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 activity of amylase, sucrase, protease and lipase has been examined in Wallago attu, Clarias batrachus and Labeo rohita. The optimum pH value for carbohydrases ranges from 5.0 to 7.0 and that for trypsin between pH 6.8 and 7.8. Lipase is active at a slightly more alkaline medium. The optimum pH for a given enzyme varies in different sections of the alimentary canal of the same fish and also from species to species. Variations are also found in the optimum substrate concentration for a given enzyme in the different sections of the alimentary canal. The activity of carbohydrases is higher in the herbivorous fish Labeo, than in the carnivorous fish Wallago, and the omnivorous fish Clarias. As for protease, maximum activity is found in Wallago. The difference is not so well marked for the activity of lipase. There is a correlation between the normal diet of the fishes and the relative activity of the digestive enzymes.
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PMID:Digestive enzymes of three teleost fishes. 1 77

The activity of carbohydrases in Puntius sophore (Ham.), Channa gachua (Ham.) and Cirrhinus mrigala (Ham.) has been studied. The carbohydrases have been found in the stomach, intestinal bulb, intestine, pyloric caeca and the hepato-pancreas. The hepatopancreas is the main site of production of these enzymes and it is in this organ and the intestine that their activity is highest. Their pH optimum lies between 5.4 and 6.4. The enzyme equipment in the teleost is adapted to their respective food and feeding habits both qualitatively and quantitatively. In Puntius (omnivorous) and Cirrhinus (herbivorous) all three carbohydrases, namely amylase (EC 3.2.1.1.), sucrase (EC 3.2.1.26.) and raffinase, while in Channa (carnivorous) only amylase and sucrase have been found to be active. In Cirrhinus mrigala, which is predominantly a herbivorous species, the concentration of carbohydrases is higher than those in the other two fishes.
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PMID:Carbohydrase activity in the digestive system of some teleost fishes. 2 Mar 12

Mycelial and yeast forms of P. brasiliensis were tested for several glucohydrolases. In addition to high levels of beta-glucanases, low amounts of alpha-glucanase, chitinase and maltase were found. Tests for invertase, amylase and lactase were negative. The levels of beta-1,3-glucanase were higher in the mycelial form. The shift to the mycelial phase correlated with an increase in the levels of beta-1,3-glucanase. The enzyme was present in the cytoplasm, cell wall and culture medium. The extracellular enzyme was purified 42 fold by ammonium sulphate precipitation and gel filtration. Maximal activity was obtained at 60 degrees C and pH of 5.0 (acetate buffer or pH 6.0 (phosphate buffer). Its Km was 0.205 mg/ml. The cell wall-bound enzyme showed a higher temperature optimum. Optimum pH and Km were also slightly different. Following treatment of the cell walls with chitinase, beta-1,3-glucanase was released into the medium.
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PMID:Beta-1-3-glucanase and dimorphism in Paracoccidioides brasiliensis. 4 May 30

Amphipathic enzymes, invertase (EC 3.2.1.26), 8-amylase (EC 3.2.1.3), and alkaline phosphatase (EC 3.1.3.1), were purified from the rat small intestinal mucosa as trypsin and Triton forms, the catalytic and regulatory characteristics of which were compared in rats and in drosophila. Differences in the catalytic propertiis of the two enzyme forms were demonstrated, which suggested that the hydrophobic part of the enzyme was involved in maintaining optimal conformation of the catalytic part. Many modifiers have beenfound to influence the Triton rather than the trypsin form of the enzyme. It is therefore suggested that the hydrophobic sub-units of the enzymes might be involved in transmitting information from the cytoplasm into the external surface of the membrane, the cell in this way regulating the activity of surface enzymes. If this is indeed the case, it is suggested that the hydrophobic part performs functions not only of external but also of internal regulation.
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PMID:Catalytic and regulatory properties of the Triton and trypsin forms of the brush border hydrolases. 4 Aug 47

The activity of pectine-lyase, polygalacturonase, pectine-methyl-esterase, amylase, and saccharase in Pythium ultimum, Pythium oligandrum, and Pythium debaryanum was determined. Cultures of fungi were cultivated under different temperatures and pH-values within 24 hours and 15 days. The optimum temperature for production of the mentioned enzymes was found to be 24 degrees C. Furthermore, the influence of pH and age of culture on activity of enzyme was investigated. The same trend was found in all the fungus species examined.
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PMID:Activity of pectinases, amylases, and saccharase in Pythium spp. 9 72

Preplant applications of potassium azide (KN3) to pine nursery beds were evaluated for effect on the soil microflora and on soil enzyme activity where either plastic-sealing or water-sealing techniques were used. Two weeks after incorporation of azide (0-224 kg/hs), soil samplings revealed reduced populations of bacteria and fungi and a corresponding decline in invertase and amylase activities. These effects were proportionate to the amount of azide used and were more pronounced in plastic-sealed plots. Phosphatase activity was little affected. Five weeks after azide application, bacterial populations were higher in treated plots than in controls. Greater numbers of bacteria were recorded from plastic-sealed plots and highest populations coincided with plots receiving the highest rates of azide, regardless of the sealing technique. Fungal populations at this sampling were generally less in treated plots than in the controls, but were higher under plastic seal. At this time, changes in invertase and amylase activities did not correspond to increased microbial numbers. Sixteen weeks after applications of KN3, bacterial populations in treated plots did not differ significantly from controls, but remained higher in plastic-sealed than water-sealed plots. Fungal populations under plastic seal had changed little and remained significantly lower in treated water-sealed plots than in controls. The earlier recorded reduction in invertase and amylase activities was still evident at the final sampling;
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PMID:Effects of potassium azide on soil microbial populations and soil enzymatic activities. 16 68

In three profiles of a semi-gley soil under the floodplain forest, variations were studied in the activities of invertase, amylase, cellobiase, cellulase, proteases, and phosphatases. In the surface soil layer, enzymatic activity was found affected by the soil moisture at a significant level, whereas in the deeper soil layers the influence of aeration was more effective. Moreover, significant correlations could be detected between the amount of available nitrogen and protease activity, while the water-soluble phosphorus acted as a represeive agent on the activity of phosphatases. Existence of correlations between the numbers of microbes and enzymes could be demonstrated for invertase and protases only.
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PMID:Enzymatic activity in a semi-gley soil under the floodplain forest in South Moravia. 20 42

In rats fed for 4, 15, and 30 days with increased amount of proteins, lipids, and carbohydrates, considerable shifts occurred in activity of enzymes of the pancreas (amylase, protease, and lipase) and small intestine (gamma--amylase, maltase group, invertase, peptidhydrolase, monoglyceriflipase). Mathematical analysis suggested a close connection between the adaptive shifts in the enzyme systems maintaining the lumen and the membrane types of digestion. The protein diet augments the proteolytic enzyme chain the lipid diet--the lipolytic chain, and the carbohydrate diet--the carbohydrate chain. The shifts should be regarded as an integrative adaptive response of the enzyme spectrum of the pancreas and small intestine to alterations in the food composition.
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PMID:[Interrelationships between the enzymatic functions of the pancreas and small intestine during adaptive processes]. 36 44

The activities of pectin-methyl-esterase, polygalacturonase, cellulase, amylase, saccharase, and protease of strains of Fusarium oxysporum (Schlecht.) f.sp. pisi (Linford) were studied. The selected strains showed different symptoms and different degrees of pathogenicity on the host plant. The measurements were performed during the growth of strains at constant temperatures and, in another experiment, on the day at different temperatures at which the individual strains were grown. Activities were determined by the plate methods and by the spectrophotometric method. It has been found that enzyme activity of the strains with different degree of pathogenicity show considerable differences in dependence on temperature and growth dynamics.
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PMID:The effect of temperature and age of strains of Fusarium oxysporum on its enzymatic activity. 47 66

The permeability of artificial lipid membranes for six enzymes, e.g. RNAse, trypsin, amylase, aldolase, invertase and alkaline phosphatase, was studied. The permeability coefficient values for these enzymes were calculated. It was shown that the penetration process consists of several steps: adsorption of enzyme on the membrane surface, diffusion of enzyme molecules through the lipid layer and enzyme desorption into the surrounding solution. The results obtained suggest that the diffusion of the enzyme molecules through the lipid layer is the limiting step of the penetration process.
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PMID:[Permeability of artificial lipid membranes to some enzymes]. 62 38


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