(Clostridium thermocellum)

Reference code: E-GALCT

350 Units at 40oC; ~ 770 Units at 60oC

This product has been discontinued

Content: 350 Units at 40oC;
~ 770 Units at 60oC
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: Minimum 1 year at 4oC. Check vial for details.
Enzyme Activity: endo-1,4-β-Galactanase
EC Number:
CAZy Family: GH53
CAS Number: 58182-40-4
Synonyms: arabinogalactan endo-beta-1,4-galactanase; arabinogalactan 4-beta-D-galactanohydrolase
Source: Clostridium thermocellum
Molecular Weight: 44,600
Concentration: Supplied at ~ 125 U/mL
Expression: Recombinant from Clostridium thermocellum
Specificity: endo-hydrolysis of (1,4)-β-D-galactosidic linkages in galactans.
Specific Activity: ~ 15 U/mg (40oC, pH 4.5 on potato galactan); 
~ 30 U/mg (60oC, pH 4.5 on potato galactan)
Unit Definition: One Unit of galactanase activity is defined as the amount of enzyme required to release one µmole of galactose reducing-sugar equivalents per minute from potato galactan in sodium acetate buffer (100 mM), pH 4.5.
Temperature Optima: 60oC
pH Optima: 4.5
Application examples: Applications established in diagnostics and research within the food and feed, carbohydrate and biofuels industries.

This product has been discontinued (read more).

High purity recombinant endo-1,4-β-Galactanase (Clostridium thermocellum) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

See all Carbohydrate Active enZYmes.

Certificate of Analysis
Safety Data Sheet
Data Sheet
Structural modifications of sugar beet pectin and the relationship of structure to functionality.

Funami, T., Nakauma, M., Ishihara, S., Tanaka, R., Inoue, T. & Phillips, G. O. (2011). Food Hydrocolloids, 25(2), 221-229.

The emulsifying properties of sugar beet pectin (SBP) were investigated in relation to its molecular structure. SBP has been subjected to an enhancement process, and this material was here compared with conventional non-enhanced SBP. The oil-in-water emulsification properties of both were compared at 1.5% concentration at pH 3.25, using 15% middle-chain triglyceride as the oil phase. Their emulsification behavior after various enzyme treatments decreased in the order: protease > arabinanase/galactanase mixture > polygalacturonase. The enzyme treatment also decreased the molecular weight of SBP. Protease degraded the high molecular weight carbohydrate–protein complex. Arabinanase/galactanase mixture was more effective in decreasing the emulsification performance than polygalacturonase. The results confirm the key role of protein as the anchor for the oil droplets and identify also the contribution of the neutral lateral chains in stabilizing emulsions by forming a hydrated layer. Protein also aggregates, which functions as a linker for the association of the carbohydrate chains consequent to the enhancement process.

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Precautionary Statements : Not Applicable
Safety Data Sheet
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