Αποτελέσματα Αναζήτησης
1 Ιουλ 2023 · For short-term effects, enzyme activities were measured at different temperatures and regressed with a model that considered catalytic activation-energy and protein-folding. The model-determined short-term optima were: α-galactosidase, 57.6 °C; sucrase, 53.4 °C; pectinase, 49.4 °C; xylanase, 50.4 °C; and cellulase, 46.5 °C.
- Xylanase Production by a Newly Isolated Aspergillus Foetidus Strain and Its Characterization
Xylanase production was studied at 30 °C for 7 days in...
- Characterization of a Novel Low Molecular Weight Sucrase From Filamentous Fungus Termitomyces Clypeatus
Sucrase is a secretory enzyme of the filamentous fungus...
- Factors Affecting Foaming Behavior in Cellulase Fermentation by Trichoderma Reesei Rut C-30
1.. IntroductionFoam fractionation is a promising tool for...
- Molecular Breeding of Cellulolytic Microbes, Plants, and Animals for Biomass Utilization
This enzyme is a heat-stable protein having maximum activity...
- Purification and Partial Characterization of Fructosyltransferase and Invertase From Aspergillus Niger As0023
The two enzymes activity was measured by the standard...
- A New Understanding of How Temperature Affects The Catalytic Activity of Enzymes
An important feature in many of these cellular and...
- The Temperature Optima of Enzymes
The variation of enzymic rate with temperature and time...
- Xylanase Production by a Newly Isolated Aspergillus Foetidus Strain and Its Characterization
The results provide evidence for a new and fundamental third thermal parameter of enzymes, Teq, arising from a subsecond timescale-reversible temperature-dependent equilibrium between the active enzyme and an inactive (or less active) form.
24 Αυγ 2023 · Introduction. Enzymes are responsible for catalysis in virtually all biological systems 1, 2, and a rational framework to improve their activity is critical to promote biotechnological...
13 Σεπ 2007 · If an enzyme is assayed for a fixed duration over a range of temperatures, we observe a plot with an apparent optimum (Fig. 1). This observed “optimum temperature” is not an intrinsic enzyme property, since it arises from a mixture of thermal properties, and from assay duration.
pH 7.4, 0.12 mM adenosine, and 0.003 units of enzyme. One unit is defined as the amount of enzyme that hydrolyzes 1 mole/min adeno-sine to inosine at 30 °C. Acid phosphatase (EC 3.1.3.2, orthophosphoric-monoester phospho-hydrolase (acid optimum)) activity was measured using p-nitrophenyl phosphate (pNPP)1 as substrate (8). Reaction mixtures (1 ...
2 Σεπ 2013 · A large ΔH eq leads to an enzyme with a sharp and relatively narrow temperature optimum, whereas a small ΔH eq results in an enzyme with a broad temperature optimum, so that activity is relatively less sensitive to changes in temperature (Fig. 3).
Determination of optimum temperature is commonly applied to characterize enzymes. It is based on the graph which shows the change in an enzyme’s activity with increasing temperature. Both the rate of chemical reaction, as well as the rate of enzyme deactivation, increase with increasing temperature.
