Naringinase (Rhamnosidase A) from Thermomicrobia sp.


A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) from Thermomicrobia sp.

SKU: rham142.
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rham142A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) that catalyzes the cleavage of the bond between terminal L(+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is very active on naringin but has also substantial activity with hesperidin as substrate.   


Available as 100 units. 

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Product : Rham142 | Naringinase 100 Units | Price : 280.00 EUR

For further information read more below or download the product sheet (pdf format).


Enzyme activity: Rham142 Rhamnosidase A (naringinase, alpha-L-rhamnosidase)  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, hesperidin and rutin

Activity determination: Rhaminosidase activity was routinely determined in a 100mM KPO4 pH 7.5 buffer for 10 minutes with 2.0mM  final conc. of p-nitro-phenyl-α-L-rhamnopyranoside.

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


Synonyms: glycoside hydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase


Protein family: Glycosyl hydrolase family 78 ( GH78 ) – GH-H clan – CAZy database GH78 family

Enzyme classificationEC

Source: Bacteria; Thermomicrobia strain PRI-1686 

Protein sequence: NBCI protein entry


Structural information: The crystal structure of alpha-L-rhamnosidase from Bacillus sp. GL1, sharing 52% sequence identity with ThermoactiveTM Rhamnosidase A, has been determined to a resolution of 1.9 Å ( Cui et al. 2007 ). –Protein Data Bank entry 2OKX


Substrates: Alpha-L-rhamnosidasaes catalyse the release of terminal rhamnose residues from polysaccharides and glycosides. Of the many natural compounds that contain terminal alpha-L-rhamnose, the flavonoids naringin, hesperidin, rutin and quercitrin have been the main natural test-substrates for alpha-L-rhamnosidases. Of these compounds, ThermoactiveTM Rhamnosidase A was found to be most active on Naringin as shown in Figure 1 (Birgisson et al 2004). The structure of naringin (4′,5,7-trihydroxyflavanone-7-α-L-rhamnopyranoside-(1,2)-β-D-glucopyranoside) and the hydrolysis by rhamnosidase is shown in Figure 2.

A plot of relative enzyme activity using different substrates

Figure 1. Substrate specificity: hydrolysis of terminal non-reducing α-L-rhamnose residues in the flovonoids naringin, hesperdin, rutin and quercitrin




Substrate and reaction catalysed by Rham142 Rhamnosidase


Figure 2. Structure of naringin, with rhamnose 1,2 linked to a glucose residue linked to the flavonoid skeleton, and the hydrolysis of the terminal α-L-rhamnose residues by rhamnosidase


Applications: Naringin is a source of bitter flavor in fruit juice and rhamnosidases with naringinase activity are frequently used for debittering citrus juice. Other biotechnological applications include manufacture of prunin; manufacture of alpha-L-rhamnosidese fom natural glycosides; clarification of juices; enhancement of wine aromas by hydrolysis of terpenyl glycosides; conversion of chloropolysporin B to chloropolysporin C and production of pharmaceutically important compounds by removal of rhamnose residues from steriods such as diosgene, desglucoruscin and ginsenosides-Rg2 (Yadav et al. 2010). Beta-glucosidases may be used in combination with alpha-L-rhamnosidases for removal of glucose from the flavonoid skeleton. ThermoactiveTM  Rhamnosidase A has been successfully demonstrated for use in production of rhamnose from narigin in a bioreactor containing immobilized E. coli cells expressing the gene for the enzyme (Birgisson et al 2007). L-Rhamnose or its derivatives are 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.


Properties of ThermoActiveRhamnosidase A:


Activity of Rham142 vs temperature

Figure 3. Temperature spetrum: The enzyme in relatively active in a rather broad temperature range (45-75°C)with optimum around 65°C



Activity of Rham142 vs pH

Figure 4. pH spectrum: pH range is about 4.5-9 with optimum about pH 7.5




Birgisson H, Hreggvidsson GO, Fridjónsson OH, Mort A, Kristjánsson JK, Mattiasson B (2004) Two new thermostable alpha-L-rhamnosidases from a novel thermophilic bacterium. Enzyme Microb. Technol. 34: 561-571

Birgisson H, Wheat JO, Hreggvidsson GO, Kristjánsson JK, Mattiasson B. (2007) Immobilization of a recombinant Escherichia coli producing a thermostable α-l-rhamnosidase: Creation of a bioreactor for hydrolyses of naringin. Enzyme and Microbial Technology 40:1181-1187

Cui Z, Maruyama Y, Mikami B, Hashimoto W and Murata K (2007) Crystal Structure of Glycoside Hydrolase Family 78 α-L-Rhamnosidase from Bacillus sp. GL. J Mol Biol 374: 384–398

Yadav V, Yadav PK, Yadav S & Yadav KDS (2010) α-L-Rhamnosidase: A review. Process Biochem 45:1226–1235

Additional information

Unit size and price

100 units – EUR 280