrogen could be a promising method for alternative fuel production. Maple tree sap is a source of environmental sugar (e.g., sucrose) that has the potential to be converted into hydrogen using the enzymes invertase, glucose dehydrogenase (GDH), hydrogenase, and glucose isomerase (GI) and the cofactor NADP+/NADPH. The kinetics of hydrogen production have been studied, and optimal conditions for hydrogen production are described. At low initial sucrose concentrations, in the absence of glucose isomerase, stoichiometric yields of 1 mol of H2/mol of sucrose were achieved. At higher sucrose concentrations, the yield of hydrogen declined so that at an initial sucrose concentration of 292 mM only 7% yield of hydrogen was obtained. The reason for this low yield was studied and shown not to be caused by enzyme inactivation or a pH drop during the reaction but due to an instability of the cofactor NADP+. Although gluconic acid inhibited both NADPH production and oxidation by GDH and hydrogenase, respectively, it was not the major cause of NADP+ instability. Fructose was also shown to be converted to hydrogen if GI was present in the reaction mixture. Also, by starting with sucrose, 1. 34 mol of H2/mol of sucrose was obtained if GI was present in the reaction mixture.
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PMID:Enzymatic conversion of sucrose to hydrogen 984 53

A photoinduced hydrogen production system, coupling sucrose degradation with invertase and glucose dehydrogenase (GDH) and hydrogen production with colloidal platinum as a catalyst using the visible light-induced photosensitization of Mg chlorophyll-a (Mg Chl-a), has been developed. Continuous hydrogen gas production was observed when the reaction mixture containing sucrose, invertase, GDH, nicotinamide adenine dinucleotide (NAD(+)), Mg Chl-a, methyl viologen (MV(2+), an electron relay reagent), and colloidal platinum was irradiated by visible light.
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PMID:Visible light induced biohydrogen production from sucrose using the photosensitization of Mg chlorophyll-a. 1212 Nov 48

A complex biocatalyst system with a bioreactor equipped with a microfiltration (MF) module was employed to produce high-content fructooligosaccharides (FOS) in a continuous process initiated by a batch process. The system used mycelia of Aspergillus japonicus CCRC 93007 or Aureobasidium pullulans ATCC 9348 with beta-fructofuranosidase activity and Gluconobacter oxydans ATCC 23771 with glucose dehydrogenase activity. Calcium carbonate slurry was used to control pH to 5.5, and gluconic acid in the reaction mixture was precipitated as calcium gluconate. Sucrose solution with an optimum concentration of 30% (w/v) was employed as feed for the complex cell system, and high-content FOS was discharged continuously from a MF module. The complex cell system was run at 30 degrees C with an aeration rate of 5 vvm and produced more than 80% FOS with the remainder being 5-7% glucose and 8-10% sucrose on a dry weight basis, plus a small amount of calcium gluconate. The system worked for a 7-day continuous production process with a dilution rate of 0.04 h(-1), and the volumetric productivity for total FOS was more than 160 g L(-1) h(-1).
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PMID:Continuous production of high-content fructooligosaccharides by a complex cell system. 1246 63

A photoinduced hydrogen production system that couples sucrose degradation with invertase and glucose dehydrogenase (GDH) and hydrogen production with colloidal platinum as a catalyst using visible light-induced photosensitization of artificial Zn chlorophyll-a (Zn Chl-a) has been developed. Continuous hydrogen gas production over more than 240 min was observed when the reaction mixture containing sucrose, invertase, GDH, nicotinamide adenine dinucreotide (NAD(+)), Zn Chl-a, methyl viologen (MV(2+), an electron relay reagent), and colloidal platinum was irradiated by visible light. Zn Chl-a was superior to that of Mg Chl-a in photostability and photosensitization activity.
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PMID:Biohydrogen production from sucrose using the visible light sensitization of artificial Zn chlorophyll-a. 1252 18

A novel phosphate solubilizing bacterium (PSB) was isolated from the rhizosphere of sugarcane and is capable of utilizing sucrose and rock phosphate as the sole carbon and phosphate source, respectively. This PSB exhibited mineral phosphate solubilizing (MPS) phenotype on sugars such as sucrose and fructose, which are not substrates for enzyme glucose dehydrogenase (GDH), along with GDH substrates, viz., glucose, xylose, and maltose, as carbon sources. PCR amplification of the rRNA gene and sequence analysis identified this bacterium as Citrobacter sp. DHRSS. On sucrose and fructose Citrobacter sp. DHRSS liberated 170 and 100 microM free phosphate from rock phosphate and secreted 49 mM (2.94 g/L) and 35 mM (2.1 g/L) acetic acid, respectively. Growth of Citrobacter sp. DHRSS on sucrose is mediated by an intracellular inducible neutral invertase. Interestingly, in the presence of GDH substrates like glucose and maltose, Citrobacter sp. DHRSS produced approximately 20 mM (4.36 g/L) gluconic acid and phosphate released was 520 and 570 microM, respectively. Citrobacter sp. DHRSS GDH activity was found when grown on GDH and non-GDH substrates, indicating that it is constitutive and could act on a wide range of aldose sugars. This study demonstrates the role of different organic acids in mineral phosphate solubilization by rhizobacteria depending on the nature of the available carbon source.
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PMID:Variation in the nature of organic acid secretion and mineral phosphate solubilization by Citrobacter sp. DHRSS in the presence of different sugars. 1796 11

A "smart" biofuel cell switchable ON and OFF upon application of several chemical signals processed by an enzyme logic network was designed. The biocomputing system performing logic operations on the input signals was composed of four enzymes: alcohol dehydrogenase (ADH), amyloglucosidase (AGS), invertase (INV) and glucose dehydrogenase (GDH). These enzymes were activated by different combinations of chemical input signals: NADH, acetaldehyde, maltose and sucrose. The sequence of biochemical reactions catalyzed by the enzymes models a logic network composed of concatenated AND/OR gates. Upon application of specific "successful" patterns of the chemical input signals, the cascade of biochemical reactions resulted in the formation of gluconic acid, thus producing acidic pH in the solution. This resulted in the activation of a pH-sensitive redox-polymer-modified cathode in the biofuel cell, thus, switching ON the entire cell and dramatically increasing its power output. Application of another chemical signal (urea in the presence of urease) resulted in the return to the initial neutral pH value, when the O(2)-reducing cathode and the entire cell are in the mute state. The reversible activation-inactivation of the biofuel cell was controlled by the enzymatic reactions logically processing a number of chemical input signals applied in different combinations. The studied biofuel cell exemplifies a new kind of bioelectronic device where the bioelectronic function is controlled by a biocomputing system. Such devices will provide a new dimension in bioelectronics and biocomputing benefiting from the integration of both concepts.
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PMID:Biofuel cell controlled by enzyme logic network--approaching physiologically regulated devices. 1935 82


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