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Sucrase (from yeast)

Sucrase Maltase from yeast E-SUCR
Product code: E-SUCR

300 Units (on sucrose)

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Available for shipping

Content: 300 Units (on sucrose)
Shipping Temperature: Ambient
Storage Temperature: Below -10oC
Formulation: Supplied as a lyophilised powder
Physical Form: Powder
Stability: Minimum 1 year at < -10oC. Check vial for details.
Enzyme Activity: Sucrase/Invertase
EC Number:
CAZy Family: GH13
CAS Number: 9001-42-7
Synonyms: alpha-glucosidase; alpha-D-glucoside glucohydrolase
Source: Yeast
Molecular Weight: 62,000
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 (40oC, 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 40oC.
Temperature Optima: 30oC
pH Optima: 6.8
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 Standards 5009.255-2016

High purity Sucrase (from yeast) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Sucrase and Fructanase (E-FRMXLQ) are used in the measurement of fructan in foods according to Chinese GB Standard 5009.255-2016.

Validation of Methods



Certificate of Analysis
Safety Data Sheet
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.

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Safety Information
Symbol : GHS08
Signal Word : Danger
Hazard Statements : H334
Precautionary Statements : P261, P284, P304+P340, P342+P311, P501
Safety Data Sheet
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