Creative Enzymes is a global leader in the development and supply of enzyme activity assays. We serve the needs of our countless customers in the pharmaceutical, biotechnological and diagnostic industries. Now, we are proud to offer the most reliable activity assays for alpha-L-rhamnosidases. Fully equipped with the most advanced spectrophotometric instrument, we guarantee the quality of tests in a professional and timely manner.

Alpha-L-rhamnosidases (EC 3.2.1.40; alpha-L-rhamnoside rhamnohydrolase) are widely distributed in nature and have been found in animal tissues, plants, yeasts, fungi and bacteria. Published data has on the other hand primarily been on rhamnosidases of fungal origins. Alpha-L-rhamnosidases are exo-type enzymes. They remove terminalα-L-rhamnosyl groups at the end of polysaccharides and glycosides containing L-rhamnose. Alpha-L-rhamnosidases belong to the glycoside hydrolase family 78 and they are the only enzymes in the family 78 to date.

A variety of industrial applications have been recognized for alpha-L-rhamnosidases. They have been used for debittering of grapefruit juices by hydrolysis of naringin to prunin and L-rhamnose. The enzyme has also been used for clarification of orange juices by hydrolysis of hesperidin and pectin and for liberating monoterpenols in wines, which contributes significantly to the aroma and flavor of wines. Alpha-L-rhamnosidases can be exploited in the production of the pure stereoisomer L-rhamnose from naringin which can act as a chiral center in chemical synthesis and as a precursor for the industrial production of aromatic compounds and flavors. Rutin and quercitrin, the most common flavonoid glycosides in the human diet, have been reported as substrates for alpha-L-rhamnosidases. Thus, alpha-L-rhamnosidases are attracting an ever-increasing interest for being used in food industry, which promotes a strong demand for quantifying the activity of the enzymes.

Creative Enzymes is capable of providing the most accurate enzymatic assays for alpha-L-rhamnosidases. The test are assured with high reliability by the most advanced spectrophotometric instruments, state-of-the-art technology, and an outstanding expert team. For details, alpha-L-rhamnosidases activities are assayed using p-nitrophenyl α-L-rhamnopyranoside as a substrate, and the formation of p-nitrophenyl wa measured spectrophotometrically at 410 nm. Overall, regardless of the challenges which may lay on your way to enzyme applications, Creative Enzymes will always meet the requirements for the next development stage and will be your best choice with satisfying services.

Figure: The crystal structure of Streptomyces avermitilis alpha-L-rhamnosidase.
PDB: 3W5M