Description
A Thermostable α-L-rhamnosidase that catalyzes the cleavage of the bond between terminal L(+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is also very active on naringin. L-Rhamnose or its derivatives is a suitable chiral structural component and can be used for the synthesis of pharmaceutical products, plant protection agents and the preparation of fragrances in the foodstuffs and perfume industries.
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Product : Rham143 | Hesperedinase 100 Units | Price : 290.00 EUR
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Mode of action: The enzyme catalyzes the cleavage of the bond between terminal L(+)-rhamnose and the aglycone of rhamnose-containing glycosides. Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides, Naringin, Hesperdin and Rutin.
Unit Definition: One unit (U) of enzyme activity is the amount that leads to the release of 1 µmol of p-nitro-phenyl-α-L-rhamnopyranoside (pnpR) per minute.
Temperature Optimum: The enzyme in relatively active in a rather broad temperature range (45-75°C)with optimum around 65°C (Figure 1)
pH Optimum: pH range is about 4.5-9 with optimum about pH 7.5
Substrate specificity: Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides, Naringin, Hesperdin and Rutin.
Unit Assay Conditions: Rhaminosidase activity was routinely determined in a 100mM KPO4 pH 7.5 buffer for 10 minutes with 2.0mM final conc. of pnpR.
References:
1) Birgisson, H., Hreggvidsson, G. O., Fridjónsson, O. H., Mort, A., Kristjánsson, J. K., Mattiasson, B., Two new thermostable α-L-rhmnosidases from a novel thermophilic bacterium. Enzyme and Microbial Technology 2004;34:561-571.
2) Birgisson, H., Wheat, J. O., Hreggvidsson, G. O., Kristjánsson, J. K., Mattiasson, B. Immobilization of a recombinant Escherichia coli producing a thermostable α-l-rhamnosidase: Creation of a bioreactor for hydrolyses of naringin. Enzyme and Microbial Technology 2007;40:1181-1187