Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
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The stability and activity of three hydrolytic enzymes, acid phosphatase (EC 3.1.3.2), beta-fructofuranosidase (EC 3.2.1.26), and beta-glucosidase (EC 3.2.1.4), were studied at 30 degrees C in two-phase systems. They were prepared with equal quantities of buffered water and a water-immiscible organic solvent. Low-molecular-weight acetates and paraffins were tested in this investigation. The kinetic constant of storage inactivation was correlated with the logarithm of solvent polarity. Enzyme stability in the presence of organic phases, whose log P value was included in 1.2-2.2, was greater than the one measured in pure buffered aqueous media. On the other hand, a dramatic enzyme denaturation took place making use of solvents at higher log P-value. Experiments carried out during the 24-h operation clarified that the reaction yield does not depend solely on solvent polarity. Acid phosphatase and beta-glucosidase, which are less resistant than beta-fructofuranosidase to temperature and shear in buffered solutions, showed especially significant enhancement of catalytic activity when hydrolysis was performed with the addition of acetates (50% v/v).
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PMID:Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, beta-glucosidase, and beta-fructofuranosidase. 136 38

We have studied changes in the activity of some lytic enzymes contained in mycelium of Aspergillus niger in cultures relative to the autolytic phase of growth. Acid phosphatase, polygalacturonidase and alpha-amylase activity reached its highest level (40.7, and 8 U/sample, respectively) at the initiation of the autolytic phase of growth. 1.3-beta-Glucanase and beta-N-acetylglucosaminidase reached its highest level (3.5 and 2 U/sample, respectively) during the first days of autolysis. Alkaline phosphatase, cellulase, invertase, esterase, chitinase and proteolytic activity is also present in autolysing mycelium of A. niger, though comparatively low. Their maximum activity coincided with the beginning of the autolytic phase of growth. In all enzymes studied here, as autolyis proceeded, enzyme activity decreased by about 90%. Only esterase activity remained nearly constant throughout the whole period of autolysis described here.
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PMID:Lytic enzyme activity in autolysing mycelium of Aspergillus niger. 634 2

Soil basal respiration potential, metabolic quotient (qCO2), and activities of urease, invertase and acid phosphomonoesterase were investigated in the root-layer of 10-, 40-, and 90-yr-old tea bushes grown on the same type of red soil. The soil daily basal respiration potential ranged from 36.23 to 58.52 mg.kg-1.d-1, and the potentials in the root-layer of 40- or 90-yr-old were greater than that of 10-yr old tea bushes. The daily qCO2, ranging from 0.30 to 0.68, was in the reverse trend. The activities of test three enzymes changed differently with tea bushes' age. Urease activity in the root-layer of all age tea bushes ranged from 41.48 to 47.72 mg.kg-1.h-1 and slightly decreased with tea bushes' age. Invertase activity was 189.29-363.40 mg.kg-1.h-1 and decreased with tea bushes' age, but its activity in the root-layer of 10-year old tea bushes was significantly greater than that in the root-layer soil of 40- or 90-year old tea bushes. Acid phosphomonoesterase activity (444.22-828.32 mg.kg-1.h-1) increased significantly with tea bushes' age. Soil basal respiration potential, qCO2 and activities of 3 soil enzymes were closely related to soil pH, soil organic carbon, total nitrogen and C/N ratio, total soluble phenol, and microbial biomass carbon, respectively.
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PMID:[Soil basal respiration and enzyme activities in the root-layer soil of tea bushes in a red soil]. 1282 66