300 Units (on sucrose)
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|Content:||300 Units (on sucrose)|
|Storage Temperature:||Below -10oC|
|Formulation:||Supplied as a lyophilised powder|
|Stability:||Minimum 1 year at < -10oC. Check vial for details.|
|Synonyms:||alpha-glucosidase; alpha-D-glucoside glucohydrolase|
|Expression:||Purified from Yeast|
|Specificity:||Hydrolysis of terminal, non-reducing (1,4)-linked α-D-glucose residues with release of D-glucose.|
|Specific Activity:||~ 20 U/mg (30oC, pH 6.8 on sucrose)|
|Unit Definition:||One Unit of sucrase activity is defined as the amount of enzyme required to release one µmole of glucose per minute from sucrose (10 mM) in sodium maleate buffer (100 mM), pH 6.8 at 30oC.|
|Application examples:||Applications for the removal of sucrose in various analytical procedures in the cereals, food and feeds, fermentation and beverage industries.|
|Method recognition:||AOAC Method 2016.06 and GB Standard 5009.255-2016|
High purity Sucrase (from yeast) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Sucrase (E-SUCR) and Fructanase (E-FRMXLQ or E-FRMXPD) are used in the measurement of fructan in foods according to Chinese GB Standard 5009.255-2016 and in the AOAC method 2016.06.
For more products, see Carbohydrate Active enZYmes list.
Validation of Methods
The molecular basis of the effect of temperature on enzyme activity.
Daniel, R. M., Peterson, M. E., Danson, M. J., Price, N. C., Kelly, S. M., Monk, C R., Weinberg, C S., Oudshoorn, M. L. & Lee, C. K. (2010). Biochem. J, 425, 353-360.
Experimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model based on increases in activity and denaturation. The Equilibrium Model provides a quantitative explanation of enzyme thermal behaviour under reaction conditions by introducing an inactive (but not denatured) intermediate in rapid equilibrium with the active form. The temperature midpoint (Teq) of the rapid equilibration between the two forms is related to the growth temperature of the organism, and the enthalpy of the equilibrium (ΔHeq) to its ability to function over various temperature ranges. In the present study, we show that the difference between the active and inactive forms is at the enzyme active site. The results reveal an apparently universal mechanism, independent of enzyme reaction or structure, based at or near the active site, by which enzymes lose activity as temperature rises, as opposed to denaturation which is global. Results show that activity losses below Teq) may lead to significant errors in the determination of ΔG*cat made on the basis of the two-state (‘Classical’) model, and the measured kcat will then not be a true indication of an enzyme's catalytic power. Overall, the results provide a molecular rationale for observations that the active site tends to be more flexible than the enzyme as a whole, and that activity losses precede denaturation, and provide a general explanation in molecular terms for the effect of temperature on enzyme activity.Hide Abstract